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Histone-lysine N-methyltransferase ASH1L

Intramolecular
Cysteine 2109 and cysteine 2133
Cysteine 2113 and cysteine 2122
Cysteine 2096 and cysteine 2109
Cysteine 2096 and cysteine 2127
Cysteine 2096 and cysteine 2098
Cysteine 2098 and cysteine 2113
Cysteine 2275 and cysteine 2280
Cysteine 2109 and cysteine 2113
Cysteine 2098 and cysteine 2129
Cysteine 2273 and cysteine 2280
More...
Cysteine 2225 and cysteine 2275
Cysteine 2273 and cysteine 2275
Cysteine 2109 and cysteine 2127
Cysteine 2096 and cysteine 2122
Cysteine 2096 and cysteine 2113
Cysteine 2225 and cysteine 2280
Cysteine 2127 and cysteine 2133
Cysteine 2096 and cysteine 2133
Cysteine 2096 and cysteine 2129
Cysteine 2127 and cysteine 2129
Cysteine 2098 and cysteine 2109
Cysteine 2122 and cysteine 2127
Cysteine 2225 and cysteine 2273
Cysteine 2109 and cysteine 2134
Cysteine 2109 and cysteine 2129
Cysteine 2098 and cysteine 2127
Cysteine 2113 and cysteine 2127
Cysteine 2113 and cysteine 2133
Cysteine 2109 and cysteine 2122
Cysteine 2122 and cysteine 2133
Cysteine 2129 and cysteine 2133
Cysteine 2098 and cysteine 2133
Cysteine 2113 and cysteine 2129
Cysteine 2098 and cysteine 2122
Cysteine 2122 and cysteine 2129
Cysteine 2133 and cysteine 2134
Cysteine 2122 and cysteine 2134
Cysteine 2129 and cysteine 2134
Cysteine 2096 and cysteine 2134
Cysteine 2098 and cysteine 2134
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase ASH1L between cysteines 2109 and 2133 (2104 and 2128 respectively in this structure).

Details

Redox score ?
95
PDB code
6ago
Structure name
crystal structure of mrg15-ash1l histone methyltransferase complex
Structure deposition date
2018-08-13
Thiol separation (Å)
4
Half-sphere exposure sum ?
68
Minimum pKa ?
0
% buried
51
Peptide accession
Q9NR48
Residue number A
2109
Residue number B
2133
Peptide name
Histone-lysine N-methyltransferase ASH1L

Ligandability

Cysteine 2109 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 2133 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase ASH1L between cysteines 2113 and 2122 (2108 and 2117 respectively in this structure).

Details

Redox score ?
90
PDB code
6wzw
Structure name
ash1l set domain in complex with as-85
Structure deposition date
2020-05-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
73
Minimum pKa ?
2
% buried
39
Peptide accession
Q9NR48
Residue number A
2113
Residue number B
2122
Peptide name
Histone-lysine N-methyltransferase ASH1L

Ligandability

Cysteine 2113 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 2122 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase ASH1L between cysteines 2096 and 2109 (2091 and 2104 respectively in this structure).

Details

Redox score ?
87
PDB code
6ago
Structure name
crystal structure of mrg15-ash1l histone methyltransferase complex
Structure deposition date
2018-08-13
Thiol separation (Å)
4
Half-sphere exposure sum ?
65
Minimum pKa ?
5
% buried
34
Peptide accession
Q9NR48
Residue number A
2096
Residue number B
2109
Peptide name
Histone-lysine N-methyltransferase ASH1L

Ligandability

Cysteine 2096 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 2109 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase ASH1L between cysteines 2096 and 2127 (2091 and 2122 respectively in this structure).

Details

Redox score ?
86
PDB code
3ope
Structure name
structural basis of auto-inhibitory mechanism of histone methyltransferase
Structure deposition date
2010-08-31
Thiol separation (Å)
3
Half-sphere exposure sum ?
63
Minimum pKa ?
7
% buried
32
Peptide accession
Q9NR48
Residue number A
2096
Residue number B
2127
Peptide name
Histone-lysine N-methyltransferase ASH1L

Ligandability

Cysteine 2096 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 2127 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase ASH1L between cysteines 2096 and 2098 (2091 and 2093 respectively in this structure).

Details

Redox score ?
86
PDB code
6x0p
Structure name
ash1l set domain q2265a mutant in complex with as-5
Structure deposition date
2020-05-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
59
Minimum pKa ?
6
% buried
36
Peptide accession
Q9NR48
Residue number A
2096
Residue number B
2098
Peptide name
Histone-lysine N-methyltransferase ASH1L

Ligandability

Cysteine 2096 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 2098 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase ASH1L between cysteines 2098 and 2113 (2093 and 2108 respectively in this structure).

Details

Redox score ?
86
PDB code
6ago
Structure name
crystal structure of mrg15-ash1l histone methyltransferase complex
Structure deposition date
2018-08-13
Thiol separation (Å)
3
Half-sphere exposure sum ?
54
Minimum pKa ?
8
% buried
16
Peptide accession
Q9NR48
Residue number A
2098
Residue number B
2113
Peptide name
Histone-lysine N-methyltransferase ASH1L

Ligandability

Cysteine 2098 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 2113 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase ASH1L between cysteines 2275 and 2280 (2270 and 2275 respectively in this structure).

Details

Redox score ?
85
PDB code
6wzw
Structure name
ash1l set domain in complex with as-85
Structure deposition date
2020-05-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
6
% buried
24
Peptide accession
Q9NR48
Residue number A
2275
Residue number B
2280
Peptide name
Histone-lysine N-methyltransferase ASH1L

Ligandability

Cysteine 2275 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 2280 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase ASH1L between cysteines 2109 and 2113 (2104 and 2108 respectively in this structure).

Details

Redox score ?
84
PDB code
6x0p
Structure name
ash1l set domain q2265a mutant in complex with as-5
Structure deposition date
2020-05-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
64
Minimum pKa ?
7
% buried
34
Peptide accession
Q9NR48
Residue number A
2109
Residue number B
2113
Peptide name
Histone-lysine N-methyltransferase ASH1L

Ligandability

Cysteine 2109 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 2113 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase ASH1L between cysteines 2098 and 2129 (2093 and 2124 respectively in this structure).

Details

Redox score ?
84
PDB code
6ago
Structure name
crystal structure of mrg15-ash1l histone methyltransferase complex
Structure deposition date
2018-08-13
Thiol separation (Å)
3
Half-sphere exposure sum ?
55
Minimum pKa ?
8
% buried
16
Peptide accession
Q9NR48
Residue number A
2098
Residue number B
2129
Peptide name
Histone-lysine N-methyltransferase ASH1L

Ligandability

Cysteine 2098 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 2129 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase ASH1L between cysteines 2273 and 2280 (2268 and 2275 respectively in this structure).

Details

Redox score ?
84
PDB code
3ope
Structure name
structural basis of auto-inhibitory mechanism of histone methyltransferase
Structure deposition date
2010-08-31
Thiol separation (Å)
4
Half-sphere exposure sum ?
43
Minimum pKa ?
8
% buried
18
Peptide accession
Q9NR48
Residue number A
2273
Residue number B
2280
Peptide name
Histone-lysine N-methyltransferase ASH1L

Ligandability

Cysteine 2273 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 2280 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase ASH1L between cysteines 2225 and 2275 (2220 and 2270 respectively in this structure).

Details

Redox score ?
84
PDB code
6ago
Structure name
crystal structure of mrg15-ash1l histone methyltransferase complex
Structure deposition date
2018-08-13
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
6
% buried
9
Peptide accession
Q9NR48
Residue number A
2225
Residue number B
2275
Peptide name
Histone-lysine N-methyltransferase ASH1L

Ligandability

Cysteine 2225 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 2275 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase ASH1L between cysteines 2273 and 2275 (2268 and 2270 respectively in this structure).

Details

Redox score ?
84
PDB code
6x0p
Structure name
ash1l set domain q2265a mutant in complex with as-5
Structure deposition date
2020-05-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
60
Minimum pKa ?
6
% buried
41
Peptide accession
Q9NR48
Residue number A
2273
Residue number B
2275
Peptide name
Histone-lysine N-methyltransferase ASH1L

Ligandability

Cysteine 2273 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 2275 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase ASH1L between cysteines 2109 and 2127 (2104 and 2122 respectively in this structure).

Details

Redox score ?
83
PDB code
6x0p
Structure name
ash1l set domain q2265a mutant in complex with as-5
Structure deposition date
2020-05-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
66
Minimum pKa ?
8
% buried
36
Peptide accession
Q9NR48
Residue number A
2109
Residue number B
2127
Peptide name
Histone-lysine N-methyltransferase ASH1L

Ligandability

Cysteine 2109 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 2127 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase ASH1L between cysteines 2096 and 2122 (2091 and 2117 respectively in this structure).

Details

Redox score ?
82
PDB code
3ope
Structure name
structural basis of auto-inhibitory mechanism of histone methyltransferase
Structure deposition date
2010-08-31
Thiol separation (Å)
3
Half-sphere exposure sum ?
76
Minimum pKa ?
7
% buried
44
Peptide accession
Q9NR48
Residue number A
2096
Residue number B
2122
Peptide name
Histone-lysine N-methyltransferase ASH1L

Ligandability

Cysteine 2096 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 2122 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase ASH1L between cysteines 2096 and 2113 (2091 and 2108 respectively in this structure).

Details

Redox score ?
82
PDB code
6x0p
Structure name
ash1l set domain q2265a mutant in complex with as-5
Structure deposition date
2020-05-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
66
Minimum pKa ?
6
% buried
48
Peptide accession
Q9NR48
Residue number A
2096
Residue number B
2113
Peptide name
Histone-lysine N-methyltransferase ASH1L

Ligandability

Cysteine 2096 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 2113 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase ASH1L between cysteines 2225 and 2280 (2220 and 2275 respectively in this structure).

Details

Redox score ?
82
PDB code
6ago
Structure name
crystal structure of mrg15-ash1l histone methyltransferase complex
Structure deposition date
2018-08-13
Thiol separation (Å)
4
Half-sphere exposure sum ?
45
Minimum pKa ?
8
% buried
3
Peptide accession
Q9NR48
Residue number A
2225
Residue number B
2280
Peptide name
Histone-lysine N-methyltransferase ASH1L

Ligandability

Cysteine 2225 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 2280 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase ASH1L between cysteines 2127 and 2133 (2122 and 2128 respectively in this structure).

Details

Redox score ?
81
PDB code
6x0p
Structure name
ash1l set domain q2265a mutant in complex with as-5
Structure deposition date
2020-05-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
67
Minimum pKa ?
8
% buried
44
Peptide accession
Q9NR48
Residue number A
2127
Residue number B
2133
Peptide name
Histone-lysine N-methyltransferase ASH1L

Ligandability

Cysteine 2127 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 2133 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase ASH1L between cysteines 2096 and 2133 (2091 and 2128 respectively in this structure).

Details

Redox score ?
80
PDB code
6ago
Structure name
crystal structure of mrg15-ash1l histone methyltransferase complex
Structure deposition date
2018-08-13
Thiol separation (Å)
6
Half-sphere exposure sum ?
68
Minimum pKa ?
1
% buried
43
Peptide accession
Q9NR48
Residue number A
2096
Residue number B
2133
Peptide name
Histone-lysine N-methyltransferase ASH1L

Ligandability

Cysteine 2096 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 2133 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase ASH1L between cysteines 2096 and 2129 (2091 and 2124 respectively in this structure).

Details

Redox score ?
79
PDB code
6ago
Structure name
crystal structure of mrg15-ash1l histone methyltransferase complex
Structure deposition date
2018-08-13
Thiol separation (Å)
5
Half-sphere exposure sum ?
64
Minimum pKa ?
5
% buried
22
Peptide accession
Q9NR48
Residue number A
2096
Residue number B
2129
Peptide name
Histone-lysine N-methyltransferase ASH1L

Ligandability

Cysteine 2096 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 2129 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase ASH1L between cysteines 2127 and 2129 (2122 and 2124 respectively in this structure).

Details

Redox score ?
78
PDB code
6x0p
Structure name
ash1l set domain q2265a mutant in complex with as-5
Structure deposition date
2020-05-17
Thiol separation (Å)
5
Half-sphere exposure sum ?
61
Minimum pKa ?
8
% buried
26
Peptide accession
Q9NR48
Residue number A
2127
Residue number B
2129
Peptide name
Histone-lysine N-methyltransferase ASH1L

Ligandability

Cysteine 2127 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 2129 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase ASH1L between cysteines 2098 and 2109 (2093 and 2104 respectively in this structure).

Details

Redox score ?
76
PDB code
6x0p
Structure name
ash1l set domain q2265a mutant in complex with as-5
Structure deposition date
2020-05-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
61
Minimum pKa ?
10
% buried
24
Peptide accession
Q9NR48
Residue number A
2098
Residue number B
2109
Peptide name
Histone-lysine N-methyltransferase ASH1L

Ligandability

Cysteine 2098 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 2109 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase ASH1L between cysteines 2122 and 2127 (2117 and 2122 respectively in this structure).

Details

Redox score ?
76
PDB code
3ope
Structure name
structural basis of auto-inhibitory mechanism of histone methyltransferase
Structure deposition date
2010-08-31
Thiol separation (Å)
4
Half-sphere exposure sum ?
52
Minimum pKa ?
9
% buried
nan
Peptide accession
Q9NR48
Residue number A
2122
Residue number B
2127
Peptide name
Histone-lysine N-methyltransferase ASH1L

Ligandability

Cysteine 2122 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 2127 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase ASH1L between cysteines 2225 and 2273 (2220 and 2268 respectively in this structure).

Details

Redox score ?
75
PDB code
6wzw
Structure name
ash1l set domain in complex with as-85
Structure deposition date
2020-05-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
59
Minimum pKa ?
10
% buried
43
Peptide accession
Q9NR48
Residue number A
2225
Residue number B
2273
Peptide name
Histone-lysine N-methyltransferase ASH1L

Ligandability

Cysteine 2225 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 2273 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase ASH1L between cysteines 2109 and 2134 (2104 and 2129 respectively in this structure).

Details

Redox score ?
75
PDB code
3ope
Structure name
structural basis of auto-inhibitory mechanism of histone methyltransferase
Structure deposition date
2010-08-31
Thiol separation (Å)
5
Half-sphere exposure sum ?
nan
Minimum pKa ?
8
% buried
1
Peptide accession
Q9NR48
Residue number A
2109
Residue number B
2134
Peptide name
Histone-lysine N-methyltransferase ASH1L

Ligandability

Cysteine 2109 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 2134 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase ASH1L between cysteines 2109 and 2129 (2104 and 2124 respectively in this structure).

Details

Redox score ?
73
PDB code
6ago
Structure name
crystal structure of mrg15-ash1l histone methyltransferase complex
Structure deposition date
2018-08-13
Thiol separation (Å)
4
Half-sphere exposure sum ?
61
Minimum pKa ?
10
% buried
30
Peptide accession
Q9NR48
Residue number A
2109
Residue number B
2129
Peptide name
Histone-lysine N-methyltransferase ASH1L

Ligandability

Cysteine 2109 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 2129 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase ASH1L between cysteines 2098 and 2127 (2093 and 2122 respectively in this structure).

Details

Redox score ?
70
PDB code
6ago
Structure name
crystal structure of mrg15-ash1l histone methyltransferase complex
Structure deposition date
2018-08-13
Thiol separation (Å)
6
Half-sphere exposure sum ?
58
Minimum pKa ?
8
% buried
28
Peptide accession
Q9NR48
Residue number A
2098
Residue number B
2127
Peptide name
Histone-lysine N-methyltransferase ASH1L

Ligandability

Cysteine 2098 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 2127 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase ASH1L between cysteines 2113 and 2127 (2108 and 2122 respectively in this structure).

Details

Redox score ?
69
PDB code
3ope
Structure name
structural basis of auto-inhibitory mechanism of histone methyltransferase
Structure deposition date
2010-08-31
Thiol separation (Å)
7
Half-sphere exposure sum ?
38
Minimum pKa ?
6
% buried
nan
Peptide accession
Q9NR48
Residue number A
2113
Residue number B
2127
Peptide name
Histone-lysine N-methyltransferase ASH1L

Ligandability

Cysteine 2113 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 2127 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase ASH1L between cysteines 2113 and 2133 (2108 and 2128 respectively in this structure).

Details

Redox score ?
68
PDB code
3ope
Structure name
structural basis of auto-inhibitory mechanism of histone methyltransferase
Structure deposition date
2010-08-31
Thiol separation (Å)
7
Half-sphere exposure sum ?
43
Minimum pKa ?
6
% buried
nan
Peptide accession
Q9NR48
Residue number A
2113
Residue number B
2133
Peptide name
Histone-lysine N-methyltransferase ASH1L

Ligandability

Cysteine 2113 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 2133 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase ASH1L between cysteines 2109 and 2122 (2104 and 2117 respectively in this structure).

Details

Redox score ?
65
PDB code
6x0p
Structure name
ash1l set domain q2265a mutant in complex with as-5
Structure deposition date
2020-05-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
78
Minimum pKa ?
13
% buried
nan
Peptide accession
Q9NR48
Residue number A
2109
Residue number B
2122
Peptide name
Histone-lysine N-methyltransferase ASH1L

Ligandability

Cysteine 2109 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 2122 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase ASH1L between cysteines 2122 and 2133 (2117 and 2128 respectively in this structure).

Details

Redox score ?
65
PDB code
6x0p
Structure name
ash1l set domain q2265a mutant in complex with as-5
Structure deposition date
2020-05-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
76
Minimum pKa ?
13
% buried
nan
Peptide accession
Q9NR48
Residue number A
2122
Residue number B
2133
Peptide name
Histone-lysine N-methyltransferase ASH1L

Ligandability

Cysteine 2122 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 2133 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase ASH1L between cysteines 2129 and 2133 (2124 and 2128 respectively in this structure).

Details

Redox score ?
64
PDB code
6x0p
Structure name
ash1l set domain q2265a mutant in complex with as-5
Structure deposition date
2020-05-17
Thiol separation (Å)
6
Half-sphere exposure sum ?
66
Minimum pKa ?
9
% buried
33
Peptide accession
Q9NR48
Residue number A
2129
Residue number B
2133
Peptide name
Histone-lysine N-methyltransferase ASH1L

Ligandability

Cysteine 2129 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 2133 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase ASH1L between cysteines 2098 and 2133 (2093 and 2128 respectively in this structure).

Details

Redox score ?
62
PDB code
3ope
Structure name
structural basis of auto-inhibitory mechanism of histone methyltransferase
Structure deposition date
2010-08-31
Thiol separation (Å)
6
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NR48
Residue number A
2098
Residue number B
2133
Peptide name
Histone-lysine N-methyltransferase ASH1L

Ligandability

Cysteine 2098 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 2133 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase ASH1L between cysteines 2113 and 2129 (2108 and 2124 respectively in this structure).

Details

Redox score ?
61
PDB code
3ope
Structure name
structural basis of auto-inhibitory mechanism of histone methyltransferase
Structure deposition date
2010-08-31
Thiol separation (Å)
8
Half-sphere exposure sum ?
35
Minimum pKa ?
6
% buried
0
Peptide accession
Q9NR48
Residue number A
2113
Residue number B
2129
Peptide name
Histone-lysine N-methyltransferase ASH1L

Ligandability

Cysteine 2113 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 2129 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase ASH1L between cysteines 2098 and 2122 (2093 and 2117 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
59
PDB code
6x0p
Structure name
ash1l set domain q2265a mutant in complex with as-5
Structure deposition date
2020-05-17
Thiol separation (Å)
6
Half-sphere exposure sum ?
72
Minimum pKa ?
9
% buried
nan
Peptide accession
Q9NR48
Residue number A
2098
Residue number B
2122
Peptide name
Histone-lysine N-methyltransferase ASH1L

Ligandability

Cysteine 2098 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 2122 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase ASH1L between cysteines 2122 and 2129 (2117 and 2124 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
57
PDB code
6ago
Structure name
crystal structure of mrg15-ash1l histone methyltransferase complex
Structure deposition date
2018-08-13
Thiol separation (Å)
7
Half-sphere exposure sum ?
75
Minimum pKa ?
7
% buried
38
Peptide accession
Q9NR48
Residue number A
2122
Residue number B
2129
Peptide name
Histone-lysine N-methyltransferase ASH1L

Ligandability

Cysteine 2122 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 2129 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase ASH1L between cysteines 2133 and 2134 (2128 and 2129 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
56
PDB code
3ope
Structure name
structural basis of auto-inhibitory mechanism of histone methyltransferase
Structure deposition date
2010-08-31
Thiol separation (Å)
5
Half-sphere exposure sum ?
73
Minimum pKa ?
13
% buried
nan
Peptide accession
Q9NR48
Residue number A
2133
Residue number B
2134
Peptide name
Histone-lysine N-methyltransferase ASH1L

Ligandability

Cysteine 2133 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 2134 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase ASH1L between cysteines 2122 and 2134 (2117 and 2129 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
55
PDB code
6wzw
Structure name
ash1l set domain in complex with as-85
Structure deposition date
2020-05-14
Thiol separation (Å)
9
Half-sphere exposure sum ?
78
Minimum pKa ?
2
% buried
45
Peptide accession
Q9NR48
Residue number A
2122
Residue number B
2134
Peptide name
Histone-lysine N-methyltransferase ASH1L

Ligandability

Cysteine 2122 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 2134 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase ASH1L between cysteines 2129 and 2134 (2124 and 2129 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
6wzw
Structure name
ash1l set domain in complex with as-85
Structure deposition date
2020-05-14
Thiol separation (Å)
8
Half-sphere exposure sum ?
66
Minimum pKa ?
9
% buried
30
Peptide accession
Q9NR48
Residue number A
2129
Residue number B
2134
Peptide name
Histone-lysine N-methyltransferase ASH1L

Ligandability

Cysteine 2129 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 2134 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase ASH1L between cysteines 2096 and 2134 (2091 and 2129 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
3ope
Structure name
structural basis of auto-inhibitory mechanism of histone methyltransferase
Structure deposition date
2010-08-31
Thiol separation (Å)
9
Half-sphere exposure sum ?
69
Minimum pKa ?
7
% buried
40
Peptide accession
Q9NR48
Residue number A
2096
Residue number B
2134
Peptide name
Histone-lysine N-methyltransferase ASH1L

Ligandability

Cysteine 2096 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 2134 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase ASH1L between cysteines 2098 and 2134 (2093 and 2129 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
6wzw
Structure name
ash1l set domain in complex with as-85
Structure deposition date
2020-05-14
Thiol separation (Å)
9
Half-sphere exposure sum ?
62
Minimum pKa ?
9
% buried
30
Peptide accession
Q9NR48
Residue number A
2098
Residue number B
2134
Peptide name
Histone-lysine N-methyltransferase ASH1L

Ligandability

Cysteine 2098 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 2134 of Histone-lysine N-methyltransferase ASH1L

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

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