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Histone-lysine N-methyltransferase, H3 lysine-36 specific

Intramolecular
Cysteine 1818 and cysteine 1829 L
Cysteine 1911 and cysteine 1920
Cysteine 1793 and cysteine 1818
Cysteine 1793 and cysteine 1823
Cysteine 2072 and cysteine 2077
Cysteine 2070 and cysteine 2072
Cysteine 2062 and cysteine 2081 L
Cysteine 2062 and cysteine 2065 L
Cysteine 1895 and cysteine 1897
Cysteine 2019 and cysteine 2044
More...
Cysteine 2019 and cysteine 2022
Cysteine 2023 and cysteine 2072 L
Cysteine 2070 and cysteine 2077
Cysteine 1895 and cysteine 1905
Cysteine 1897 and cysteine 1911
Cysteine 2031 and cysteine 2036
Cysteine 1911 and cysteine 1925
Cysteine 2022 and cysteine 2072 L
Cysteine 1905 and cysteine 1925
Cysteine 1803 and cysteine 1809
Cysteine 1921 and cysteine 1968 L
Cysteine 2065 and cysteine 2081 L
Cysteine 1920 and cysteine 1925
Cysteine 2031 and cysteine 2057 L
Cysteine 2073 and cysteine 2100 L
Cysteine 2022 and cysteine 2044
Cysteine 1793 and cysteine 1809
Cysteine 2076 and cysteine 2100 L
Cysteine 1897 and cysteine 1905
Cysteine 1921 and cysteine 1975 L
Cysteine 2073 and cysteine 2076 L
Cysteine 2036 and cysteine 2057 L
Cysteine 1823 and cysteine 1829 L
Cysteine 1895 and cysteine 1931 L
Cysteine 1803 and cysteine 1829 L
Cysteine 1897 and cysteine 1925
Cysteine 1897 and cysteine 1931 L
Cysteine 1905 and cysteine 1920
Cysteine 1809 and cysteine 1829 L
Cysteine 1897 and cysteine 1920
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase, H3 lysine-36 specific between cysteines 1818 and 1829.

Details

Redox score ?
92
PDB code
8fbg
Structure name
crystal structure of nsd1 mutant-y1869c
Structure deposition date
2022-11-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
77
Minimum pKa ?
0
% buried
48
Peptide accession
O88491
Residue number A
1818
Residue number B
1829
Peptide name
Histone-lysine N-methyltransferase, H3 lysine-36 specific

Ligandability

Cysteine 1818 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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 1829 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase, H3 lysine-36 specific between cysteines 1911 and 1920.

Details

Redox score ?
92
PDB code
6kqp
Structure name
nsd1 set domain in complex with sam
Structure deposition date
2019-08-18
Thiol separation (Å)
4
Half-sphere exposure sum ?
72
Minimum pKa ?
3
% buried
48
Peptide accession
Q96L73
Residue number A
1911
Residue number B
1920
Peptide name
Histone-lysine N-methyltransferase, H3 lysine-36 specific

Ligandability

Cysteine 1911 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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 1920 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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, H3 lysine-36 specific between cysteines 1793 and 1818.

Details

Redox score ?
92
PDB code
8fbg
Structure name
crystal structure of nsd1 mutant-y1869c
Structure deposition date
2022-11-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
72
Minimum pKa ?
0
% buried
38
Peptide accession
O88491
Residue number A
1793
Residue number B
1818
Peptide name
Histone-lysine N-methyltransferase, H3 lysine-36 specific

Ligandability

Cysteine 1793 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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 1818 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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, H3 lysine-36 specific between cysteines 1793 and 1823.

Details

Redox score ?
90
PDB code
8fbg
Structure name
crystal structure of nsd1 mutant-y1869c
Structure deposition date
2022-11-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
5
% buried
28
Peptide accession
O88491
Residue number A
1793
Residue number B
1823
Peptide name
Histone-lysine N-methyltransferase, H3 lysine-36 specific

Ligandability

Cysteine 1793 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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 1823 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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, H3 lysine-36 specific between cysteines 2072 and 2077.

Details

Redox score ?
90
PDB code
6kqp
Structure name
nsd1 set domain in complex with sam
Structure deposition date
2019-08-18
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
6
% buried
8
Peptide accession
Q96L73
Residue number A
2072
Residue number B
2077
Peptide name
Histone-lysine N-methyltransferase, H3 lysine-36 specific

Ligandability

Cysteine 2072 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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 2077 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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, H3 lysine-36 specific between cysteines 2070 and 2072.

Details

Redox score ?
87
PDB code
6kqp
Structure name
nsd1 set domain in complex with sam
Structure deposition date
2019-08-18
Thiol separation (Å)
4
Half-sphere exposure sum ?
62
Minimum pKa ?
6
% buried
24
Peptide accession
Q96L73
Residue number A
2070
Residue number B
2072
Peptide name
Histone-lysine N-methyltransferase, H3 lysine-36 specific

Ligandability

Cysteine 2070 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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 2072 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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, H3 lysine-36 specific between cysteines 2062 and 2081 (52 and 71 respectively in this structure).

Details

Redox score ?
87
PDB code
2naa
Structure name
nsd1-phd_5-c5hch tandem domain structure
Structure deposition date
2015-12-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
5
% buried
0
Peptide accession
O88491
Residue number A
2062
Residue number B
2081
Peptide name
Histone-lysine N-methyltransferase, H3 lysine-36 specific

Ligandability

Cysteine 2062 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 2081 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase, H3 lysine-36 specific between cysteines 2062 and 2065 (52 and 55 respectively in this structure).

Details

Redox score ?
86
PDB code
2naa
Structure name
nsd1-phd_5-c5hch tandem domain structure
Structure deposition date
2015-12-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
46
Minimum pKa ?
5
% buried
0
Peptide accession
O88491
Residue number A
2062
Residue number B
2065
Peptide name
Histone-lysine N-methyltransferase, H3 lysine-36 specific

Ligandability

Cysteine 2062 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 2065 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase, H3 lysine-36 specific between cysteines 1895 and 1897.

Details

Redox score ?
86
PDB code
6kqp
Structure name
nsd1 set domain in complex with sam
Structure deposition date
2019-08-18
Thiol separation (Å)
3
Half-sphere exposure sum ?
61
Minimum pKa ?
7
% buried
21
Peptide accession
Q96L73
Residue number A
1895
Residue number B
1897
Peptide name
Histone-lysine N-methyltransferase, H3 lysine-36 specific

Ligandability

Cysteine 1895 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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 1897 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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, H3 lysine-36 specific between cysteines 2019 and 2044 (9 and 34 respectively in this structure).

Details

Redox score ?
85
PDB code
2naa
Structure name
nsd1-phd_5-c5hch tandem domain structure
Structure deposition date
2015-12-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
6
% buried
10
Peptide accession
O88491
Residue number A
2019
Residue number B
2044
Peptide name
Histone-lysine N-methyltransferase, H3 lysine-36 specific

Ligandability

Cysteine 2019 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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 2044 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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, H3 lysine-36 specific between cysteines 2019 and 2022 (9 and 12 respectively in this structure).

Details

Redox score ?
84
PDB code
2naa
Structure name
nsd1-phd_5-c5hch tandem domain structure
Structure deposition date
2015-12-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
52
Minimum pKa ?
6
% buried
6
Peptide accession
O88491
Residue number A
2019
Residue number B
2022
Peptide name
Histone-lysine N-methyltransferase, H3 lysine-36 specific

Ligandability

Cysteine 2019 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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 2022 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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, H3 lysine-36 specific between cysteines 2023 and 2072 (172 and 221 respectively in this structure).

Details

Redox score ?
84
PDB code
3ooi
Structure name
crystal structure of human histone-lysine n-methyltransferase nsd1 set domain in complex with s-adenosyl-l-methionine
Structure deposition date
2010-08-31
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
6
% buried
15
Peptide accession
Q96L73
Residue number A
2023
Residue number B
2072
Peptide name
Histone-lysine N-methyltransferase, H3 lysine-36 specific

Ligandability

Cysteine 2023 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 2072 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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, H3 lysine-36 specific between cysteines 2070 and 2077 (219 and 226 respectively in this structure).

Details

Redox score ?
84
PDB code
3ooi
Structure name
crystal structure of human histone-lysine n-methyltransferase nsd1 set domain in complex with s-adenosyl-l-methionine
Structure deposition date
2010-08-31
Thiol separation (Å)
4
Half-sphere exposure sum ?
47
Minimum pKa ?
9
% buried
16
Peptide accession
Q96L73
Residue number A
2070
Residue number B
2077
Peptide name
Histone-lysine N-methyltransferase, H3 lysine-36 specific

Ligandability

Cysteine 2070 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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 2077 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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, H3 lysine-36 specific between cysteines 1895 and 1905.

Details

Redox score ?
83
PDB code
6kqp
Structure name
nsd1 set domain in complex with sam
Structure deposition date
2019-08-18
Thiol separation (Å)
4
Half-sphere exposure sum ?
70
Minimum pKa ?
7
% buried
32
Peptide accession
Q96L73
Residue number A
1895
Residue number B
1905
Peptide name
Histone-lysine N-methyltransferase, H3 lysine-36 specific

Ligandability

Cysteine 1895 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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 1905 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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, H3 lysine-36 specific between cysteines 1897 and 1911.

Details

Redox score ?
83
PDB code
6kqq
Structure name
nsd1 set domain in complex with bt3 and sam
Structure deposition date
2019-08-18
Thiol separation (Å)
4
Half-sphere exposure sum ?
59
Minimum pKa ?
8
% buried
24
Peptide accession
Q96L73
Residue number A
1897
Residue number B
1911
Peptide name
Histone-lysine N-methyltransferase, H3 lysine-36 specific

Ligandability

Cysteine 1897 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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 1911 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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, H3 lysine-36 specific between cysteines 2031 and 2036 (21 and 26 respectively in this structure).

Details

Redox score ?
82
PDB code
2naa
Structure name
nsd1-phd_5-c5hch tandem domain structure
Structure deposition date
2015-12-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
56
Minimum pKa ?
7
% buried
34
Peptide accession
O88491
Residue number A
2031
Residue number B
2036
Peptide name
Histone-lysine N-methyltransferase, H3 lysine-36 specific

Ligandability

Cysteine 2031 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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 2036 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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, H3 lysine-36 specific between cysteines 1911 and 1925.

Details

Redox score ?
82
PDB code
6kqp
Structure name
nsd1 set domain in complex with sam
Structure deposition date
2019-08-18
Thiol separation (Å)
6
Half-sphere exposure sum ?
61
Minimum pKa ?
3
% buried
38
Peptide accession
Q96L73
Residue number A
1911
Residue number B
1925
Peptide name
Histone-lysine N-methyltransferase, H3 lysine-36 specific

Ligandability

Cysteine 1911 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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 1925 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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, H3 lysine-36 specific between cysteines 2022 and 2072.

Details

Redox score ?
81
PDB code
6kqq
Structure name
nsd1 set domain in complex with bt3 and sam
Structure deposition date
2019-08-18
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
6
% buried
32
Peptide accession
Q96L73
Residue number A
2022
Residue number B
2072
Peptide name
Histone-lysine N-methyltransferase, H3 lysine-36 specific

Ligandability

Cysteine 2022 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 2072 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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, H3 lysine-36 specific between cysteines 1905 and 1925.

Details

Redox score ?
81
PDB code
6kqp
Structure name
nsd1 set domain in complex with sam
Structure deposition date
2019-08-18
Thiol separation (Å)
3
Half-sphere exposure sum ?
68
Minimum pKa ?
9
% buried
34
Peptide accession
Q96L73
Residue number A
1905
Residue number B
1925
Peptide name
Histone-lysine N-methyltransferase, H3 lysine-36 specific

Ligandability

Cysteine 1905 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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 1925 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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, H3 lysine-36 specific between cysteines 1803 and 1809.

Details

Redox score ?
81
PDB code
8fbg
Structure name
crystal structure of nsd1 mutant-y1869c
Structure deposition date
2022-11-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
68
Minimum pKa ?
8
% buried
35
Peptide accession
O88491
Residue number A
1803
Residue number B
1809
Peptide name
Histone-lysine N-methyltransferase, H3 lysine-36 specific

Ligandability

Cysteine 1803 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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 1809 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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, H3 lysine-36 specific between cysteines 1921 and 1968.

Details

Redox score ?
81
PDB code
8fbg
Structure name
crystal structure of nsd1 mutant-y1869c
Structure deposition date
2022-11-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
53
Minimum pKa ?
8
% buried
19
Peptide accession
O88491
Residue number A
1921
Residue number B
1968
Peptide name
Histone-lysine N-methyltransferase, H3 lysine-36 specific

Ligandability

Cysteine 1921 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 1968 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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, H3 lysine-36 specific between cysteines 2065 and 2081 (55 and 71 respectively in this structure).

Details

Redox score ?
80
PDB code
2naa
Structure name
nsd1-phd_5-c5hch tandem domain structure
Structure deposition date
2015-12-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
45
Minimum pKa ?
8
% buried
0
Peptide accession
O88491
Residue number A
2065
Residue number B
2081
Peptide name
Histone-lysine N-methyltransferase, H3 lysine-36 specific

Ligandability

Cysteine 2065 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 2081 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase, H3 lysine-36 specific between cysteines 1920 and 1925.

Details

Redox score ?
80
PDB code
6kqp
Structure name
nsd1 set domain in complex with sam
Structure deposition date
2019-08-18
Thiol separation (Å)
3
Half-sphere exposure sum ?
71
Minimum pKa ?
9
% buried
42
Peptide accession
Q96L73
Residue number A
1920
Residue number B
1925
Peptide name
Histone-lysine N-methyltransferase, H3 lysine-36 specific

Ligandability

Cysteine 1920 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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 1925 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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, H3 lysine-36 specific between cysteines 2031 and 2057 (21 and 47 respectively in this structure).

Details

Redox score ?
79
PDB code
2naa
Structure name
nsd1-phd_5-c5hch tandem domain structure
Structure deposition date
2015-12-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
73
Minimum pKa ?
7
% buried
44
Peptide accession
O88491
Residue number A
2031
Residue number B
2057
Peptide name
Histone-lysine N-methyltransferase, H3 lysine-36 specific

Ligandability

Cysteine 2031 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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 2057 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase, H3 lysine-36 specific between cysteines 2073 and 2100 (63 and 90 respectively in this structure).

Details

Redox score ?
79
PDB code
2naa
Structure name
nsd1-phd_5-c5hch tandem domain structure
Structure deposition date
2015-12-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
9
% buried
26
Peptide accession
O88491
Residue number A
2073
Residue number B
2100
Peptide name
Histone-lysine N-methyltransferase, H3 lysine-36 specific

Ligandability

Cysteine 2073 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 2100 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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, H3 lysine-36 specific between cysteines 2022 and 2044 (12 and 34 respectively in this structure).

Details

Redox score ?
78
PDB code
2naa
Structure name
nsd1-phd_5-c5hch tandem domain structure
Structure deposition date
2015-12-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
46
Minimum pKa ?
9
% buried
4
Peptide accession
O88491
Residue number A
2022
Residue number B
2044
Peptide name
Histone-lysine N-methyltransferase, H3 lysine-36 specific

Ligandability

Cysteine 2022 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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 2044 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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, H3 lysine-36 specific between cysteines 1793 and 1809.

Details

Redox score ?
78
PDB code
8fbh
Structure name
crystal structure of nsd1 mutant-t1927a
Structure deposition date
2022-11-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
O88491
Residue number A
1793
Residue number B
1809
Peptide name
Histone-lysine N-methyltransferase, H3 lysine-36 specific

Ligandability

Cysteine 1793 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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 1809 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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, H3 lysine-36 specific between cysteines 2076 and 2100 (66 and 90 respectively in this structure).

Details

Redox score ?
78
PDB code
2naa
Structure name
nsd1-phd_5-c5hch tandem domain structure
Structure deposition date
2015-12-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
61
Minimum pKa ?
8
% buried
29
Peptide accession
O88491
Residue number A
2076
Residue number B
2100
Peptide name
Histone-lysine N-methyltransferase, H3 lysine-36 specific

Ligandability

Cysteine 2076 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 2100 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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, H3 lysine-36 specific between cysteines 1897 and 1905.

Details

Redox score ?
77
PDB code
6kqq
Structure name
nsd1 set domain in complex with bt3 and sam
Structure deposition date
2019-08-18
Thiol separation (Å)
4
Half-sphere exposure sum ?
66
Minimum pKa ?
10
% buried
20
Peptide accession
Q96L73
Residue number A
1897
Residue number B
1905
Peptide name
Histone-lysine N-methyltransferase, H3 lysine-36 specific

Ligandability

Cysteine 1897 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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 1905 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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, H3 lysine-36 specific between cysteines 1921 and 1975.

Details

Redox score ?
77
PDB code
8fbh
Structure name
crystal structure of nsd1 mutant-t1927a
Structure deposition date
2022-11-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
47
Minimum pKa ?
nan
% buried
nan
Peptide accession
O88491
Residue number A
1921
Residue number B
1975
Peptide name
Histone-lysine N-methyltransferase, H3 lysine-36 specific

Ligandability

Cysteine 1921 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 1975 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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, H3 lysine-36 specific between cysteines 2073 and 2076 (63 and 66 respectively in this structure).

Details

Redox score ?
76
PDB code
2naa
Structure name
nsd1-phd_5-c5hch tandem domain structure
Structure deposition date
2015-12-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
68
Minimum pKa ?
8
% buried
35
Peptide accession
O88491
Residue number A
2073
Residue number B
2076
Peptide name
Histone-lysine N-methyltransferase, H3 lysine-36 specific

Ligandability

Cysteine 2073 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 2076 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase, H3 lysine-36 specific between cysteines 2036 and 2057 (26 and 47 respectively in this structure).

Details

Redox score ?
76
PDB code
2naa
Structure name
nsd1-phd_5-c5hch tandem domain structure
Structure deposition date
2015-12-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
65
Minimum pKa ?
9
% buried
46
Peptide accession
O88491
Residue number A
2036
Residue number B
2057
Peptide name
Histone-lysine N-methyltransferase, H3 lysine-36 specific

Ligandability

Cysteine 2036 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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 2057 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase, H3 lysine-36 specific between cysteines 1823 and 1829.

Details

Redox score ?
76
PDB code
8fbh
Structure name
crystal structure of nsd1 mutant-t1927a
Structure deposition date
2022-11-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
O88491
Residue number A
1823
Residue number B
1829
Peptide name
Histone-lysine N-methyltransferase, H3 lysine-36 specific

Ligandability

Cysteine 1823 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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 1829 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase, H3 lysine-36 specific between cysteines 1895 and 1931.

Details

Redox score ?
74
PDB code
6kqp
Structure name
nsd1 set domain in complex with sam
Structure deposition date
2019-08-18
Thiol separation (Å)
6
Half-sphere exposure sum ?
66
Minimum pKa ?
3
% buried
38
Peptide accession
Q96L73
Residue number A
1895
Residue number B
1931
Peptide name
Histone-lysine N-methyltransferase, H3 lysine-36 specific

Ligandability

Cysteine 1895 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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 1931 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase, H3 lysine-36 specific between cysteines 1803 and 1829.

Details

Redox score ?
71
PDB code
8fbg
Structure name
crystal structure of nsd1 mutant-y1869c
Structure deposition date
2022-11-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
72
Minimum pKa ?
12
% buried
39
Peptide accession
O88491
Residue number A
1803
Residue number B
1829
Peptide name
Histone-lysine N-methyltransferase, H3 lysine-36 specific

Ligandability

Cysteine 1803 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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 1829 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase, H3 lysine-36 specific between cysteines 1897 and 1925.

Details

Redox score ?
68
PDB code
6kqp
Structure name
nsd1 set domain in complex with sam
Structure deposition date
2019-08-18
Thiol separation (Å)
6
Half-sphere exposure sum ?
59
Minimum pKa ?
9
% buried
23
Peptide accession
Q96L73
Residue number A
1897
Residue number B
1925
Peptide name
Histone-lysine N-methyltransferase, H3 lysine-36 specific

Ligandability

Cysteine 1897 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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 1925 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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, H3 lysine-36 specific between cysteines 1897 and 1931.

Details

Redox score ?
67
PDB code
6kqq
Structure name
nsd1 set domain in complex with bt3 and sam
Structure deposition date
2019-08-18
Thiol separation (Å)
8
Half-sphere exposure sum ?
65
Minimum pKa ?
4
% buried
29
Peptide accession
Q96L73
Residue number A
1897
Residue number B
1931
Peptide name
Histone-lysine N-methyltransferase, H3 lysine-36 specific

Ligandability

Cysteine 1897 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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 1931 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase, H3 lysine-36 specific between cysteines 1905 and 1920.

Details

Redox score ?
67
PDB code
6kqp
Structure name
nsd1 set domain in complex with sam
Structure deposition date
2019-08-18
Thiol separation (Å)
3
Half-sphere exposure sum ?
79
Minimum pKa ?
13
% buried
44
Peptide accession
Q96L73
Residue number A
1905
Residue number B
1920
Peptide name
Histone-lysine N-methyltransferase, H3 lysine-36 specific

Ligandability

Cysteine 1905 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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 1920 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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, H3 lysine-36 specific between cysteines 1809 and 1829.

Details

Redox score ?
67
PDB code
8fbg
Structure name
crystal structure of nsd1 mutant-y1869c
Structure deposition date
2022-11-29
Thiol separation (Å)
6
Half-sphere exposure sum ?
64
Minimum pKa ?
8
% buried
43
Peptide accession
O88491
Residue number A
1809
Residue number B
1829
Peptide name
Histone-lysine N-methyltransferase, H3 lysine-36 specific

Ligandability

Cysteine 1809 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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 1829 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase, H3 lysine-36 specific between cysteines 1897 and 1920.

Details

Redox score ?
63
PDB code
6kqp
Structure name
nsd1 set domain in complex with sam
Structure deposition date
2019-08-18
Thiol separation (Å)
6
Half-sphere exposure sum ?
70
Minimum pKa ?
10
% buried
34
Peptide accession
Q96L73
Residue number A
1897
Residue number B
1920
Peptide name
Histone-lysine N-methyltransferase, H3 lysine-36 specific

Ligandability

Cysteine 1897 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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 1920 of Histone-lysine N-methyltransferase, H3 lysine-36 specific

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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