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Histone-lysine N-methyltransferase 2B

Intramolecular
Cysteine 2705 and cysteine 2710
Cysteine 2655 and cysteine 2710
Cysteine 2703 and cysteine 2705
Cysteine 2703 and cysteine 2710
Cysteine 2655 and cysteine 2705
Cysteine 972 and cysteine 1005
Cysteine 969 and cysteine 972
Cysteine 966 and cysteine 969
Cysteine 978 and cysteine 981
Cysteine 978 and cysteine 1000
More...
Cysteine 984 and cysteine 1000
Cysteine 981 and cysteine 984
Cysteine 966 and cysteine 1005
Cysteine 969 and cysteine 1005
Cysteine 981 and cysteine 1000
Cysteine 966 and cysteine 972
Cysteine 2655 and cysteine 2703
Cysteine 978 and cysteine 984
Cysteine 999 and cysteine 1000 L
Cysteine 981 and cysteine 999 L
Cysteine 999 and cysteine 1005 L
Cysteine 2591 and cysteine 2659
Cysteine 972 and cysteine 999 L
Cysteine 984 and cysteine 999 L
Cysteine 969 and cysteine 999 L
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase 2B between cysteines 2705 and 2710.

Details

Redox score ?
92
PDB code
7bre
Structure name
the crystal structure of mll2 in complex with ash2l and rbbp5
Structure deposition date
2020-03-28
Thiol separation (Å)
3
Half-sphere exposure sum ?
49
Minimum pKa ?
5
% buried
16
Peptide accession
Q9UMN6
Residue number A
2705
Residue number B
2710
Peptide name
Histone-lysine N-methyltransferase 2B

Ligandability

Cysteine 2705 of Histone-lysine N-methyltransferase 2B

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 2710 of Histone-lysine N-methyltransferase 2B

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 2B between cysteines 2655 and 2710.

Details

Redox score ?
90
PDB code
7bre
Structure name
the crystal structure of mll2 in complex with ash2l and rbbp5
Structure deposition date
2020-03-28
Thiol separation (Å)
3
Half-sphere exposure sum ?
47
Minimum pKa ?
6
% buried
16
Peptide accession
Q9UMN6
Residue number A
2655
Residue number B
2710
Peptide name
Histone-lysine N-methyltransferase 2B

Ligandability

Cysteine 2655 of Histone-lysine N-methyltransferase 2B

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 2710 of Histone-lysine N-methyltransferase 2B

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 2B between cysteines 2703 and 2705.

Details

Redox score ?
90
PDB code
7bre
Structure name
the crystal structure of mll2 in complex with ash2l and rbbp5
Structure deposition date
2020-03-28
Thiol separation (Å)
3
Half-sphere exposure sum ?
56
Minimum pKa ?
5
% buried
30
Peptide accession
Q9UMN6
Residue number A
2703
Residue number B
2705
Peptide name
Histone-lysine N-methyltransferase 2B

Ligandability

Cysteine 2703 of Histone-lysine N-methyltransferase 2B

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 2705 of Histone-lysine N-methyltransferase 2B

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 2B between cysteines 2703 and 2710.

Details

Redox score ?
84
PDB code
7bre
Structure name
the crystal structure of mll2 in complex with ash2l and rbbp5
Structure deposition date
2020-03-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
45
Minimum pKa ?
8
% buried
20
Peptide accession
Q9UMN6
Residue number A
2703
Residue number B
2710
Peptide name
Histone-lysine N-methyltransferase 2B

Ligandability

Cysteine 2703 of Histone-lysine N-methyltransferase 2B

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 2710 of Histone-lysine N-methyltransferase 2B

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 2B between cysteines 2655 and 2705.

Details

Redox score ?
78
PDB code
7bre
Structure name
the crystal structure of mll2 in complex with ash2l and rbbp5
Structure deposition date
2020-03-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
8
% buried
22
Peptide accession
Q9UMN6
Residue number A
2655
Residue number B
2705
Peptide name
Histone-lysine N-methyltransferase 2B

Ligandability

Cysteine 2655 of Histone-lysine N-methyltransferase 2B

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 2705 of Histone-lysine N-methyltransferase 2B

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 2B between cysteines 972 and 1005.

Details

Redox score ?
77
PDB code
4pzi
Structure name
zinc finger region of mll2 in complex with cpg dna
Structure deposition date
2014-03-31
Thiol separation (Å)
3
Half-sphere exposure sum ?
50
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UMN6
Residue number A
972
Residue number B
1005
Peptide name
Histone-lysine N-methyltransferase 2B

Ligandability

Cysteine 972 of Histone-lysine N-methyltransferase 2B

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 1005 of Histone-lysine N-methyltransferase 2B

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 2B between cysteines 969 and 972.

Details

Redox score ?
76
PDB code
4pzi
Structure name
zinc finger region of mll2 in complex with cpg dna
Structure deposition date
2014-03-31
Thiol separation (Å)
4
Half-sphere exposure sum ?
42
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UMN6
Residue number A
969
Residue number B
972
Peptide name
Histone-lysine N-methyltransferase 2B

Ligandability

Cysteine 969 of Histone-lysine N-methyltransferase 2B

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 972 of Histone-lysine N-methyltransferase 2B

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 2B between cysteines 966 and 969.

Details

Redox score ?
75
PDB code
4pzi
Structure name
zinc finger region of mll2 in complex with cpg dna
Structure deposition date
2014-03-31
Thiol separation (Å)
4
Half-sphere exposure sum ?
37
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UMN6
Residue number A
966
Residue number B
969
Peptide name
Histone-lysine N-methyltransferase 2B

Ligandability

Cysteine 966 of Histone-lysine N-methyltransferase 2B

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 969 of Histone-lysine N-methyltransferase 2B

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 2B between cysteines 978 and 981.

Details

Redox score ?
75
PDB code
4pzi
Structure name
zinc finger region of mll2 in complex with cpg dna
Structure deposition date
2014-03-31
Thiol separation (Å)
4
Half-sphere exposure sum ?
37
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UMN6
Residue number A
978
Residue number B
981
Peptide name
Histone-lysine N-methyltransferase 2B

Ligandability

Cysteine 978 of Histone-lysine N-methyltransferase 2B

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 981 of Histone-lysine N-methyltransferase 2B

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 2B between cysteines 978 and 1000.

Details

Redox score ?
75
PDB code
4pzi
Structure name
zinc finger region of mll2 in complex with cpg dna
Structure deposition date
2014-03-31
Thiol separation (Å)
4
Half-sphere exposure sum ?
46
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UMN6
Residue number A
978
Residue number B
1000
Peptide name
Histone-lysine N-methyltransferase 2B

Ligandability

Cysteine 978 of Histone-lysine N-methyltransferase 2B

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 1000 of Histone-lysine N-methyltransferase 2B

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 2B between cysteines 984 and 1000.

Details

Redox score ?
75
PDB code
4pzi
Structure name
zinc finger region of mll2 in complex with cpg dna
Structure deposition date
2014-03-31
Thiol separation (Å)
4
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UMN6
Residue number A
984
Residue number B
1000
Peptide name
Histone-lysine N-methyltransferase 2B

Ligandability

Cysteine 984 of Histone-lysine N-methyltransferase 2B

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 1000 of Histone-lysine N-methyltransferase 2B

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 2B between cysteines 981 and 984.

Details

Redox score ?
75
PDB code
4pzi
Structure name
zinc finger region of mll2 in complex with cpg dna
Structure deposition date
2014-03-31
Thiol separation (Å)
4
Half-sphere exposure sum ?
45
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UMN6
Residue number A
981
Residue number B
984
Peptide name
Histone-lysine N-methyltransferase 2B

Ligandability

Cysteine 981 of Histone-lysine N-methyltransferase 2B

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 984 of Histone-lysine N-methyltransferase 2B

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 2B between cysteines 966 and 1005.

Details

Redox score ?
75
PDB code
4pzi
Structure name
zinc finger region of mll2 in complex with cpg dna
Structure deposition date
2014-03-31
Thiol separation (Å)
4
Half-sphere exposure sum ?
45
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UMN6
Residue number A
966
Residue number B
1005
Peptide name
Histone-lysine N-methyltransferase 2B

Ligandability

Cysteine 966 of Histone-lysine N-methyltransferase 2B

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 1005 of Histone-lysine N-methyltransferase 2B

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 2B between cysteines 969 and 1005.

Details

Redox score ?
74
PDB code
4pzi
Structure name
zinc finger region of mll2 in complex with cpg dna
Structure deposition date
2014-03-31
Thiol separation (Å)
4
Half-sphere exposure sum ?
44
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UMN6
Residue number A
969
Residue number B
1005
Peptide name
Histone-lysine N-methyltransferase 2B

Ligandability

Cysteine 969 of Histone-lysine N-methyltransferase 2B

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 1005 of Histone-lysine N-methyltransferase 2B

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 2B between cysteines 981 and 1000.

Details

Redox score ?
74
PDB code
4pzi
Structure name
zinc finger region of mll2 in complex with cpg dna
Structure deposition date
2014-03-31
Thiol separation (Å)
4
Half-sphere exposure sum ?
44
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UMN6
Residue number A
981
Residue number B
1000
Peptide name
Histone-lysine N-methyltransferase 2B

Ligandability

Cysteine 981 of Histone-lysine N-methyltransferase 2B

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 1000 of Histone-lysine N-methyltransferase 2B

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 2B between cysteines 966 and 972.

Details

Redox score ?
74
PDB code
4pzi
Structure name
zinc finger region of mll2 in complex with cpg dna
Structure deposition date
2014-03-31
Thiol separation (Å)
4
Half-sphere exposure sum ?
43
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UMN6
Residue number A
966
Residue number B
972
Peptide name
Histone-lysine N-methyltransferase 2B

Ligandability

Cysteine 966 of Histone-lysine N-methyltransferase 2B

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 972 of Histone-lysine N-methyltransferase 2B

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 2B between cysteines 2655 and 2703.

Details

Redox score ?
73
PDB code
7bre
Structure name
the crystal structure of mll2 in complex with ash2l and rbbp5
Structure deposition date
2020-03-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
10
% buried
29
Peptide accession
Q9UMN6
Residue number A
2655
Residue number B
2703
Peptide name
Histone-lysine N-methyltransferase 2B

Ligandability

Cysteine 2655 of Histone-lysine N-methyltransferase 2B

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 2703 of Histone-lysine N-methyltransferase 2B

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 2B between cysteines 978 and 984.

Details

Redox score ?
73
PDB code
4pzi
Structure name
zinc finger region of mll2 in complex with cpg dna
Structure deposition date
2014-03-31
Thiol separation (Å)
4
Half-sphere exposure sum ?
46
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UMN6
Residue number A
978
Residue number B
984
Peptide name
Histone-lysine N-methyltransferase 2B

Ligandability

Cysteine 978 of Histone-lysine N-methyltransferase 2B

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 984 of Histone-lysine N-methyltransferase 2B

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 2B between cysteines 999 and 1000. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
54
PDB code
4pzi
Structure name
zinc finger region of mll2 in complex with cpg dna
Structure deposition date
2014-03-31
Thiol separation (Å)
7
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UMN6
Residue number A
999
Residue number B
1000
Peptide name
Histone-lysine N-methyltransferase 2B

Ligandability

Cysteine 999 of Histone-lysine N-methyltransferase 2B

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.

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 1000 of Histone-lysine N-methyltransferase 2B

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 2B between cysteines 981 and 999. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
4pzi
Structure name
zinc finger region of mll2 in complex with cpg dna
Structure deposition date
2014-03-31
Thiol separation (Å)
8
Half-sphere exposure sum ?
46
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UMN6
Residue number A
981
Residue number B
999
Peptide name
Histone-lysine N-methyltransferase 2B

Ligandability

Cysteine 981 of Histone-lysine N-methyltransferase 2B

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 999 of Histone-lysine N-methyltransferase 2B

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.

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 2B between cysteines 999 and 1005. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
4pzi
Structure name
zinc finger region of mll2 in complex with cpg dna
Structure deposition date
2014-03-31
Thiol separation (Å)
8
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UMN6
Residue number A
999
Residue number B
1005
Peptide name
Histone-lysine N-methyltransferase 2B

Ligandability

Cysteine 999 of Histone-lysine N-methyltransferase 2B

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.

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 1005 of Histone-lysine N-methyltransferase 2B

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 2B between cysteines 2591 and 2659. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
7bre
Structure name
the crystal structure of mll2 in complex with ash2l and rbbp5
Structure deposition date
2020-03-28
Thiol separation (Å)
8
Half-sphere exposure sum ?
71
Minimum pKa ?
10
% buried
60
Peptide accession
Q9UMN6
Residue number A
2591
Residue number B
2659
Peptide name
Histone-lysine N-methyltransferase 2B

Ligandability

Cysteine 2591 of Histone-lysine N-methyltransferase 2B

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 2659 of Histone-lysine N-methyltransferase 2B

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 2B between cysteines 972 and 999. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
4pzi
Structure name
zinc finger region of mll2 in complex with cpg dna
Structure deposition date
2014-03-31
Thiol separation (Å)
9
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UMN6
Residue number A
972
Residue number B
999
Peptide name
Histone-lysine N-methyltransferase 2B

Ligandability

Cysteine 972 of Histone-lysine N-methyltransferase 2B

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 999 of Histone-lysine N-methyltransferase 2B

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.

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 2B between cysteines 984 and 999. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
4pzi
Structure name
zinc finger region of mll2 in complex with cpg dna
Structure deposition date
2014-03-31
Thiol separation (Å)
9
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UMN6
Residue number A
984
Residue number B
999
Peptide name
Histone-lysine N-methyltransferase 2B

Ligandability

Cysteine 984 of Histone-lysine N-methyltransferase 2B

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 999 of Histone-lysine N-methyltransferase 2B

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.

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 2B between cysteines 969 and 999. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
4pzi
Structure name
zinc finger region of mll2 in complex with cpg dna
Structure deposition date
2014-03-31
Thiol separation (Å)
10
Half-sphere exposure sum ?
47
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UMN6
Residue number A
969
Residue number B
999
Peptide name
Histone-lysine N-methyltransferase 2B

Ligandability

Cysteine 969 of Histone-lysine N-methyltransferase 2B

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 999 of Histone-lysine N-methyltransferase 2B

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.

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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