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Histone-lysine N-methyltransferase SETD2

Intramolecular
Cysteine 1680 and cysteine 1685
Cysteine 1678 and cysteine 1680
Cysteine 1678 and cysteine 1685
Cysteine 1529 and cysteine 1533 L
Cysteine 1499 and cysteine 1501
Cysteine 1631 and cysteine 1685
Cysteine 1501 and cysteine 1520
Cysteine 1529 and cysteine 1539 L
Cysteine 1631 and cysteine 1680
Cysteine 1499 and cysteine 1516
More...
Cysteine 1533 and cysteine 1539 L
Cysteine 1516 and cysteine 1533 L
Cysteine 1516 and cysteine 1529
Cysteine 1499 and cysteine 1529
Cysteine 1520 and cysteine 1529
Cysteine 1499 and cysteine 1520
Cysteine 1516 and cysteine 1520
Cysteine 1499 and cysteine 1533 L
Cysteine 1501 and cysteine 1516
Cysteine 1631 and cysteine 1678
Cysteine 1516 and cysteine 1539 L
Cysteine 1501 and cysteine 1529
Cysteine 1520 and cysteine 1533 L
Cysteine 1501 and cysteine 1533 L
Cysteine 1520 and cysteine 1539 L
Cysteine 1499 and cysteine 1539 L
Cysteine 1501 and cysteine 1539 L
Cysteine 1449 and cysteine 1463
Cysteine 2485 and cysteine 2532
Cysteine 1449 and cysteine 1623
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase SETD2 between cysteines 1680 and 1685.

Details

Redox score ?
89
PDB code
5lsx
Structure name
structure of the epigenetic oncogene mmset and inhibition by n-alkyl sinefungin derivatives
Structure deposition date
2016-09-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
48
Minimum pKa ?
6
% buried
9
Peptide accession
Q9BYW2
Residue number A
1680
Residue number B
1685
Peptide name
Histone-lysine N-methyltransferase SETD2

Ligandability

Cysteine 1680 of Histone-lysine N-methyltransferase SETD2

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 1685 of Histone-lysine N-methyltransferase SETD2

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 SETD2 between cysteines 1678 and 1680.

Details

Redox score ?
89
PDB code
7lzb
Structure name
crystal structure of setd2 bound to compound 2
Structure deposition date
2021-03-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
52
Minimum pKa ?
5
% buried
30
Peptide accession
Q9BYW2
Residue number A
1678
Residue number B
1680
Peptide name
Histone-lysine N-methyltransferase SETD2

Ligandability

Cysteine 1678 of Histone-lysine N-methyltransferase SETD2

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 1680 of Histone-lysine N-methyltransferase SETD2

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 SETD2 between cysteines 1678 and 1685.

Details

Redox score ?
88
PDB code
7ty3
Structure name
crystal structure of setd2 bound to an indole-based inhibitor
Structure deposition date
2022-02-11
Thiol separation (Å)
3
Half-sphere exposure sum ?
42
Minimum pKa ?
8
% buried
20
Peptide accession
Q9BYW2
Residue number A
1678
Residue number B
1685
Peptide name
Histone-lysine N-methyltransferase SETD2

Ligandability

Cysteine 1678 of Histone-lysine N-methyltransferase SETD2

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 1685 of Histone-lysine N-methyltransferase SETD2

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 SETD2 between cysteines 1529 and 1533.

Details

Redox score ?
88
PDB code
7ty2
Structure name
crystal structure of setd2 bound to an indole-based inhibitor
Structure deposition date
2022-02-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
68
Minimum pKa ?
5
% buried
32
Peptide accession
Q9BYW2
Residue number A
1529
Residue number B
1533
Peptide name
Histone-lysine N-methyltransferase SETD2

Ligandability

Cysteine 1529 of Histone-lysine N-methyltransferase SETD2

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 1533 of Histone-lysine N-methyltransferase SETD2

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 SETD2 between cysteines 1499 and 1501.

Details

Redox score ?
88
PDB code
5lt6
Structure name
structure of the epigenetic oncogene mmset and inhibition by n-alkyl sinefungin derivatives
Structure deposition date
2016-09-06
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
6
% buried
18
Peptide accession
Q9BYW2
Residue number A
1499
Residue number B
1501
Peptide name
Histone-lysine N-methyltransferase SETD2

Ligandability

Cysteine 1499 of Histone-lysine N-methyltransferase SETD2

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 1501 of Histone-lysine N-methyltransferase SETD2

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 SETD2 between cysteines 1631 and 1685.

Details

Redox score ?
86
PDB code
5lsx
Structure name
structure of the epigenetic oncogene mmset and inhibition by n-alkyl sinefungin derivatives
Structure deposition date
2016-09-05
Thiol separation (Å)
3
Half-sphere exposure sum ?
46
Minimum pKa ?
8
% buried
6
Peptide accession
Q9BYW2
Residue number A
1631
Residue number B
1685
Peptide name
Histone-lysine N-methyltransferase SETD2

Ligandability

Cysteine 1631 of Histone-lysine N-methyltransferase SETD2

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 1685 of Histone-lysine N-methyltransferase SETD2

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 SETD2 between cysteines 1501 and 1520.

Details

Redox score ?
85
PDB code
7ty2
Structure name
crystal structure of setd2 bound to an indole-based inhibitor
Structure deposition date
2022-02-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
8
% buried
18
Peptide accession
Q9BYW2
Residue number A
1501
Residue number B
1520
Peptide name
Histone-lysine N-methyltransferase SETD2

Ligandability

Cysteine 1501 of Histone-lysine N-methyltransferase SETD2

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 1520 of Histone-lysine N-methyltransferase SETD2

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 SETD2 between cysteines 1529 and 1539.

Details

Redox score ?
85
PDB code
6j9j
Structure name
crystal structure of sestd2 in complex with h3
Structure deposition date
2019-01-23
Thiol separation (Å)
4
Half-sphere exposure sum ?
71
Minimum pKa ?
5
% buried
43
Peptide accession
Q9BYW2
Residue number A
1529
Residue number B
1539
Peptide name
Histone-lysine N-methyltransferase SETD2

Ligandability

Cysteine 1529 of Histone-lysine N-methyltransferase SETD2

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 1539 of Histone-lysine N-methyltransferase SETD2

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 SETD2 between cysteines 1631 and 1680.

Details

Redox score ?
85
PDB code
5lsx
Structure name
structure of the epigenetic oncogene mmset and inhibition by n-alkyl sinefungin derivatives
Structure deposition date
2016-09-05
Thiol separation (Å)
3
Half-sphere exposure sum ?
58
Minimum pKa ?
6
% buried
14
Peptide accession
Q9BYW2
Residue number A
1631
Residue number B
1680
Peptide name
Histone-lysine N-methyltransferase SETD2

Ligandability

Cysteine 1631 of Histone-lysine N-methyltransferase SETD2

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 1680 of Histone-lysine N-methyltransferase SETD2

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 SETD2 between cysteines 1499 and 1516.

Details

Redox score ?
84
PDB code
7lzb
Structure name
crystal structure of setd2 bound to compound 2
Structure deposition date
2021-03-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
64
Minimum pKa ?
6
% buried
26
Peptide accession
Q9BYW2
Residue number A
1499
Residue number B
1516
Peptide name
Histone-lysine N-methyltransferase SETD2

Ligandability

Cysteine 1499 of Histone-lysine N-methyltransferase SETD2

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 1516 of Histone-lysine N-methyltransferase SETD2

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 SETD2 between cysteines 1533 and 1539.

Details

Redox score ?
84
PDB code
5lsz
Structure name
structure of the epigenetic oncogene mmset and inhibition by n-alkyl sinefungin derivatives
Structure deposition date
2016-09-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
57
Minimum pKa ?
7
% buried
28
Peptide accession
Q9BYW2
Residue number A
1533
Residue number B
1539
Peptide name
Histone-lysine N-methyltransferase SETD2

Ligandability

Cysteine 1533 of Histone-lysine N-methyltransferase SETD2

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 1539 of Histone-lysine N-methyltransferase SETD2

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 SETD2 between cysteines 1516 and 1533.

Details

Redox score ?
84
PDB code
7lzf
Structure name
crystal structure of setd2 bound to compound 57
Structure deposition date
2021-03-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
8
% buried
36
Peptide accession
Q9BYW2
Residue number A
1516
Residue number B
1533
Peptide name
Histone-lysine N-methyltransferase SETD2

Ligandability

Cysteine 1516 of Histone-lysine N-methyltransferase SETD2

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 1533 of Histone-lysine N-methyltransferase SETD2

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 SETD2 between cysteines 1516 and 1529.

Details

Redox score ?
84
PDB code
5v21
Structure name
crystal structure of human setd2 set-domain in complex with h3k36m peptide and sam
Structure deposition date
2017-03-02
Thiol separation (Å)
4
Half-sphere exposure sum ?
73
Minimum pKa ?
5
% buried
36
Peptide accession
Q9BYW2
Residue number A
1516
Residue number B
1529
Peptide name
Histone-lysine N-methyltransferase SETD2

Ligandability

Cysteine 1516 of Histone-lysine N-methyltransferase SETD2

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 1529 of Histone-lysine N-methyltransferase SETD2

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 SETD2 between cysteines 1499 and 1529.

Details

Redox score ?
84
PDB code
5lss
Structure name
structure of the epigenetic oncogene mmset and inhibition by n-alkyl sinefungin derivatives
Structure deposition date
2016-09-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
68
Minimum pKa ?
4
% buried
28
Peptide accession
Q9BYW2
Residue number A
1499
Residue number B
1529
Peptide name
Histone-lysine N-methyltransferase SETD2

Ligandability

Cysteine 1499 of Histone-lysine N-methyltransferase SETD2

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 1529 of Histone-lysine N-methyltransferase SETD2

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 SETD2 between cysteines 1520 and 1529.

Details

Redox score ?
84
PDB code
7lzb
Structure name
crystal structure of setd2 bound to compound 2
Structure deposition date
2021-03-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
66
Minimum pKa ?
5
% buried
34
Peptide accession
Q9BYW2
Residue number A
1520
Residue number B
1529
Peptide name
Histone-lysine N-methyltransferase SETD2

Ligandability

Cysteine 1520 of Histone-lysine N-methyltransferase SETD2

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 1529 of Histone-lysine N-methyltransferase SETD2

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 SETD2 between cysteines 1499 and 1520.

Details

Redox score ?
83
PDB code
7ty2
Structure name
crystal structure of setd2 bound to an indole-based inhibitor
Structure deposition date
2022-02-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
56
Minimum pKa ?
8
% buried
22
Peptide accession
Q9BYW2
Residue number A
1499
Residue number B
1520
Peptide name
Histone-lysine N-methyltransferase SETD2

Ligandability

Cysteine 1499 of Histone-lysine N-methyltransferase SETD2

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 1520 of Histone-lysine N-methyltransferase SETD2

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 SETD2 between cysteines 1516 and 1520.

Details

Redox score ?
83
PDB code
7lzd
Structure name
crystal structure of setd2 bound to compound 35
Structure deposition date
2021-03-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
8
% buried
36
Peptide accession
Q9BYW2
Residue number A
1516
Residue number B
1520
Peptide name
Histone-lysine N-methyltransferase SETD2

Ligandability

Cysteine 1516 of Histone-lysine N-methyltransferase SETD2

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 1520 of Histone-lysine N-methyltransferase SETD2

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 SETD2 between cysteines 1499 and 1533.

Details

Redox score ?
79
PDB code
5lt6
Structure name
structure of the epigenetic oncogene mmset and inhibition by n-alkyl sinefungin derivatives
Structure deposition date
2016-09-06
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
7
% buried
41
Peptide accession
Q9BYW2
Residue number A
1499
Residue number B
1533
Peptide name
Histone-lysine N-methyltransferase SETD2

Ligandability

Cysteine 1499 of Histone-lysine N-methyltransferase SETD2

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 1533 of Histone-lysine N-methyltransferase SETD2

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 SETD2 between cysteines 1501 and 1516.

Details

Redox score ?
77
PDB code
5lt6
Structure name
structure of the epigenetic oncogene mmset and inhibition by n-alkyl sinefungin derivatives
Structure deposition date
2016-09-06
Thiol separation (Å)
4
Half-sphere exposure sum ?
60
Minimum pKa ?
11
% buried
26
Peptide accession
Q9BYW2
Residue number A
1501
Residue number B
1516
Peptide name
Histone-lysine N-methyltransferase SETD2

Ligandability

Cysteine 1501 of Histone-lysine N-methyltransferase SETD2

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 1516 of Histone-lysine N-methyltransferase SETD2

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 SETD2 between cysteines 1631 and 1678.

Details

Redox score ?
76
PDB code
5lsy
Structure name
structure of the epigenetic oncogene mmset and inhibition by n-alkyl sinefungin derivatives
Structure deposition date
2016-09-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
10
% buried
34
Peptide accession
Q9BYW2
Residue number A
1631
Residue number B
1678
Peptide name
Histone-lysine N-methyltransferase SETD2

Ligandability

Cysteine 1631 of Histone-lysine N-methyltransferase SETD2

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 1678 of Histone-lysine N-methyltransferase SETD2

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 SETD2 between cysteines 1516 and 1539.

Details

Redox score ?
75
PDB code
5lt6
Structure name
structure of the epigenetic oncogene mmset and inhibition by n-alkyl sinefungin derivatives
Structure deposition date
2016-09-06
Thiol separation (Å)
4
Half-sphere exposure sum ?
68
Minimum pKa ?
10
% buried
48
Peptide accession
Q9BYW2
Residue number A
1516
Residue number B
1539
Peptide name
Histone-lysine N-methyltransferase SETD2

Ligandability

Cysteine 1516 of Histone-lysine N-methyltransferase SETD2

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 1539 of Histone-lysine N-methyltransferase SETD2

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 SETD2 between cysteines 1501 and 1529.

Details

Redox score ?
72
PDB code
5v21
Structure name
crystal structure of human setd2 set-domain in complex with h3k36m peptide and sam
Structure deposition date
2017-03-02
Thiol separation (Å)
6
Half-sphere exposure sum ?
65
Minimum pKa ?
5
% buried
24
Peptide accession
Q9BYW2
Residue number A
1501
Residue number B
1529
Peptide name
Histone-lysine N-methyltransferase SETD2

Ligandability

Cysteine 1501 of Histone-lysine N-methyltransferase SETD2

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 1529 of Histone-lysine N-methyltransferase SETD2

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 SETD2 between cysteines 1520 and 1533.

Details

Redox score ?
70
PDB code
7ty2
Structure name
crystal structure of setd2 bound to an indole-based inhibitor
Structure deposition date
2022-02-11
Thiol separation (Å)
6
Half-sphere exposure sum ?
56
Minimum pKa ?
8
% buried
28
Peptide accession
Q9BYW2
Residue number A
1520
Residue number B
1533
Peptide name
Histone-lysine N-methyltransferase SETD2

Ligandability

Cysteine 1520 of Histone-lysine N-methyltransferase SETD2

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 1533 of Histone-lysine N-methyltransferase SETD2

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 SETD2 between cysteines 1501 and 1533.

Details

Redox score ?
68
PDB code
5v22
Structure name
crystal structure of human setd2 set-domain in complex with h3k36m peptide and sah
Structure deposition date
2017-03-02
Thiol separation (Å)
7
Half-sphere exposure sum ?
53
Minimum pKa ?
8
% buried
20
Peptide accession
Q9BYW2
Residue number A
1501
Residue number B
1533
Peptide name
Histone-lysine N-methyltransferase SETD2

Ligandability

Cysteine 1501 of Histone-lysine N-methyltransferase SETD2

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 1533 of Histone-lysine N-methyltransferase SETD2

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 SETD2 between cysteines 1520 and 1539.

Details

Redox score ?
67
PDB code
7ty3
Structure name
crystal structure of setd2 bound to an indole-based inhibitor
Structure deposition date
2022-02-11
Thiol separation (Å)
6
Half-sphere exposure sum ?
59
Minimum pKa ?
9
% buried
38
Peptide accession
Q9BYW2
Residue number A
1520
Residue number B
1539
Peptide name
Histone-lysine N-methyltransferase SETD2

Ligandability

Cysteine 1520 of Histone-lysine N-methyltransferase SETD2

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 1539 of Histone-lysine N-methyltransferase SETD2

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 SETD2 between cysteines 1499 and 1539.

Details

Redox score ?
60
PDB code
6vdb
Structure name
setd2 in complex with a h3-variant super-substrate peptide
Structure deposition date
2019-12-24
Thiol separation (Å)
6
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9BYW2
Residue number A
1499
Residue number B
1539
Peptide name
Histone-lysine N-methyltransferase SETD2

Ligandability

Cysteine 1499 of Histone-lysine N-methyltransferase SETD2

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 1539 of Histone-lysine N-methyltransferase SETD2

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 SETD2 between cysteines 1501 and 1539. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
53
PDB code
5v22
Structure name
crystal structure of human setd2 set-domain in complex with h3k36m peptide and sah
Structure deposition date
2017-03-02
Thiol separation (Å)
8
Half-sphere exposure sum ?
57
Minimum pKa ?
12
% buried
28
Peptide accession
Q9BYW2
Residue number A
1501
Residue number B
1539
Peptide name
Histone-lysine N-methyltransferase SETD2

Ligandability

Cysteine 1501 of Histone-lysine N-methyltransferase SETD2

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 1539 of Histone-lysine N-methyltransferase SETD2

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 SETD2 between cysteines 1449 and 1463. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
7lzb
Structure name
crystal structure of setd2 bound to compound 2
Structure deposition date
2021-03-09
Thiol separation (Å)
8
Half-sphere exposure sum ?
49
Minimum pKa ?
12
% buried
nan
Peptide accession
Q9BYW2
Residue number A
1449
Residue number B
1463
Peptide name
Histone-lysine N-methyltransferase SETD2

Ligandability

Cysteine 1449 of Histone-lysine N-methyltransferase SETD2

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 1463 of Histone-lysine N-methyltransferase SETD2

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 SETD2 between cysteines 2485 and 2532 (33 and 80 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
2a7o
Structure name
solution structure of the hset2/hypb sri domain
Structure deposition date
2005-07-05
Thiol separation (Å)
9
Half-sphere exposure sum ?
63
Minimum pKa ?
11
% buried
44
Peptide accession
Q9BYW2
Residue number A
2485
Residue number B
2532
Peptide name
Histone-lysine N-methyltransferase SETD2

Ligandability

Cysteine 2485 of Histone-lysine N-methyltransferase SETD2

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 2532 of Histone-lysine N-methyltransferase SETD2

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 SETD2 between cysteines 1449 and 1623. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
5lt6
Structure name
structure of the epigenetic oncogene mmset and inhibition by n-alkyl sinefungin derivatives
Structure deposition date
2016-09-06
Thiol separation (Å)
8
Half-sphere exposure sum ?
76
Minimum pKa ?
11
% buried
71
Peptide accession
Q9BYW2
Residue number A
1449
Residue number B
1623
Peptide name
Histone-lysine N-methyltransferase SETD2

Ligandability

Cysteine 1449 of Histone-lysine N-methyltransferase SETD2

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 1623 of Histone-lysine N-methyltransferase SETD2

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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