ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Histone-lysine N-methyltransferase 2D

Intramolecular
Cysteine 1507 and cysteine 1510
Cysteine 1507 and cysteine 1534
Cysteine 1523 and cysteine 1556
Cysteine 1553 and cysteine 1556
Cysteine 1523 and cysteine 1526
Cysteine 1526 and cysteine 1553
Cysteine 1526 and cysteine 1556
Cysteine 1523 and cysteine 1553
Cysteine 1510 and cysteine 1534
Cysteine 1507 and cysteine 1553
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase 2D between cysteines 1507 and 1510.

Details

Redox score ?
87
PDB code
6o7g
Structure name
solution structure of mll4 phd6 domain in complex with histone h4k16ac peptide
Structure deposition date
2019-03-07
Thiol separation (Å)
4
Half-sphere exposure sum ?
45
Minimum pKa ?
6
% buried
6
Peptide accession
O14686
Residue number A
1507
Residue number B
1510
Peptide name
Histone-lysine N-methyltransferase 2D

Ligandability

Cysteine 1507 of Histone-lysine N-methyltransferase 2D

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in 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 1510 of Histone-lysine N-methyltransferase 2D

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in 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 2D between cysteines 1507 and 1534.

Details

Redox score ?
86
PDB code
6o7g
Structure name
solution structure of mll4 phd6 domain in complex with histone h4k16ac peptide
Structure deposition date
2019-03-07
Thiol separation (Å)
4
Half-sphere exposure sum ?
50
Minimum pKa ?
6
% buried
14
Peptide accession
O14686
Residue number A
1507
Residue number B
1534
Peptide name
Histone-lysine N-methyltransferase 2D

Ligandability

Cysteine 1507 of Histone-lysine N-methyltransferase 2D

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in 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 1534 of Histone-lysine N-methyltransferase 2D

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in 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 2D between cysteines 1523 and 1556.

Details

Redox score ?
85
PDB code
6o7g
Structure name
solution structure of mll4 phd6 domain in complex with histone h4k16ac peptide
Structure deposition date
2019-03-07
Thiol separation (Å)
4
Half-sphere exposure sum ?
53
Minimum pKa ?
6
% buried
6
Peptide accession
O14686
Residue number A
1523
Residue number B
1556
Peptide name
Histone-lysine N-methyltransferase 2D

Ligandability

Cysteine 1523 of Histone-lysine N-methyltransferase 2D

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in 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 1556 of Histone-lysine N-methyltransferase 2D

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in 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 2D between cysteines 1553 and 1556.

Details

Redox score ?
83
PDB code
6o7g
Structure name
solution structure of mll4 phd6 domain in complex with histone h4k16ac peptide
Structure deposition date
2019-03-07
Thiol separation (Å)
4
Half-sphere exposure sum ?
53
Minimum pKa ?
8
% buried
4
Peptide accession
O14686
Residue number A
1553
Residue number B
1556
Peptide name
Histone-lysine N-methyltransferase 2D

Ligandability

Cysteine 1553 of Histone-lysine N-methyltransferase 2D

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in 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 1556 of Histone-lysine N-methyltransferase 2D

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in 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 2D between cysteines 1523 and 1526.

Details

Redox score ?
82
PDB code
6o7g
Structure name
solution structure of mll4 phd6 domain in complex with histone h4k16ac peptide
Structure deposition date
2019-03-07
Thiol separation (Å)
4
Half-sphere exposure sum ?
56
Minimum pKa ?
6
% buried
6
Peptide accession
O14686
Residue number A
1523
Residue number B
1526
Peptide name
Histone-lysine N-methyltransferase 2D

Ligandability

Cysteine 1523 of Histone-lysine N-methyltransferase 2D

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in 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 1526 of Histone-lysine N-methyltransferase 2D

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in 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 2D between cysteines 1526 and 1553.

Details

Redox score ?
80
PDB code
6o7g
Structure name
solution structure of mll4 phd6 domain in complex with histone h4k16ac peptide
Structure deposition date
2019-03-07
Thiol separation (Å)
4
Half-sphere exposure sum ?
56
Minimum pKa ?
8
% buried
4
Peptide accession
O14686
Residue number A
1526
Residue number B
1553
Peptide name
Histone-lysine N-methyltransferase 2D

Ligandability

Cysteine 1526 of Histone-lysine N-methyltransferase 2D

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in 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 1553 of Histone-lysine N-methyltransferase 2D

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in 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 2D between cysteines 1526 and 1556.

Details

Redox score ?
80
PDB code
6o7g
Structure name
solution structure of mll4 phd6 domain in complex with histone h4k16ac peptide
Structure deposition date
2019-03-07
Thiol separation (Å)
4
Half-sphere exposure sum ?
41
Minimum pKa ?
10
% buried
0
Peptide accession
O14686
Residue number A
1526
Residue number B
1556
Peptide name
Histone-lysine N-methyltransferase 2D

Ligandability

Cysteine 1526 of Histone-lysine N-methyltransferase 2D

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in 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 1556 of Histone-lysine N-methyltransferase 2D

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in 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 2D between cysteines 1523 and 1553.

Details

Redox score ?
79
PDB code
6o7g
Structure name
solution structure of mll4 phd6 domain in complex with histone h4k16ac peptide
Structure deposition date
2019-03-07
Thiol separation (Å)
4
Half-sphere exposure sum ?
68
Minimum pKa ?
6
% buried
10
Peptide accession
O14686
Residue number A
1523
Residue number B
1553
Peptide name
Histone-lysine N-methyltransferase 2D

Ligandability

Cysteine 1523 of Histone-lysine N-methyltransferase 2D

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in 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 1553 of Histone-lysine N-methyltransferase 2D

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in 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 2D between cysteines 1510 and 1534.

Details

Redox score ?
79
PDB code
6o7g
Structure name
solution structure of mll4 phd6 domain in complex with histone h4k16ac peptide
Structure deposition date
2019-03-07
Thiol separation (Å)
4
Half-sphere exposure sum ?
41
Minimum pKa ?
9
% buried
8
Peptide accession
O14686
Residue number A
1510
Residue number B
1534
Peptide name
Histone-lysine N-methyltransferase 2D

Ligandability

Cysteine 1510 of Histone-lysine N-methyltransferase 2D

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in 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 1534 of Histone-lysine N-methyltransferase 2D

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in 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 2D between cysteines 1507 and 1553. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
6o7g
Structure name
solution structure of mll4 phd6 domain in complex with histone h4k16ac peptide
Structure deposition date
2019-03-07
Thiol separation (Å)
10
Half-sphere exposure sum ?
61
Minimum pKa ?
6
% buried
10
Peptide accession
O14686
Residue number A
1507
Residue number B
1553
Peptide name
Histone-lysine N-methyltransferase 2D

Ligandability

Cysteine 1507 of Histone-lysine N-methyltransferase 2D

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in 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 1553 of Histone-lysine N-methyltransferase 2D

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in 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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