ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Home
About
List

Histone-lysine N-methyltransferase PRDM16

Intramolecular
Cysteine 176 and cysteine 178
Cysteine 113 and cysteine 186
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase PRDM16 between cysteines 176 and 178. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
2n1i
Structure name
structure of the pr domain from prdm16
Structure deposition date
2015-04-02
Thiol separation (Å)
9
Half-sphere exposure sum ?
36
Minimum pKa ?
9
% buried
0
Peptide accession
Q9HAZ2
Residue number A
176
Residue number B
178
Peptide name
Histone-lysine N-methyltransferase PRDM16

Ligandability

Cysteine 176 of Histone-lysine N-methyltransferase PRDM16

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in 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 178 of Histone-lysine N-methyltransferase PRDM16

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in 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 PRDM16 between cysteines 113 and 186. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
2n1i
Structure name
structure of the pr domain from prdm16
Structure deposition date
2015-04-02
Thiol separation (Å)
9
Half-sphere exposure sum ?
63
Minimum pKa ?
9
% buried
42
Peptide accession
Q9HAZ2
Residue number A
113
Residue number B
186
Peptide name
Histone-lysine N-methyltransferase PRDM16

Ligandability

Cysteine 113 of Histone-lysine N-methyltransferase PRDM16

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in 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 186 of Histone-lysine N-methyltransferase PRDM16

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in 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.

If this tool was useful for finding a disulphide, please cite: