ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Histone-lysine N-methyltransferase SETD7

Intermolecular
Cysteine 119 and cysteine 119
Intramolecular
Cysteine 303 and cysteine 318
A redox-regulated disulphide may form between two units of Histone-lysine N-methyltransferase SETD7 at cysteines 119 and 119.

Details

Redox score ?
71
PDB code
1xqh
Structure name
crystal structure of a ternary complex of the methyltransferase set9 (also known as set7/9) with a p53 peptide and sah
Structure deposition date
2004-10-12
Thiol separation (Å)
4
Half-sphere exposure sum ?
74
Minimum pKa ?
9
% buried
72
Peptide A name
Histone-lysine N-methyltransferase SETD7
Peptide B name
Histone-lysine N-methyltransferase SETD7
Peptide A accession
Q8WTS6
Peptide B accession
Q8WTS6
Peptide A residue number
119
Peptide B residue number
119

Ligandability

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase SETD7 between cysteines 303 and 318. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
3m56
Structure name
set7/9 y305f in complex with taf10-k189me2 peptide and adohcy
Structure deposition date
2010-03-12
Thiol separation (Å)
9
Half-sphere exposure sum ?
77
Minimum pKa ?
12
% buried
94
Peptide accession
Q8WTS6
Residue number A
303
Residue number B
318
Peptide name
Histone-lysine N-methyltransferase SETD7

Ligandability

Cysteine 303 of Histone-lysine N-methyltransferase SETD7

Cysteine 318 of Histone-lysine N-methyltransferase SETD7

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