ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Poly [ADP-ribose] polymerase 2

Intramolecular
Cysteine 264 and cysteine 278
Cysteine 246 and cysteine 367
A redox-regulated disulphide may form within Poly [ADP-ribose] polymerase 2 between cysteines 264 and 278. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
51
PDB code
1gs0
Structure name
crystal structure of the catalytic fragment of murine poly (adp-ribose) polymerase-2
Structure deposition date
2001-12-19
Thiol separation (Å)
8
Half-sphere exposure sum ?
64
Minimum pKa ?
10
% buried
29
Peptide accession
O88554
Residue number A
264
Residue number B
278
Peptide name
Poly [ADP-ribose] polymerase 2

Ligandability

Cysteine 264 of Poly [ADP-ribose] polymerase 2

Cysteine 278 of Poly [ADP-ribose] polymerase 2

A redox-regulated disulphide may form within Poly [ADP-ribose] polymerase 2 between cysteines 246 and 367 (233 and 354 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
6x0m
Structure name
bridging of double-strand dna break activates parp2/hpf1 to modify chromatin
Structure deposition date
2020-05-16
Thiol separation (Å)
9
Half-sphere exposure sum ?
72
Minimum pKa ?
12
% buried
80
Peptide accession
Q9UGN5
Residue number A
246
Residue number B
367
Peptide name
Poly [ADP-ribose] polymerase 2

Ligandability

Cysteine 246 of Poly [ADP-ribose] polymerase 2

Cysteine 367 of Poly [ADP-ribose] polymerase 2

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