Poly [ADP-ribose] polymerase 2
1gs0 B 264 B 278
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
6x0m P 233 P 354
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
If this tool was useful for finding a disulphide, please cite: