ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Poly(A)-specific ribonuclease PARN

Intermolecular
Cysteine 108 and cysteine 108
Intramolecular
Cysteine 302 and cysteine 317
A redox-regulated disulphide may form between two units of Poly(A)-specific ribonuclease PARN at cysteines 108 and 108.

Details

Redox score ?
69
PDB code
3d45
Structure name
crystal structure of mouse parn in complex with m7gpppg
Structure deposition date
2008-05-13
Thiol separation (Å)
4
Half-sphere exposure sum ?
77
Minimum pKa ?
8
% buried
100
Peptide A name
Poly(A)-specific ribonuclease PARN
Peptide B name
Poly(A)-specific ribonuclease PARN
Peptide A accession
Q8VDG3
Peptide B accession
Q8VDG3
Peptide A residue number
108
Peptide B residue number
108

Ligandability

A redox-regulated disulphide may form within Poly(A)-specific ribonuclease PARN between cysteines 302 and 317. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
2a1s
Structure name
crystal structure of native parn nuclease domain
Structure deposition date
2005-06-21
Thiol separation (Å)
9
Half-sphere exposure sum ?
53
Minimum pKa ?
9
% buried
20
Peptide accession
O95453
Residue number A
302
Residue number B
317
Peptide name
Poly(A)-specific ribonuclease PARN

Ligandability

Cysteine 302 of Poly(A)-specific ribonuclease PARN

Cysteine 317 of Poly(A)-specific ribonuclease PARN

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