ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Gem-associated protein 2

Intramolecular
Cysteine 89 and cysteine 241
Cysteine 148 and cysteine 221
A redox-regulated disulphide may form within Gem-associated protein 2 between cysteines 89 and 241. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
5xjs
Structure name
crystal structure of the gemin2-binding domain of smn, gemin2dn39 in complex with smd1(1-82)/d2/f/e from human
Structure deposition date
2017-05-04
Thiol separation (Å)
8
Half-sphere exposure sum ?
75
Minimum pKa ?
11
% buried
88
Peptide accession
O14893
Residue number A
89
Residue number B
241
Peptide name
Gem-associated protein 2

Ligandability

Cysteine 89 of Gem-associated protein 2

Cysteine 241 of Gem-associated protein 2

A redox-regulated disulphide may form within Gem-associated protein 2 between cysteines 148 and 221. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
2leh
Structure name
solution structure of the core smn-gemin2 complex
Structure deposition date
2011-06-15
Thiol separation (Å)
10
Half-sphere exposure sum ?
58
Minimum pKa ?
11
% buried
58
Peptide accession
O14893
Residue number A
148
Residue number B
221
Peptide name
Gem-associated protein 2

Ligandability

Cysteine 148 of Gem-associated protein 2

Cysteine 221 of Gem-associated protein 2

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