ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Septin-7

Intramolecular
Cysteine 160 and cysteine 161
Cysteine 204 and cysteine 280
A redox-regulated disulphide may form within Septin-7 between cysteines 160 and 161 (141 and 142 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
2qag
Structure name
crystal structure of human septin trimer 2/6/7
Structure deposition date
2007-06-15
Thiol separation (Å)
7
Half-sphere exposure sum ?
82
Minimum pKa ?
10
% buried
57
Peptide accession
Q16181
Residue number A
160
Residue number B
161
Peptide name
Septin-7

Ligandability

Cysteine 160 of Septin-7

Cysteine 161 of Septin-7

A redox-regulated disulphide may form within Septin-7 between cysteines 204 and 280 (185 and 261 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
3t5d
Structure name
crystal structure of septin 7 in complex with gdp
Structure deposition date
2011-07-27
Thiol separation (Å)
9
Half-sphere exposure sum ?
72
Minimum pKa ?
11
% buried
86
Peptide accession
Q16181
Residue number A
204
Residue number B
280
Peptide name
Septin-7

Ligandability

Cysteine 204 of Septin-7

Cysteine 280 of Septin-7

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