ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Home
About
List

Cytohesin-2

Intramolecular
Cysteine 172 and cysteine 185
Cysteine 172 and cysteine 174
Cysteine 288 and cysteine 338
A redox-regulated disulphide may form within Cytohesin-2 between cysteines 172 and 185.

Details

Redox score ?
73
PDB code
4jmo
Structure name
complexe of arno sec7 domain with the protein-protein interaction inhibitor n-(4-hydroxy-2,6-dimethylphenyl)-4- methoxybenzenesulfonamide
Structure deposition date
2013-03-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
31
Peptide accession
Q99418
Residue number A
172
Residue number B
185
Peptide name
Cytohesin-2

Ligandability

Cysteine 172 of Cytohesin-2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 185 of Cytohesin-2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Cytohesin-2 between cysteines 172 and 174. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
4jxh
Structure name
complexe of arno sec7 domain with the protein-protein interaction inhibitor n-(4-hydroxy-2,6-dimethylphenyl)benzenesulfonamide at ph 8
Structure deposition date
2013-03-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
55
Minimum pKa ?
7
% buried
32
Peptide accession
Q99418
Residue number A
172
Residue number B
174
Peptide name
Cytohesin-2

Ligandability

Cysteine 172 of Cytohesin-2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 174 of Cytohesin-2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Cytohesin-2 between cysteines 288 and 338. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
1u27
Structure name
triglycine variant of the arno pleckstrin homology domain in complex with ins(1,3,4,5)p4
Structure deposition date
2004-07-16
Thiol separation (Å)
9
Half-sphere exposure sum ?
58
Minimum pKa ?
10
% buried
25
Peptide accession
P63034
Residue number A
288
Residue number B
338
Peptide name
Cytohesin-2

Ligandability

Cysteine 288 of Cytohesin-2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 338 of Cytohesin-2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

If this tool was useful for finding a disulphide, please cite: