ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Cytohesin-1

Intramolecular
Cysteine 173 and cysteine 186
Cysteine 175 and cysteine 186
Cysteine 173 and cysteine 175
A redox-regulated disulphide may form within Cytohesin-1 between cysteines 173 and 186 (177 and 190 respectively in this structure).

Details

Redox score ?
74
PDB code
4a4p
Structure name
crystal structure of the sec7 domain from human cytohesin1
Structure deposition date
2011-10-19
Thiol separation (Å)
4
Half-sphere exposure sum ?
67
Minimum pKa ?
7
% buried
69
Peptide accession
Q15438
Residue number A
173
Residue number B
186
Peptide name
Cytohesin-1

Ligandability

Cysteine 173 of Cytohesin-1

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 186 of Cytohesin-1

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-1 between cysteines 175 and 186. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
58
PDB code
1bc9
Structure name
cytohesin-1/b2-1 sec7 domain, nmr, minimized average structure
Structure deposition date
1998-05-06
Thiol separation (Å)
6
Half-sphere exposure sum ?
66
Minimum pKa ?
10
% buried
60
Peptide accession
Q15438
Residue number A
175
Residue number B
186
Peptide name
Cytohesin-1

Ligandability

Cysteine 175 of Cytohesin-1

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 186 of Cytohesin-1

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-1 between cysteines 173 and 175 (177 and 179 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
4a4p
Structure name
crystal structure of the sec7 domain from human cytohesin1
Structure deposition date
2011-10-19
Thiol separation (Å)
9
Half-sphere exposure sum ?
56
Minimum pKa ?
7
% buried
38
Peptide accession
Q15438
Residue number A
173
Residue number B
175
Peptide name
Cytohesin-1

Ligandability

Cysteine 173 of Cytohesin-1

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 175 of Cytohesin-1

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.

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