ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Rho guanine nucleotide exchange factor 9

Intramolecular
Cysteine 97 and cysteine 99
Cysteine 140 and cysteine 231
Cysteine 205 and cysteine 254
A redox-regulated disulphide may form within Rho guanine nucleotide exchange factor 9 between cysteines 97 and 99 (37 and 39 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
58
PDB code
2dfk
Structure name
crystal structure of the cdc42-collybistin ii complex
Structure deposition date
2006-03-02
Thiol separation (Å)
7
Half-sphere exposure sum ?
nan
Minimum pKa ?
10
% buried
nan
Peptide accession
Q9QX73
Residue number A
97
Residue number B
99
Peptide name
Rho guanine nucleotide exchange factor 9

Ligandability

Cysteine 97 of Rho guanine nucleotide exchange factor 9

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 99 of Rho guanine nucleotide exchange factor 9

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 Rho guanine nucleotide exchange factor 9 between cysteines 140 and 231. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
56
PDB code
4mt6
Structure name
crystal structure of closed inactive collybistin
Structure deposition date
2013-09-19
Thiol separation (Å)
6
Half-sphere exposure sum ?
56
Minimum pKa ?
11
% buried
64
Peptide accession
Q9QX73
Residue number A
140
Residue number B
231
Peptide name
Rho guanine nucleotide exchange factor 9

Ligandability

Cysteine 140 of Rho guanine nucleotide exchange factor 9

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 231 of Rho guanine nucleotide exchange factor 9

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 Rho guanine nucleotide exchange factor 9 between cysteines 205 and 254 (145 and 194 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
2dfk
Structure name
crystal structure of the cdc42-collybistin ii complex
Structure deposition date
2006-03-02
Thiol separation (Å)
7
Half-sphere exposure sum ?
83
Minimum pKa ?
12
% buried
100
Peptide accession
Q9QX73
Residue number A
205
Residue number B
254
Peptide name
Rho guanine nucleotide exchange factor 9

Ligandability

Cysteine 205 of Rho guanine nucleotide exchange factor 9

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 254 of Rho guanine nucleotide exchange factor 9

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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