ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Rho GTPase-activating protein 21

Intramolecular
Cysteine 1016 and cysteine 1018
Cysteine 994 and cysteine 1018
Cysteine 994 and cysteine 1016
A redox-regulated disulphide may form within Rho GTPase-activating protein 21 between cysteines 1016 and 1018 (1015 and 1017 respectively in this structure).

Details

Redox score ?
75
PDB code
2j59
Structure name
crystal structure of the arf1:arhgap21-arfbd complex
Structure deposition date
2006-09-13
Thiol separation (Å)
4
Half-sphere exposure sum ?
53
Minimum pKa ?
7
% buried
60
Peptide accession
Q8NI19
Residue number A
1016
Residue number B
1018
Peptide name
Rho GTPase-activating protein 21

Ligandability

Cysteine 1016 of Rho GTPase-activating protein 21

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 1018 of Rho GTPase-activating protein 21

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 GTPase-activating protein 21 between cysteines 994 and 1018 (71 and 95 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
2dhj
Structure name
solution structure of the ph domain of rho gtpase activating protein 21 from human
Structure deposition date
2006-03-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
64
Minimum pKa ?
10
% buried
68
Peptide accession
Q7Z3P7
Residue number A
994
Residue number B
1018
Peptide name
Rho GTPase-activating protein 21

Ligandability

Cysteine 994 of Rho GTPase-activating protein 21

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 1018 of Rho GTPase-activating protein 21

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 GTPase-activating protein 21 between cysteines 994 and 1016 (993 and 1015 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
2j59
Structure name
crystal structure of the arf1:arhgap21-arfbd complex
Structure deposition date
2006-09-13
Thiol separation (Å)
9
Half-sphere exposure sum ?
63
Minimum pKa ?
9
% buried
64
Peptide accession
Q8NI19
Residue number A
994
Residue number B
1016
Peptide name
Rho GTPase-activating protein 21

Ligandability

Cysteine 994 of Rho GTPase-activating protein 21

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 1016 of Rho GTPase-activating protein 21

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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