ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Adenylosuccinate synthetase isozyme 2

Intramolecular
Cysteine 60 and cysteine 280
Cysteine 58 and cysteine 60
Cysteine 60 and cysteine 274
A redox-regulated disulphide may form within Adenylosuccinate synthetase isozyme 2 between cysteines 60 and 280. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
2v40
Structure name
human adenylosuccinate synthetase isozyme 2 in complex with gdp
Structure deposition date
2007-06-27
Thiol separation (Å)
9
Half-sphere exposure sum ?
79
Minimum pKa ?
10
% buried
66
Peptide accession
P30520
Residue number A
60
Residue number B
280
Peptide name
Adenylosuccinate synthetase isozyme 2

Ligandability

Cysteine 60 of Adenylosuccinate synthetase isozyme 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 280 of Adenylosuccinate synthetase isozyme 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 Adenylosuccinate synthetase isozyme 2 between cysteines 58 and 60. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
34
PDB code
2v40
Structure name
human adenylosuccinate synthetase isozyme 2 in complex with gdp
Structure deposition date
2007-06-27
Thiol separation (Å)
8
Half-sphere exposure sum ?
94
Minimum pKa ?
11
% buried
100
Peptide accession
P30520
Residue number A
58
Residue number B
60
Peptide name
Adenylosuccinate synthetase isozyme 2

Ligandability

Cysteine 58 of Adenylosuccinate synthetase isozyme 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 60 of Adenylosuccinate synthetase isozyme 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 Adenylosuccinate synthetase isozyme 2 between cysteines 60 and 274. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
31
PDB code
2v40
Structure name
human adenylosuccinate synthetase isozyme 2 in complex with gdp
Structure deposition date
2007-06-27
Thiol separation (Å)
9
Half-sphere exposure sum ?
94
Minimum pKa ?
11
% buried
98
Peptide accession
P30520
Residue number A
60
Residue number B
274
Peptide name
Adenylosuccinate synthetase isozyme 2

Ligandability

Cysteine 60 of Adenylosuccinate synthetase isozyme 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 274 of Adenylosuccinate synthetase isozyme 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.

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