ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Alanine aminotransferase 2

Intramolecular
Cysteine 240 and cysteine 311
Cysteine 142 and cysteine 158
Cysteine 467 and cysteine 477
A redox-regulated disulphide may form within Alanine aminotransferase 2 between cysteines 240 and 311. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
55
PDB code
3ihj
Structure name
human alanine aminotransferase 2 in complex with plp
Structure deposition date
2009-07-30
Thiol separation (Å)
8
Half-sphere exposure sum ?
52
Minimum pKa ?
10
% buried
38
Peptide accession
Q8TD30
Residue number A
240
Residue number B
311
Peptide name
Alanine aminotransferase 2

Ligandability

Cysteine 240 of Alanine aminotransferase 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 311 of Alanine aminotransferase 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 Alanine aminotransferase 2 between cysteines 142 and 158. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
51
PDB code
3ihj
Structure name
human alanine aminotransferase 2 in complex with plp
Structure deposition date
2009-07-30
Thiol separation (Å)
9
Half-sphere exposure sum ?
nan
Minimum pKa ?
9
% buried
11
Peptide accession
Q8TD30
Residue number A
142
Residue number B
158
Peptide name
Alanine aminotransferase 2

Ligandability

Cysteine 142 of Alanine aminotransferase 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 158 of Alanine aminotransferase 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 Alanine aminotransferase 2 between cysteines 467 and 477. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
3ihj
Structure name
human alanine aminotransferase 2 in complex with plp
Structure deposition date
2009-07-30
Thiol separation (Å)
9
Half-sphere exposure sum ?
77
Minimum pKa ?
10
% buried
80
Peptide accession
Q8TD30
Residue number A
467
Residue number B
477
Peptide name
Alanine aminotransferase 2

Ligandability

Cysteine 467 of Alanine aminotransferase 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 477 of Alanine aminotransferase 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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