ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Methylthioribulose-1-phosphate dehydratase

Intramolecular
Cysteine 147 and cysteine 188 L
Cysteine 32 and cysteine 97
Cysteine 211 and cysteine 213
A redox-regulated disulphide may form within Methylthioribulose-1-phosphate dehydratase between cysteines 147 and 188.

Details

Redox score ?
75
PDB code
4m6r
Structure name
structural and biochemical basis for the inhibition of cell death by apip, a methionine salvage enzyme
Structure deposition date
2013-08-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
80
Minimum pKa ?
6
% buried
70
Peptide accession
Q96GX9
Residue number A
147
Residue number B
188
Peptide name
Methylthioribulose-1-phosphate dehydratase

Ligandability

Cysteine 147 of Methylthioribulose-1-phosphate dehydratase

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 188 of Methylthioribulose-1-phosphate dehydratase

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 Methylthioribulose-1-phosphate dehydratase between cysteines 32 and 97. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
4m6r
Structure name
structural and biochemical basis for the inhibition of cell death by apip, a methionine salvage enzyme
Structure deposition date
2013-08-10
Thiol separation (Å)
10
Half-sphere exposure sum ?
73
Minimum pKa ?
8
% buried
100
Peptide accession
Q96GX9
Residue number A
32
Residue number B
97
Peptide name
Methylthioribulose-1-phosphate dehydratase

Ligandability

Cysteine 32 of Methylthioribulose-1-phosphate dehydratase

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 97 of Methylthioribulose-1-phosphate dehydratase

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 Methylthioribulose-1-phosphate dehydratase between cysteines 211 and 213. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
27
PDB code
4m6r
Structure name
structural and biochemical basis for the inhibition of cell death by apip, a methionine salvage enzyme
Structure deposition date
2013-08-10
Thiol separation (Å)
10
Half-sphere exposure sum ?
83
Minimum pKa ?
13
% buried
100
Peptide accession
Q96GX9
Residue number A
211
Residue number B
213
Peptide name
Methylthioribulose-1-phosphate dehydratase

Ligandability

Cysteine 211 of Methylthioribulose-1-phosphate dehydratase

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 213 of Methylthioribulose-1-phosphate dehydratase

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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