ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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S-formylglutathione hydrolase

Intramolecular
Cysteine 28 and cysteine 88
Cysteine 176 and cysteine 243 L
Cysteine 176 and cysteine 181 L
A redox-regulated disulphide may form within S-formylglutathione hydrolase between cysteines 28 and 88.

Details

Redox score ?
70
PDB code
3fcx
Structure name
crystal structure of human esterase d
Structure deposition date
2008-11-24
Thiol separation (Å)
4
Half-sphere exposure sum ?
47
Minimum pKa ?
11
% buried
49
Peptide accession
P10768
Residue number A
28
Residue number B
88
Peptide name
S-formylglutathione hydrolase

Ligandability

Cysteine 28 of S-formylglutathione hydrolase

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 88 of S-formylglutathione hydrolase

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 S-formylglutathione hydrolase between cysteines 176 and 243. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
3fcx
Structure name
crystal structure of human esterase d
Structure deposition date
2008-11-24
Thiol separation (Å)
8
Half-sphere exposure sum ?
76
Minimum pKa ?
12
% buried
84
Peptide accession
P10768
Residue number A
176
Residue number B
243
Peptide name
S-formylglutathione hydrolase

Ligandability

Cysteine 176 of S-formylglutathione hydrolase

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 243 of S-formylglutathione hydrolase

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 S-formylglutathione hydrolase between cysteines 176 and 181. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
34
PDB code
3fcx
Structure name
crystal structure of human esterase d
Structure deposition date
2008-11-24
Thiol separation (Å)
10
Half-sphere exposure sum ?
71
Minimum pKa ?
11
% buried
90
Peptide accession
P10768
Residue number A
176
Residue number B
181
Peptide name
S-formylglutathione hydrolase

Ligandability

Cysteine 176 of S-formylglutathione hydrolase

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 181 of S-formylglutathione hydrolase

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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