a tool for identifying drug-targetable redox-active disulphides

fructose-bisphosphatase

Intermolecular

Cysteine 129 and cysteine 184

A redox-regulated disulphide may form between two units of fructose-bisphosphatase at cysteines 129 and 184 (128 and 183 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

31

PDB code

Structure name

structure of human liver fbpase complexed with covalent allosteric inhibitor

Structure deposition date

2020-01-17

Thiol separation (Å)

9

Half-sphere exposure sum ?

71

Minimum pK_a ?

13

% buried

nan

Peptide A name

fructose-bisphosphatase

Peptide B name

fructose-bisphosphatase

Peptide A accession

Peptide B accession

Peptide A residue number

129

Peptide B residue number

184

Ligandability

Cysteine 129 of fructose-bisphosphatase

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 184 of fructose-bisphosphatase

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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