a tool for identifying drug-targetable redox-active disulphides

Far upstream element-binding protein 1

Intramolecular

Cysteine 132 and cysteine 148

A redox-regulated disulphide may form within Far upstream element-binding protein 1 between cysteines 132 and 148 (131 and 147 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

39

PDB code

Structure name

crystal structure of a far upstream element (fuse) binding protein 1 (fubp1) from homo sapiens at 1

Structure deposition date

2013-07-02

Thiol separation (Å)

10

Half-sphere exposure sum ?

nan

Minimum pK_a ?

11

% buried

51

Peptide accession

Residue number A

132

Residue number B

148

Peptide name

Far upstream element-binding protein 1

Ligandability

Cysteine 132 of Far upstream element-binding protein 1

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 148 of Far upstream element-binding protein 1

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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