a tool for identifying drug-targetable redox-active disulphides

Retinol-binding protein 1

Intramolecular

Cysteine 83 and cysteine 96

A redox-regulated disulphide may form within Retinol-binding protein 1 between cysteines 83 and 96 (82 and 95 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

41

PDB code

Structure name

crystal structure of human cellular retinol-binding protein 1 in complex with cannabidiorcin (cbdo)

Structure deposition date

2018-07-25

Thiol separation (Å)

8

Half-sphere exposure sum ?

70

Minimum pK_a ?

11

% buried

88

Peptide accession

Residue number A

83

Residue number B

96

Peptide name

Retinol-binding protein 1

Ligandability

Cysteine 83 of Retinol-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 96 of Retinol-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.

If this tool was useful for finding a disulphide, please cite: