a tool for identifying drug-targetable redox-active disulphides

Mitochondrial chaperone BCS1

Intramolecular

Cysteine 234 and cysteine 356

A redox-regulated disulphide may form within Mitochondrial chaperone BCS1 between cysteines 234 and 356 (1234 and 1356 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

43

PDB code

Structure name

structure analysis of full-length mouse bcs1 complex

Structure deposition date

2019-10-05

Thiol separation (Å)

9

Half-sphere exposure sum ?

61

Minimum pK_a ?

11

% buried

58

Peptide accession

Residue number A

234

Residue number B

356

Peptide name

Mitochondrial chaperone BCS1

Ligandability

Cysteine 234 of Mitochondrial chaperone BCS1

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 356 of Mitochondrial chaperone BCS1

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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