a tool for identifying drug-targetable redox-active disulphides

ATP synthase F(0) complex subunit C2, mitochondrial

Intermolecular

Cysteine 132 and cysteine 132

A redox-regulated disulphide may form between two units of ATP synthase F(0) complex subunit C2, mitochondrial at cysteines 132 and 132 (64 and 64 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

32

PDB code

Structure name

bovine atp synthase rotor domain state 2

Structure deposition date

2020-06-18

Thiol separation (Å)

9

Half-sphere exposure sum ?

98

Minimum pK_a ?

12

% buried

100

Peptide A name

ATP synthase F(0) complex subunit C2, mitochondrial

Peptide B name

ATP synthase F(0) complex subunit C2, mitochondrial

Peptide A accession

Peptide B accession

Peptide A residue number

132

Peptide B residue number

132

Ligandability

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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