Pyruvate dehydrogenase E1 component subunit beta, mitochondrial

Intermolecular

Intramolecular

A redox-regulated disulphide may form between two units of Pyruvate dehydrogenase E1 component subunit beta, mitochondrial at cysteines 306 and 306 (276 and 276 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

3exg

Structure name

crystal structure of the pyruvate dehydrogenase (e1p) component of human pyruvate dehydrogenase complex

Structure deposition date

2008-10-16

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

100

Peptide A name

Pyruvate dehydrogenase E1 component subunit beta, mitochondrial

Peptide B name

Pyruvate dehydrogenase E1 component subunit beta, mitochondrial

Peptide A accession

P11177

Peptide B accession

P11177

Peptide A residue number

306

Peptide B residue number

306

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Pyruvate dehydrogenase E1 component subunit beta, mitochondrial between cysteines 249 and 263 (219 and 233 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?