L-lactate dehydrogenase C chain

Intermolecular

Intramolecular

A redox-regulated disulphide may form between two units of L-lactate dehydrogenase C chain at cysteines 21 and 21 (20 and 20 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

2ldx

Structure name

characterization of the antigenic sites on the refined 3- angstroms resolution structure of mouse testicular lactate dehydrogenase c4

Structure deposition date

1987-11-25

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide A name

L-lactate dehydrogenase C chain

Peptide B name

L-lactate dehydrogenase C chain

Peptide A accession

P00342

Peptide B accession

P00342

Peptide A residue number

Peptide B residue number

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.

A redox-regulated disulphide may form within L-lactate dehydrogenase C chain between cysteines 163 and 293 (162 and 292 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?