Malate dehydrogenase, cytoplasmic

Intermolecular

Intramolecular

A redox-regulated disulphide may form between two units of Malate dehydrogenase, cytoplasmic at cysteines 60 and 251. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

7rrl

Structure name

alternate crystal form of human malate dehydrogenase i

Structure deposition date

2021-08-09

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

100

Peptide A name

Malate dehydrogenase, cytoplasmic

Peptide B name

Malate dehydrogenase, cytoplasmic

Peptide A accession

P40925

Peptide B accession

P40925

Peptide A residue number

Peptide B residue number

251

Ligandability

Cysteine 60 of Malate dehydrogenase, cytoplasmic

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 251 of Malate dehydrogenase, cytoplasmic

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 Malate dehydrogenase, cytoplasmic between cysteines 137 and 154 (136 and 153 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?