Inosine-5'-monophosphate dehydrogenase 1

Intermolecular

Intramolecular

A redox-regulated disulphide may form between two units of Inosine-5'-monophosphate dehydrogenase 1 at cysteines 339 and 468. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

7rfe

Structure name

human impdh1 treated with gtp, imp, and nad+; interface-centered

Structure deposition date

2021-07-14

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

100

Peptide A name

Inosine-5'-monophosphate dehydrogenase 1

Peptide B name

Inosine-5'-monophosphate dehydrogenase 1

Peptide A accession

P20839

Peptide B accession

P20839

Peptide A residue number

339

Peptide B residue number

468

Ligandability

Cysteine 339 of Inosine-5'-monophosphate dehydrogenase 1

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 468 of Inosine-5'-monophosphate dehydrogenase 1

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 Isoform 5 of Inosine-5'-monophosphate dehydrogenase 1 between cysteines 402 and 406 (327 and 331 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?