a tool for identifying drug-targetable redox-active disulphides

Serine hydroxymethyltransferase, mitochondrial

Intermolecular

Cysteine 91 and cysteine 68

A redox-regulated disulphide may form between two units of Serine hydroxymethyltransferase, mitochondrial at cysteines 91 and 68 (70 and 47 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

42

PDB code

Structure name

structure of human shmt2 protein mutant

Structure deposition date

2017-02-09

Thiol separation (Å)

8

Half-sphere exposure sum ?

84

Minimum pK_a ?

10

% buried

84

Peptide A name

Serine hydroxymethyltransferase, mitochondrial

Peptide B name

Serine hydroxymethyltransferase, mitochondrial

Peptide A accession

Peptide B accession

Peptide A residue number

91

Peptide B residue number

68

Ligandability

Cysteine 91 of Serine hydroxymethyltransferase, mitochondrial

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 68 of Serine hydroxymethyltransferase, mitochondrial

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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