a tool for identifying drug-targetable redox-active disulphides

Glycine N-methyltransferase

Intermolecular

Cysteine 58 and cysteine 186

A redox-regulated disulphide may form between two units of Glycine N-methyltransferase at cysteines 58 and 186 (57 and 185 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

39

PDB code

Structure name

crystal structure of mouse glycine n-methyltransferase (monoclinic form)

Structure deposition date

2003-10-28

Thiol separation (Å)

8

Half-sphere exposure sum ?

77

Minimum pK_a ?

11

% buried

81

Peptide A name

Glycine N-methyltransferase

Peptide B name

Glycine N-methyltransferase

Peptide A accession

Peptide B accession

Peptide A residue number

58

Peptide B residue number

186

Ligandability

Cysteine 58 of Glycine N-methyltransferase

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 186 of Glycine N-methyltransferase

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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