a tool for identifying drug-targetable redox-active disulphides

Gamma-glutamylaminecyclotransferase

Intramolecular

Cysteine 35 and cysteine 62

A redox-regulated disulphide may form within Gamma-glutamylaminecyclotransferase between cysteines 35 and 62.

Details

Redox score ?

61

PDB code

Structure name

nmr solution structure of a2ld1 (gi:13879369)

Structure deposition date

2009-06-30

Thiol separation (Å)

6

Half-sphere exposure sum ?

63

Minimum pK_a ?

10

% buried

17

Peptide accession

Residue number A

35

Residue number B

62

Peptide name

Gamma-glutamylaminecyclotransferase

Ligandability

Cysteine 35 of Gamma-glutamylaminecyclotransferase

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 62 of Gamma-glutamylaminecyclotransferase

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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