a tool for identifying drug-targetable redox-active disulphides

Glutaminyl-peptide cyclotransferase-like protein

Intramolecular

Cysteine 167 and cysteine 191

A redox-regulated disulphide may form within Glutaminyl-peptide cyclotransferase-like protein between cysteines 167 and 191.

Details

Redox score ?

66

PDB code

Structure name

crystal structure of the catalytic domain of human golgi-resident glutaminyl cyclase in complex with 1-benzylimidazole

Structure deposition date

2010-10-20

Thiol separation (Å)

4

Half-sphere exposure sum ?

98

Minimum pK_a ?

8

% buried

100

Peptide accession

Residue number A

167

Residue number B

191

Peptide name

Glutaminyl-peptide cyclotransferase-like protein

Ligandability

Cysteine 167 of Glutaminyl-peptide cyclotransferase-like protein

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 191 of Glutaminyl-peptide cyclotransferase-like protein

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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