a tool for identifying drug-targetable redox-active disulphides

glutaminyl-peptide cyclotransferase

Intramolecular

Cysteine 140 and cysteine 165

A redox-regulated disulphide may form within glutaminyl-peptide cyclotransferase between cysteines 140 and 165.

Details

Redox score ?

74

PDB code

Structure name

structure of glycosylated murine glutaminyl cyclase in presence of the inhibitor pq50 (pdbd150)

Structure deposition date

2011-06-17

Thiol separation (Å)

2

Half-sphere exposure sum ?

100

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

140

Residue number B

165

Peptide name

glutaminyl-peptide cyclotransferase

Ligandability

Cysteine 140 of glutaminyl-peptide cyclotransferase

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 165 of glutaminyl-peptide cyclotransferase

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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