a tool for identifying drug-targetable redox-active disulphides

Pepsin A

Intramolecular

Cysteine 104 and cysteine 109

A redox-regulated disulphide may form within Pepsin A between cysteines 104 and 109 (45 and 50 respectively in this structure).

Details

Redox score ?

89

PDB code

Structure name

the high resolution crystal structure of porcine pepsinogen

Structure deposition date

1991-09-03

Thiol separation (Å)

2

Half-sphere exposure sum ?

60

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

104

Residue number B

109

Peptide name

Pepsin A

Ligandability

Cysteine 104 of Pepsin A

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 109 of Pepsin A

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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