a tool for identifying drug-targetable redox-active disulphides

Leptin

Intramolecular

Cysteine 117 and cysteine 167

A redox-regulated disulphide may form within Leptin between cysteines 117 and 167 (96 and 146 respectively in this structure).

Details

Redox score ?

90

PDB code

Structure name

human obesity protein, leptin

Structure deposition date

1997-10-31

Thiol separation (Å)

2

Half-sphere exposure sum ?

nan

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

117

Residue number B

167

Peptide name

Leptin

Ligandability

Cysteine 117 of Leptin

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 167 of Leptin

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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