a tool for identifying drug-targetable redox-active disulphides

Interleukin-2

Intramolecular

Cysteine 78 and cysteine 125

A redox-regulated disulphide may form within Interleukin-2 between cysteines 78 and 125 (58 and 105 respectively in this structure).

Details

Redox score ?

68

PDB code

Structure name

crystal structure of human interleukin-2 y31c covalently modified at c31 with (1h-indol-3-yl)-(2-mercapto-ethoxyimino)-acetic acid

Structure deposition date

2002-07-02

Thiol separation (Å)

5

Half-sphere exposure sum ?

54

Minimum pK_a ?

10

% buried

18

Peptide accession

Residue number A

78

Residue number B

125

Peptide name

Interleukin-2

Ligandability

Cysteine 78 of Interleukin-2

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 125 of Interleukin-2

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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