ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Gamma-interferon-inducible protein 16

Intramolecular
Cysteine 351 and cysteine 366
A redox-regulated disulphide may form within Gamma-interferon-inducible protein 16 between cysteines 351 and 366 (164 and 179 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
PDB code
2oq0
Structure name
crystal structure of the first hin-200 domain of interferon-inducible protein 16
Structure deposition date
2007-01-30
Thiol separation (Å)
9
Half-sphere exposure sum ?
75
Minimum pKa ?
11
% buried
96
Peptide accession
Q16666
Residue number A
351
Residue number B
366
Peptide name
Gamma-interferon-inducible protein 16

Ligandability

Cysteine 351 of Gamma-interferon-inducible protein 16

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 366 of Gamma-interferon-inducible protein 16

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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