ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Omega-amidase NIT2

Intramolecular
Cysteine 146 and cysteine 170
A redox-regulated disulphide may form within Omega-amidase NIT2 between cysteines 146 and 170 (184 and 208 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
2w1v
Structure name
crystal structure of mouse nitrilase-2 at 1
Structure deposition date
2008-10-21
Thiol separation (Å)
8
Half-sphere exposure sum ?
65
Minimum pKa ?
12
% buried
76
Peptide accession
Q9JHW2
Residue number A
146
Residue number B
170
Peptide name
Omega-amidase NIT2

Ligandability

Cysteine 146 of Omega-amidase NIT2

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 170 of Omega-amidase NIT2

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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