ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Carbonic anhydrase 2

Intramolecular
Cysteine 23 and cysteine 203
A redox-regulated disulphide may form within Carbonic anhydrase 2 between cysteines 23 and 203.

Details

Redox score ?
nan
PDB code
4hba
Structure name
structural and catalytic characterization of a thermal and acid stable variant of human carbonic anhydrase ii containing an engineered disulfide bond
Structure deposition date
2012-09-27
Thiol separation (Å)
2
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00918
Residue number A
23
Residue number B
203
Peptide name
Carbonic anhydrase 2

Ligandability

Cysteine 23 of Carbonic anhydrase 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 203 of Carbonic anhydrase 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 23 in protein A could not be asigned to a Uniprot residue.
Cysteine 203 in protein B could not be asigned to a Uniprot residue.
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