ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Hsp90 co-chaperone Cdc37

Intramolecular
Cysteine 382 and cysteine 404
A redox-regulated disulphide may form within Hsp90 co-chaperone Cdc37 between cysteines 382 and 404.

Details

Redox score ?
nan
PDB code
5hpe
Structure name
phosphatase domain of pp5 bound to a phosphomimetic cdc37 substrate peptide
Structure deposition date
2016-01-20
Thiol separation (Å)
9
Half-sphere exposure sum ?
71
Minimum pKa ?
11
% buried
61
Peptide accession
K7EJ06
Residue number A
382
Residue number B
404
Peptide name
Hsp90 co-chaperone Cdc37

Ligandability

Cysteine 382 of Hsp90 co-chaperone Cdc37

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 404 of Hsp90 co-chaperone Cdc37

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 382 in protein A could not be asigned to a Uniprot residue.
Cysteine 404 in protein B could not be asigned to a Uniprot residue.
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