Hsp90 co-chaperone Cdc37
2nca A 54 A 57
A redox-regulated disulphide may form within Hsp90 co-chaperone Cdc37 between cysteines 54 and 57. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
57
PDB code
2nca
Structure name
structural model for the n-terminal domain of human cdc37
Structure deposition date
2016-03-23
Thiol separation (Å)
8
Half-sphere exposure sum ?
45
Minimum pKa ?
9
% buried
3
Peptide accession
Q16543
Residue number A
54
Residue number B
57
Peptide name
Hsp90 co-chaperone Cdc37
Ligandability
Cysteine 54 of Hsp90 co-chaperone Cdc37
Cysteine 57 of Hsp90 co-chaperone Cdc37
2nca A 57 A 64
A redox-regulated disulphide may form within Hsp90 co-chaperone Cdc37 between cysteines 57 and 64. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
2nca
Structure name
structural model for the n-terminal domain of human cdc37
Structure deposition date
2016-03-23
Thiol separation (Å)
10
Half-sphere exposure sum ?
48
Minimum pKa ?
9
% buried
3
Peptide accession
Q16543
Residue number A
57
Residue number B
64
Peptide name
Hsp90 co-chaperone Cdc37
Ligandability
Cysteine 57 of Hsp90 co-chaperone Cdc37
Cysteine 64 of Hsp90 co-chaperone Cdc37
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