ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Vesicle-associated membrane protein-associated protein B/C

Intermolecular
Cysteine 53 and cysteine 53
Intramolecular
Cysteine 53 and cysteine 121
A redox-regulated disulphide may form between two units of Vesicle-associated membrane protein-associated protein B/C at cysteines 53 and 53.

Details

Redox score ?
78
PDB code
3ikk
Structure name
crystal structure analysis of msp domain
Structure deposition date
2009-08-06
Thiol separation (Å)
2
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide A name
Vesicle-associated membrane protein-associated protein B/C
Peptide B name
Vesicle-associated membrane protein-associated protein B/C
Peptide A accession
O95292
Peptide B accession
O95292
Peptide A residue number
53
Peptide B residue number
53

Ligandability

A redox-regulated disulphide may form within Vesicle-associated membrane protein-associated protein B/C between cysteines 53 and 121. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
2mdk
Structure name
nmr solution structure of msp-p56s domain/vapb in dpc
Structure deposition date
2013-09-11
Thiol separation (Å)
10
Half-sphere exposure sum ?
38
Minimum pKa ?
10
% buried
20
Peptide accession
O95292
Residue number A
53
Residue number B
121
Peptide name
Vesicle-associated membrane protein-associated protein B/C

Ligandability

Cysteine 53 of Vesicle-associated membrane protein-associated protein B/C

Cysteine 121 of Vesicle-associated membrane protein-associated protein B/C

If this tool was useful for finding a disulphide, please cite: