ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Ig gamma-1 chain C region, membrane-bound form

Intermolecular
Cysteine 107 of Immunoglobulin kappa constant and cysteine 102
Intramolecular
Cysteine 244 and cysteine 92
A redox-regulated disulphide may form between cysteine 107 of Immunoglobulin kappa constant and cysteine 102 of Ig gamma-1 chain C region, membrane-bound form (213 and 218 respectively in this structure).

Details

Redox score ?
88
PDB code
1kcr
Structure name
crystal structure of antibody pc283 in complex with ps1 peptide
Structure deposition date
2001-11-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
nan
Minimum pKa ?
9
% buried
0
Peptide A name
Immunoglobulin kappa constant
Peptide B name
Ig gamma-1 chain C region, membrane-bound form
Peptide A accession
P01837
Peptide B accession
P01869
Peptide A residue number
107
Peptide B residue number
102

Ligandability

Cysteine 107 of Immunoglobulin kappa constant

Cysteine 102 of Ig gamma-1 chain C region, membrane-bound form

A redox-regulated disulphide may form within Ig gamma-1 chain C region, membrane-bound form between cysteines 244 and 92 (22 and 92 respectively in this structure).

Details

Redox score ?
nan
PDB code
1acy
Structure name
crystal structure of the principal neutralizing site of hiv- 1
Structure deposition date
1994-02-10
Thiol separation (Å)
2
Half-sphere exposure sum ?
85
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01869
Residue number A
244
Residue number B
92
Peptide name
Ig gamma-1 chain C region, membrane-bound form

Ligandability

Cysteine 244 of Ig gamma-1 chain C region, membrane-bound form

Cysteine 92 of Ig gamma-1 chain C region, membrane-bound form

Cysteine 92 in protein B could not be asigned to a Uniprot residue.
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