ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Genome polyprotein

Intermolecular
Cysteine 100 of Immunoglobulin gamma-1 heavy chain and cysteine 429
Cysteine 100 of Immunoglobulin gamma-1 heavy chain and cysteine 505
A redox-regulated disulphide may form between cysteine 100 of Immunoglobulin gamma-1 heavy chain and cysteine 429 of Genome polyprotein.

Details

Redox score ?
65
PDB code
6bkb
Structure name
structure of hepatitis c virus envelope glycoprotein e2 core from genotype 6a bound to broadly neutralizing antibody ar3a
Structure deposition date
2017-11-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
87
Minimum pKa ?
nan
% buried
nan
Peptide A name
Immunoglobulin gamma-1 heavy chain
Peptide B name
Genome polyprotein
Peptide A accession
P0DOX5
Peptide B accession
B9V0E2
Peptide A residue number
100
Peptide B residue number
429

Ligandability

Cysteine 100 of Immunoglobulin gamma-1 heavy chain

Cysteine 429 of Genome polyprotein

Cysteine 100 in protein A could not be asigned to a Uniprot residue.
A redox-regulated disulphide may form between cysteine 100 of Immunoglobulin gamma-1 heavy chain and cysteine 505 of Genome polyprotein (100 and 503 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
53
PDB code
6bkb
Structure name
structure of hepatitis c virus envelope glycoprotein e2 core from genotype 6a bound to broadly neutralizing antibody ar3a
Structure deposition date
2017-11-08
Thiol separation (Å)
6
Half-sphere exposure sum ?
86
Minimum pKa ?
nan
% buried
nan
Peptide A name
Immunoglobulin gamma-1 heavy chain
Peptide B name
Genome polyprotein
Peptide A accession
P0DOX5
Peptide B accession
B9V0E2
Peptide A residue number
100
Peptide B residue number
505

Ligandability

Cysteine 100 of Immunoglobulin gamma-1 heavy chain

Cysteine 505 of Genome polyprotein

Cysteine 100 in protein A could not be asigned to a Uniprot residue.
If this tool was useful for finding a disulphide, please cite: