ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Complement component C8 gamma chain

Intermolecular
Cysteine 194 of Complement component C8 alpha chain and cysteine 60
Intramolecular
Cysteine 96 and cysteine 188
A redox-regulated disulphide may form between cysteine 194 of Complement component C8 alpha chain and cysteine 60 of Complement component C8 gamma chain (164 and 40 respectively in this structure).

Details

Redox score ?
84
PDB code
2rd7
Structure name
human complement membrane attack proteins share a common fold with bacterial cytolysins
Structure deposition date
2007-09-21
Thiol separation (Å)
2
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide A name
Complement component C8 alpha chain
Peptide B name
Complement component C8 gamma chain
Peptide A accession
P07357
Peptide B accession
P07360
Peptide A residue number
194
Peptide B residue number
60

Ligandability

Cysteine 194 of Complement component C8 alpha chain

Cysteine 60 of Complement component C8 gamma chain

A redox-regulated disulphide may form within Complement component C8 gamma chain between cysteines 96 and 188 (76 and 168 respectively in this structure).

Details

Redox score ?
82
PDB code
1iw2
Structure name
x-ray structure of human complement protein c8gamma at ph=7
Structure deposition date
2002-04-11
Thiol separation (Å)
2
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
P07360
Residue number A
96
Residue number B
188
Peptide name
Complement component C8 gamma chain

Ligandability

Cysteine 96 of Complement component C8 gamma chain

Cysteine 188 of Complement component C8 gamma chain

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