› 3hs0

X-ray diffraction
3Å resolution

Cobra Venom Factor (CVF) in complex with human factor B

Released:
DOI: 10.2210/pdb3hs0/pdb
PDB entry 3hs0 coloured by chain, front view.
PDB entry 3hs0 coloured by chain, side view.
PDB entry 3hs0 coloured by chain, top view.
Source organisms:
Primary publication:
Insights into complement convertase formation based on the structure of the factor B-cobra venom factor complex.
Janssen BJ, Gomes L, Koning RI, Svergun DI, Koster AJ, Fritzinger DC, Vogel CW, Gros P
EMBO J 28 2469-78 (2009)
PMID: 19574954

Function and Biology Details

Reaction catalysed: 
Cleavage of Arg-|-Ser bond in complement component C3 alpha-chain to yield C3a and C3b, and Arg-|- bond in complement component C5 alpha-chain to yield C5a and C5b.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assemblies composition:
hetero tetramer (preferred)
hetero octamer
Assembly name:
PDBe Complex ID:
PDB-CPX-133306 (preferred)
Entry contents:
4 distinct polypeptide molecules
Macromolecules (5 distinct):
Cobra venom factor alpha chain Chains: A, F
Molecule details ›
Chains: A, F
Length: 627 amino acids
Theoretical weight: 69.58 KDa
Source organism: Naja kaouthia
UniProt:
  • Canonical: Q91132 (Residues: 23-649; Coverage: 39%)
Sequence domains:
Structure domains:
Cobra venom factor gamma chain Chains: B, G
Molecule details ›
Chains: B, G
Length: 252 amino acids
Theoretical weight: 28.42 KDa
Source organism: Naja kaouthia
UniProt:
  • Canonical: Q91132 (Residues: 733-984; Coverage: 16%)
Sequence domains:
Structure domains:
Cobra venom factor beta chain Chains: C, H
Molecule details ›
Chains: C, H
Length: 379 amino acids
Theoretical weight: 43.63 KDa
Source organism: Naja kaouthia
UniProt:
  • Canonical: Q91132 (Residues: 1264-1642; Coverage: 23%)
Sequence domains:
Structure domains:
Complement factor B Chains: D, I
Molecule details ›
Chains: D, I
Length: 741 amino acids
Theoretical weight: 83.19 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: P00751 (Residues: 26-764; Coverage: 100%)
Gene names: BF, BFD, CFB
Sequence domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
2 bound ligands:
Ligand NAG 7 x NAG
Ligand MG 4 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P212121
Unit cell:
a: 134.026Å b: 136.975Å c: 283.74Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.19 0.189 0.243
Expression system: Homo sapiens

Quick links

Citations

10 review citations

Complement System Part I - Molecular Mechanisms of Activation and Regulation.
Merle et al. (2015)
9 more

2 mentions without citation

Insights into complement convertase formation based on the structure of the factor B-cobra venom factor complex.
Janssen et al. (2009)
1 more