3erb

X-ray diffraction
1.8Å resolution

The Crystal Structure of C2b, a Fragment of Complement Component C2 produced during C3-convertase Formation

Released:
Source organism: Homo sapiens
Primary publication:
The structure of C2b, a fragment of complement component C2 produced during C3 convertase formation.
Acta Crystallogr D Biol Crystallogr 65 266-74 (2009)
PMID: 19237749

Function and Biology Details

Reaction catalysed:
Selective cleavage of Arg-|-Ser bond in complement component C3 alpha-chain to form C3a and C3b, and Arg-|- bond in complement component C5 alpha-chain to form C5a and C5b.
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-139130 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Complement C2b fragment Chain: A
Molecule details ›
Chain: A
Length: 223 amino acids
Theoretical weight: 23.71 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
UniProt:
  • Canonical: P06681 (Residues: 21-243; Coverage: 31%)
Gene name: C2
Sequence domains: Sushi repeat (SCR repeat)
Structure domains: Complement Module, domain 1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P31
Unit cell:
a: 60.06Å b: 60.06Å c: 61.687Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.216 0.214 0.24
Expression system: Trichoplusia ni