PDBe 4cbo

X-ray diffraction
1.8Å resolution

Crystal structure of Complement Factor D mutant R202A after ensemble refinement

Released:
Source organism: Homo sapiens
Primary publication:
Ensemble refinement shows conformational flexibility in crystal structures of human complement factor D.
OpenAccess logo Acta Crystallogr. D Biol. Crystallogr. 70 733-43 (2014)
PMID: 24598742

Function and Biology Details

Reaction catalysed:
Selective cleavage of Arg-|-Lys bond in complement factor B when in complex with complement subcomponent C3b or with cobra venom factor.
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Complement factor D Chains: A, B
Molecule details ›
Chains: A, B
Length: 228 amino acids
Theoretical weight: 24.35 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: P00746 (Residues: 26-253; Coverage: 98%)
Gene names: CFD, DF, PFD
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P212121
Unit cell:
a: 44.14Å b: 67.31Å c: 133.14Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.166 0.163 0.212
Expression system: Homo sapiens