PDBe 1dsu

X-ray diffraction
2Å resolution

HUMAN FACTOR D, COMPLEMENT ACTIVATING ENZYME

Released:

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:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
FACTOR D Chains: A, B
Molecule details ›
Chains: A, B
Length: 228 amino acids
Theoretical weight: 24.44 KDa
Source organism: Homo sapiens
Structure domains: Trypsin-like serine proteases

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P1
Unit cell:
a: 40.99Å b: 65.02Å c: 40.36Å
α: 101.26° β: 109.89° γ: 74.32°
R-values:
R R work R free
0.188 0.188 0.203