› 1dsu

X-ray diffraction
2Å resolution

HUMAN FACTOR D, COMPLEMENT ACTIVATING ENZYME

Released:
DOI: 10.2210/pdb1dsu/pdb
PDB entry 1dsu coloured by chain, front view.
PDB entry 1dsu coloured by chain, side view.
PDB entry 1dsu coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure of human factor D. A complement system protein at 2.0 A resolution.
Narayana SV, Carson M, el-Kabbani O, Kilpatrick JM, Moore D, Chen X, Bugg CE, Volanakis JE, DeLucas LJ
J Mol Biol 235 695-708 (1994)
PMID: 8289289

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:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133229 (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: 24.44 KDa
Source organism: 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

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

Quick links

Citations

17 review citations

Structural basis of substrate specificity in the serine proteases.
Perona et al. (1995)
16 more

10 mentions without citation

Allostery in trypsin-like proteases suggests new therapeutic strategies.
Gohara et al. (2011)
9 more