› 1bio

X-ray diffraction
1.5Å resolution

HUMAN COMPLEMENT FACTOR D IN COMPLEX WITH ISATOIC ANHYDRIDE INHIBITOR

Released:
DOI: 10.2210/pdb1bio/pdb
PDB entry 1bio coloured by chain, front view.
PDB entry 1bio coloured by chain, side view.
PDB entry 1bio coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structures of native and complexed complement factor D: implications of the atypical His57 conformation and self-inhibitory loop in the regulation of specific serine protease activity.
Jing H, Babu YS, Moore D, Kilpatrick JM, Liu XY, Volanakis JE, Narayana SV
J Mol Biol 282 1061-81 (1998)
PMID: 9753554

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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133224 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Complement factor D Chain: A
Molecule details ›
Chain: A
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

2 bound ligands:
Ligand SOA 1 x SOA
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P21
Unit cell:
a: 55.48Å b: 49.91Å c: 39.43Å
α: 90° β: 105.69° γ: 90°
R-values:
R R work R free
0.186 0.186 0.191

Quick links

Citations

10 review citations

Complement driven by conformational changes.
Gros et al. (2008)
9 more

10 mentions without citation

Coupling between catalytic site and collective dynamics: a requirement for mechanochemical activity of enzymes.
Yang et al. (2005)
9 more