› 1dst

X-ray diffraction
2Å resolution

MUTANT OF FACTOR D WITH ENHANCED CATALYTIC ACTIVITY

Released:
DOI: 10.2210/pdb1dst/pdb
PDB entry 1dst coloured by chain, front view.
PDB entry 1dst coloured by chain, side view.
PDB entry 1dst coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of a complement factor D mutant expressing enhanced catalytic activity.
Kim S, Narayana SV, Volanakis JE
J Biol Chem 270 24399-405 (1995)
PMID: 7592653

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: 24.6 KDa
Source organism: Homo sapiens
Expression system: Cricetulus griseus
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: P3121
Unit cell:
a: 45.38Å b: 45.38Å c: 175.21Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
not available not available 0.213
Expression system: Cricetulus griseus

Quick links

Citations

4 review citations

Complement factor D, a novel serine protease.
Volanakis et al. (1996)
3 more

3 mentions without citation

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