› 1fdp

X-ray diffraction
2.1Å resolution

PROENZYME OF HUMAN COMPLEMENT FACTOR D, RECOMBINANT PROFACTOR D

Released:
DOI: 10.2210/pdb1fdp/pdb
PDB entry 1fdp coloured by chain, front view.
PDB entry 1fdp coloured by chain, side view.
PDB entry 1fdp coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis of profactor D activation: from a highly flexible zymogen to a novel self-inhibited serine protease, complement factor D.
Jing H, Macon KJ, Moore D, DeLucas LJ, Volanakis JE, Narayana SV
EMBO J 18 804-14 (1999)
PMID: 10022823

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:
  • not assigned
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 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 235 amino acids
Theoretical weight: 25.15 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P00746 (Residues: 19-253; Coverage: 100%)
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
X-ray source: RIGAKU RU200
Spacegroup: P21
Unit cell:
a: 65.05Å b: 70.32Å c: 86.3Å
α: 90° β: 101.98° γ: 90°
R-values:
R R work R free
0.204 0.204 0.251
Expression system: Spodoptera frugiperda

Quick links

Citations

7 review citations

Role of Ras and Mapks in TGFbeta signaling.
Mulder KM. (2000)
6 more

2 mentions without citation

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