› 1dle

X-ray diffraction
2.1Å resolution

FACTOR B SERINE PROTEASE DOMAIN

Released:
DOI: 10.2210/pdb1dle/pdb
PDB entry 1dle coloured by chain, front view.
PDB entry 1dle coloured by chain, side view.
PDB entry 1dle coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
New structural motifs on the chymotrypsin fold and their potential roles in complement factor B.
Jing H, Xu Y, Carson M, Moore D, Macon KJ, Volanakis JE, Narayana SV
EMBO J 19 164-73 (2000)
PMID: 10637221

Function and Biology Details

Reaction catalysed: 
Cleavage of Arg-|-Ser bond in complement component C3 alpha-chain to yield C3a and C3b, and Arg-|- bond in complement component C5 alpha-chain to yield C5a and C5b.
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-133307 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Complement factor B Bb fragment Chains: A, B
Molecule details ›
Chains: A, B
Length: 298 amino acids
Theoretical weight: 33.7 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P00751 (Residues: 470-764; Coverage: 40%)
Gene names: BF, BFD, CFB
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
Spacegroup: P21
Unit cell:
a: 51.643Å b: 74.259Å c: 73.258Å
α: 90° β: 95.55° γ: 90°
R-values:
R R work R free
0.21 0.209 0.249

Quick links

Citations

5 review citations

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

12 mentions without citation

Could a Non-Cellular Molecular Interactome in the Blood Circulation Influence Pathogens' Infectivity?
Hardy et al. (2023)
11 more