› 5fo8

X-ray diffraction
2.4Å resolution

Crystal Structure of Human Complement C3b in Complex with MCP (CCP1-4)

Released:
DOI: 10.2210/pdb5fo8/pdb
Model geometry
Fit model/data
PDB entry 5fo8 coloured by chain, front view.
PDB entry 5fo8 coloured by chain, side view.
PDB entry 5fo8 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Regulators of complement activity mediate inhibitory mechanisms through a common C3b-binding mode.
Forneris F, Wu J, Xue X, Ricklin D, Lin Z, Sfyroera G, Tzekou A, Volokhina E, Granneman JC, Hauhart R, Bertram P, Liszewski MK, Atkinson JP, Lambris JD, Gros P
OpenAccess logo EMBO J 35 1133-49 (2016)
PMID: 27013439

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:
  • not assigned
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133829 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (5 distinct):
Complement C3 beta chain Chain: A
Molecule details ›
Chain: A
Length: 645 amino acids
Theoretical weight: 71.39 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P01024 (Residues: 23-667; Coverage: 39%)
Gene names: C3, CPAMD1
Sequence domains:
Structure domains:
Complement C3b Chain: B
Molecule details ›
Chain: B
Length: 915 amino acids
Theoretical weight: 104.07 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P01024 (Residues: 749-1663; Coverage: 56%)
Gene names: C3, CPAMD1
Sequence domains:
Structure domains:
Membrane cofactor protein Chain: C

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, BMA
Carbohydrate polymer
1 bound ligand:
Ligand EDO 32 x EDO
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: ESRF BEAMLINE ID29
Unit cell:
a: 82.83Å b: 130.63Å c: 233.83Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.19 0.188 0.219
Expression system: Escherichia coli

Quick links

Citations

24 review citations

Novel mechanisms and functions of complement.
Hajishengallis et al. (2017)
23 more

7 mentions without citation

Complement component C3: A structural perspective and potential therapeutic implications.
Geisbrecht et al. (2022)
6 more