› 3nms

X-ray diffraction
4.1Å resolution

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133825 (preferred)
Entry contents:
4 distinct polypeptide molecules
Macromolecules (4 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:
Complement C3c alpha' chain fragment 2 Chain: C
Molecule details ›
Chain: C
Length: 343 amino acids
Theoretical weight: 39.54 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P01024 (Residues: 1321-1663; Coverage: 21%)
Gene names: C3, CPAMD1
Sequence domains:
Staphylococcal complement inhibitor Chain: M
Molecule details ›
Chain: M
Length: 88 amino acids
Theoretical weight: 10.06 KDa
Source organism: Staphylococcus aureus subsp. aureus Mu50
Expression system: Escherichia coli
UniProt:
  • Canonical: Q931M7 (Residues: 32-116; Coverage: 100%)
Gene names: SAV1942, scn
Sequence domains: Staphylococcal complement inhibitor SCIN
Complement C3c alpha' chain fragment 1 Chain: B
Molecule details ›
Chain: B
Length: 206 amino acids
Theoretical weight: 23.62 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P01024 (Residues: 749-954; Coverage: 13%)
Gene names: C3, CPAMD1
Sequence domains:

Ligands and Environments

1 bound ligand:
Ligand NAG 1 x NAG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P21212
Unit cell:
a: 214.067Å b: 68.434Å c: 114.928Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.273 0.271 0.289
Expression system: Escherichia coli

Quick links

Citations

7 review citations

Complement System Part II: Role in Immunity.
Merle et al. (2015)
6 more

1 mention without citation

Molecular basis for complement recognition and inhibition determined by crystallographic studies of the staphylococcal complement inhibitor (SCIN) bound to C3c and C3b.
Garcia et al. (2010)