1md8

X-ray diffraction
2.8Å resolution

Monomeric structure of the active catalytic domain of complement protease C1r

Released:

Function and Biology Details

Reaction catalysed:
Selective cleavage of Lys(or Arg)-|-Ile bond in complement subcomponent C1s to form C1s (EC 3.4.21.42).
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-133182 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Complement C1r subcomponent heavy chain Chain: A
Molecule details ›
Chain: A
Length: 329 amino acids
Theoretical weight: 37.2 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
UniProt:
  • Canonical: P00736 (Residues: 375-703; Coverage: 48%)
Gene name: C1R
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM30A
Spacegroup: C2
Unit cell:
a: 112.911Å b: 49.459Å c: 77.249Å
α: 90° β: 106.19° γ: 90°
R-values:
R R work R free
0.204 0.198 0.269
Expression system: Trichoplusia ni