1nzi

X-ray diffraction
1.5Å resolution

Crystal Structure of the CUB1-EGF Interaction Domain of Complement Protease C1s

Released:

Function and Biology Details

Reaction catalysed:
Cleavage of Arg-|-Ala bond in complement component C4 to form C4a and C4b, and Lys(or Arg)-|-Lys bond in complement component C2 to form C2a and C2b: the 'classical' pathway C3 convertase.
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-140783 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Complement C1s subcomponent heavy chain Chains: A, B
Molecule details ›
Chains: A, B
Length: 159 amino acids
Theoretical weight: 18.14 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
UniProt:
  • Canonical: P09871 (Residues: 16-174; Coverage: 24%)
Gene name: C1S
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P1
Unit cell:
a: 35.134Å b: 47.499Å c: 56.679Å
α: 87.74° β: 78.04° γ: 75.67°
R-values:
R R work R free
0.217 0.216 0.234
Expression system: Trichoplusia ni