4j1y

X-ray diffraction
2.66Å resolution

The X-ray crystal structure of human complement protease C1s zymogen

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:
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
PDBe Complex ID:
PDB-CPX-140780 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Complement C1s subcomponent heavy chain Chains: A, B
Molecule details ›
Chains: A, B
Length: 397 amino acids
Theoretical weight: 43.77 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P09871 (Residues: 292-688; Coverage: 59%)
Gene name: C1S
Sequence domains:
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: AUSTRALIAN SYNCHROTRON BEAMLINE MX2
Spacegroup: C222
Unit cell:
a: 149.89Å b: 158.9Å c: 78.7Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.203 0.2 0.259
Expression system: Escherichia coli