1elv

X-ray diffraction
1.7Å resolution

CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN COMPLEMENT C1S PROTEASE

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

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-140780 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Complement C1s subcomponent heavy chain Chain: A
Molecule details ›
Chain: A
Length: 333 amino acids
Theoretical weight: 36.69 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P09871 (Residues: 358-688; Coverage: 49%)
Gene name: C1S
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, FUC
2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P21
Unit cell:
a: 39.08Å b: 79.65Å c: 60.21Å
α: 90° β: 91.24° γ: 90°
R-values:
R R work R free
0.186 0.186 0.219
Expression system: Spodoptera frugiperda