› 1md7

X-ray diffraction
3.2Å resolution

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
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
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: 328 amino acids
Theoretical weight: 37.05 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
UniProt:
  • Canonical: P00736 (Residues: 375-702; Coverage: 48%)
Gene name: C1R
Sequence domains:
Structure 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: ESRF BEAMLINE ID13
Spacegroup: P64
Unit cell:
a: 167.06Å b: 167.06Å c: 43.648Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.243 0.217 0.285
Expression system: Trichoplusia ni

Quick links

Citations

13 review citations

Complement System Part I - Molecular Mechanisms of Activation and Regulation.
Merle et al. (2015)
12 more

3 mentions without citation

Allostery in trypsin-like proteases suggests new therapeutic strategies.
Gohara et al. (2011)
2 more