› 2qy0

X-ray diffraction
2.6Å resolution

Active dimeric structure of the catalytic domain of C1r reveals enzyme-product like contacts

Released:
DOI: 10.2210/pdb2qy0/pdb
PDB entry 2qy0 coloured by chain, front view.
PDB entry 2qy0 coloured by chain, side view.
PDB entry 2qy0 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Revisiting the mechanism of the autoactivation of the complement protease C1r in the C1 complex: structure of the active catalytic region of C1r.
Kardos J, Harmat V, Palló A, Barabás O, Szilágyi K, Gráf L, Náray-Szabó G, Goto Y, Závodszky P, Gál P
Mol Immunol 45 1752-60 (2008)
PMID: 17996945

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 domain:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133185 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Complement C1r subcomponent heavy chain Chains: A, C
Molecule details ›
Chains: A, C
Length: 159 amino acids
Theoretical weight: 18.48 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P00736 (Residues: 309-463; Coverage: 23%)
Gene name: C1R
Sequence domains: Sushi repeat (SCR repeat)
Structure domains: Complement Module, domain 1
Complement C1r subcomponent light chain Chains: B, D
Molecule details ›
Chains: B, D
Length: 242 amino acids
Theoretical weight: 27.13 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P00736 (Residues: 464-705; Coverage: 35%)
Gene name: C1R
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

1 bound ligand:
Ligand GOL 7 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: P212121
Unit cell:
a: 74.541Å b: 92.416Å c: 162.848Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.213 0.211 0.259
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Paths reunited: Initiation of the classical and lectin pathways of complement activation.
Wallis et al. (2010)
5 more

3 mentions without citation

Functional and Structural Characterization of a Potent C1q Inhibitor Targeting the Classical Pathway of the Complement System.
Laursen et al. (2020)
2 more