› 1apq

Solution NMR

STRUCTURE OF THE EGF-LIKE MODULE OF HUMAN C1R, NMR, 19 STRUCTURES

Released:
DOI: 10.2210/pdb1apq/pdb
PDB entry 1apq coloured by chain, ensemble of 19 models, front view.
PDB entry 1apq coloured by chain, ensemble of 19 models, side view.
PDB entry 1apq coloured by chain, ensemble of 19 models, top view.
Source organism: Homo sapiens
Primary publication:
Solution structure of the epidermal growth factor (EGF)-like module of human complement protease C1r, an atypical member of the EGF family.
Bersch B, Hernandez JF, Marion D, Arlaud GJ
Biochemistry 37 1204-14 (1998)
PMID: 9477945

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:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

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: 53 amino acids
Theoretical weight: 5.98 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P00736 (Residues: 140-192; Coverage: 8%)
Gene name: C1R
Sequence domains: Coagulation Factor Xa inhibitory site
Structure domains: Laminin

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: SIMULATED ANNEALING, RESTRAINED MOLECULAR DYNAMICS
Expression system: Not provided

Quick links

Citations

7 review citations

Structure and activation of the C1 complex of complement: unraveling the puzzle.
Gaboriaud et al. (2004)
6 more

7 mentions without citation

Improved prediction of critical residues for protein function based on network and phylogenetic analyses.
Thibert et al. (2005)
6 more