› 1gyk

X-ray diffraction
2.2Å resolution

Serum Amyloid P Component co-crystallised with MOBDG at neutral pH

Released:
DOI: 10.2210/pdb1gyk/pdb
PDB entry 1gyk coloured by chain, front view.
PDB entry 1gyk coloured by chain, side view.
PDB entry 1gyk coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The structures of crystalline complexes of human serum amyloid P component with its carbohydrate ligand, the cyclic pyruvate acetal of galactose.
Thompson D, Pepys MB, Tickle I, Wood S
J Mol Biol 320 1081-6 (2002)
PMID: 12126626

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo pentamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-136123 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serum amyloid P-component Chains: A, B, C, D, E
Molecule details ›
Chains: A, B, C, D, E
Length: 204 amino acids
Theoretical weight: 23.28 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P02743 (Residues: 20-223; Coverage: 100%)
Gene names: APCS, PTX2
Sequence domains: Pentaxin family
Structure domains: Jelly Rolls

Ligands and Environments

2 bound ligands:
Ligand CA 9 x CA
Ligand CDG 4 x CDG
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 95.76Å b: 70.53Å c: 103.41Å
α: 90° β: 96.8° γ: 90°
R-values:
R R work R free
0.186 0.186 0.224

Quick links

Citations

5 review citations

Amyloid accomplices and enforcers.
Alexandrescu AT. (2005)
4 more

3 mentions without citation

Insights into the quaternary association of proteins through structure graphs: a case study of lectins.
Brinda et al. (2005)
2 more