4avt

X-ray diffraction
3.2Å resolution

Structure of CPHPC bound to Serum Amyloid P Component

Released:
Source organism: Homo sapiens
Primary publication:
Interaction of serum amyloid P component with hexanoyl bis(D-proline) (CPHPC).
OpenAccess logo Acta Crystallogr. D Biol. Crystallogr. 70 2232-40 (2014)
PMID: 25084341

Function and Biology Details

Structure analysis Details

Assembly composition:
homo pentamer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serum amyloid P-component Chains: A, B, C, D, E, F, G, H, I, J
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J
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

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-3
Spacegroup: P43212
Unit cell:
a: 230.864Å b: 230.864Å c: 281.393Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.189 0.197