4avv

X-ray diffraction
1.6Å 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).
Acta Crystallogr D Biol Crystallogr 70 2232-40 (2014)
PMID: 25084341

Function and Biology Details

Structure analysis Details

Assembly composition:
homo pentamer (preferred)
PDBe Complex ID:
PDB-CPX-136123 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (3 distinct):
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

Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer : NEW Components: NAG, SIA, BMA, MAN, GAL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: C2
Unit cell:
a: 154.379Å b: 108.579Å c: 120.263Å
α: 90° β: 138.53° γ: 90°
R-values:
R R work R free
0.15 0.15 0.175