› 3l2y

X-ray diffraction
2.7Å resolution

The structure of C-reactive protein bound to phosphoethanolamine

Released:
DOI: 10.2210/pdb3l2y/pdb
PDB entry 3l2y coloured by chain, front view.
PDB entry 3l2y coloured by chain, side view.
PDB entry 3l2y coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis of ligand specificity in the human pentraxins, C-reactive protein and serum amyloid P component.
Mikolajek H, Kolstoe SE, Pye VE, Mangione P, Pepys MB, Wood SP
J Mol Recognit 24 371-7 (2011)
PMID: 21360619

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo pentamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-136120 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
C-reactive protein Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T
Length: 206 amino acids
Theoretical weight: 23.07 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P02741 (Residues: 19-224; Coverage: 100%)
Gene names: CRP, PTX1
Sequence domains: Pentaxin family
Structure domains: Jelly Rolls

Ligands and Environments

2 bound ligands:
Ligand CA 40 x CA
Ligand OPE 20 x OPE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P41
Unit cell:
a: 278.448Å b: 278.448Å c: 92.111Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.225 0.224 0.246

Quick links

Citations

12 review citations

Post-translational control of protein function by disulfide bond cleavage.
Cook et al. (2013)
11 more

1 mention without citation

Cryo-Electron Microscopy and Biochemical Analysis Offer Insights Into the Effects of Acidic pH, Such as Occur During Acidosis, on the Complement Binding Properties of C-Reactive Protein.
Noone et al. (2021)