› 2bo2

X-ray diffraction
2.6Å resolution

EGF Domains 1,2,5 of human EMR2, a 7-TM immune system molecule, in complex with calcium.

Released:
DOI: 10.2210/pdb2bo2/pdb
PDB entry 2bo2 coloured by chain, front view.
PDB entry 2bo2 coloured by chain, side view.
PDB entry 2bo2 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural and functional characterization of a novel T cell receptor co-regulatory protein complex, CD97-CD55.
Abbott RJ, Spendlove I, Roversi P, Fitzgibbon H, Knott V, Teriete P, McDonnell JM, Handford PA, Lea SM
J Biol Chem 282 22023-32 (2007)
PMID: 17449467

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-193771 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Adhesion G protein-coupled receptor E2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 143 amino acids
Theoretical weight: 15.59 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9UHX3 (Residues: 25-260; Coverage: 18%)
Gene names: ADGRE2, EMR2
Sequence domains: Calcium-binding EGF domain
Structure domains: Laminin

Ligands and Environments

2 bound ligands:
Ligand CA 4 x CA
Ligand CAC 1 x CAC
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P21
Unit cell:
a: 80.845Å b: 61.377Å c: 35.584Å
α: 90° β: 84.1° γ: 90°
R-values:
R R work R free
0.239 0.238 0.26
Expression system: Escherichia coli

Quick links

Citations

11 review citations

The role of complement in tumor growth.
Pio et al. (2014)
10 more

8 mentions without citation

Analysis of nidogen-1/laminin γ1 interaction by cross-linking, mass spectrometry, and computational modeling reveals multiple binding modes.
Lössl et al. (2014)
7 more