PDBe 5gni

X-ray diffraction
3.01Å resolution

The crystal structure of PECAM-1 IgL1-2 trans-homophilic dimer

Released:
Source organism: Homo sapiens
Primary publication:
Structural Basis for Human PECAM-1-Mediated Trans-homophilic Cell Adhesion.
OpenAccess logo Sci Rep 6 38655 (2016)
PMID: 27958302

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Platelet endothelial cell adhesion molecule Chains: A, B
Molecule details ›
Chains: A, B
Length: 213 amino acids
Theoretical weight: 24.55 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
UniProt:
  • Canonical: P16284 (Residues: 28-232; Coverage: 29%)
Gene name: PECAM1

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: I222
Unit cell:
a: 60.522Å b: 141.496Å c: 169.918Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.223 0.22 0.281
Expression system: Trichoplusia ni