› 1hng

X-ray diffraction
2.8Å resolution

CRYSTAL STRUCTURE AT 2.8 ANGSTROMS RESOLUTION OF A SOLUBLE FORM OF THE CELL ADHESION MOLECULE CD2

Released:
DOI: 10.2210/pdb1hng/pdb
PDB entry 1hng coloured by chain, front view.
PDB entry 1hng coloured by chain, side view.
PDB entry 1hng coloured by chain, top view.
Source organism: Rattus rattus
Primary publication:
Crystal structure at 2.8 A resolution of a soluble form of the cell adhesion molecule CD2.
Jones EY, Davis SJ, Williams AF, Harlos K, Stuart DI
Nature 360 232-9 (1992)
PMID: 1279440

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140435 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
T-cell surface antigen CD2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 176 amino acids
Theoretical weight: 20.14 KDa
Source organism: Rattus rattus
Expression system: Not provided
UniProt:
  • Canonical: P08921 (Residues: 23-198; Coverage: 55%)
Gene name: Cd2
Sequence domains:
Structure domains: Immunoglobulins

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P41212
Unit cell:
a: 111.4Å b: 111.4Å c: 86.9Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.215 0.215 not available
Expression system: Not provided

Quick links

Citations

51 review citations

3D domain swapping: a mechanism for oligomer assembly.
Bennett et al. (1995)
50 more

24 mentions without citation

What lessons can be learned from studying the folding of homologous proteins?
Nickson et al. (2010)
23 more