› 1gya

Solution NMR

N-GLYCAN AND POLYPEPTIDE NMR SOLUTION STRUCTURES OF THE ADHESION DOMAIN OF HUMAN CD2

Released:
DOI: 10.2210/pdb1gya/pdb
PDB entry 1gya coloured by chain, ensemble of 18 models, front view.
PDB entry 1gya coloured by chain, ensemble of 18 models, side view.
PDB entry 1gya coloured by chain, ensemble of 18 models, top view.
Source organism: Homo sapiens
Primary publication:
Conformation and function of the N-linked glycan in the adhesion domain of human CD2.
Wyss DF, Choi JS, Li J, Knoppers MH, Willis KJ, Arulanandam AR, Smolyar A, Reinherz EL, Wagner G
Science 269 1273-8 (1995)
PMID: 7544493

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139163 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
T-cell surface antigen CD2 Chain: A
Molecule details ›
Chain: A
Length: 105 amino acids
Theoretical weight: 12.45 KDa
Source organism: Homo sapiens
Expression system: Cricetulus griseus
UniProt:
  • Canonical: P06729 (Residues: 25-129; Coverage: 32%)
Gene names: CD2, SRBC
Sequence domains: Immunoglobulin V-set domain
Structure domains: Immunoglobulins

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, BMA, MAN
Carbohydrate polymer
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: distance geometry
Expression system: Cricetulus griseus

Quick links

Citations

28 review citations

Glycosylation: heterogeneity and the 3D structure of proteins.
Rudd et al. (1997)
27 more

11 mentions without citation

The intrinsic and extrinsic effects of N-linked glycans on glycoproteostasis.
Hebert et al. (2014)
10 more