› 4acr

X-ray diffraction
2.55Å resolution

Crystal structure of N-glycosylated, C-terminally truncated human glypican-1

Released:
DOI: 10.2210/pdb4acr/pdb
PDB entry 4acr coloured by chain, front view.
PDB entry 4acr coloured by chain, side view.
PDB entry 4acr coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of N-glycosylated human glypican-1 core protein: structure of two loops evolutionarily conserved in vertebrate glypican-1.
Svensson G, Awad W, Håkansson M, Mani K, Logan DT
J Biol Chem 287 14040-51 (2012)
PMID: 22351761

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-152787 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Secreted glypican-1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 478 amino acids
Theoretical weight: 53.71 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: P35052 (Residues: 24-479; Coverage: 85%)
Gene name: GPC1
Sequence domains: Glypican

Ligands and Environments

1 bound ligand:
Ligand NAG 6 x NAG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I911-2
Spacegroup: P21
Unit cell:
a: 47.17Å b: 168.63Å c: 147.76Å
α: 90° β: 94.59° γ: 90°
R-values:
R R work R free
0.253 0.251 0.292
Expression system: Homo sapiens

Quick links

Citations

11 review citations

Proteoglycan form and function: A comprehensive nomenclature of proteoglycans.
Iozzo et al. (2015)
10 more

10 mentions without citation

Role of glypican-1 in regulating multiple cellular signaling pathways.
Pan et al. (2021)
9 more