› 3o3u

X-ray diffraction
1.5Å resolution

Crystal Structure of Human Receptor for Advanced Glycation Endproducts (RAGE)

Released:
DOI: 10.2210/pdb3o3u/pdb
PDB entry 3o3u coloured by chain, front view.
PDB entry 3o3u coloured by chain, side view.
PDB entry 3o3u coloured by chain, top view.
Source organisms:
Primary publication:
The 1.5 Å crystal structure of human receptor for advanced glycation endproducts (RAGE) ectodomains reveals unique features determining ligand binding.
Park H, Adsit FG, Boyington JC
J Biol Chem 285 40762-70 (2010)
PMID: 20943659

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142568 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Advanced glycosylation end product-specific receptor; Maltose/maltodextrin-binding periplasmic protein Chain: N
Molecule details ›
Chain: N
Length: 581 amino acids
Theoretical weight: 63.43 KDa
Source organisms: Expression system: Escherichia coli
UniProt:
  • Canonical: P0AEX9 (Residues: 28-384; Coverage: 97%)
  • Canonical: Q15109 (Residues: 23-231; Coverage: 55%)
Gene names: AGER, JW3994, RAGE, b4034, malE
Sequence domains:
Structure domains: Immunoglobulins

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC
Carbohydrate polymer
1 bound ligand:
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P21212
Unit cell:
a: 81.739Å b: 89.308Å c: 97.978Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.169 0.168 0.184
Expression system: Escherichia coli

Quick links

Citations

30 review citations

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Tang et al. (2012)
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22 mentions without citation

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Moller-Tank et al. (2014)
21 more