› 3apu

X-ray diffraction
2.1Å resolution

Crystal structure of the A variant of human alpha1-acid glycoprotein

Released:
DOI: 10.2210/pdb3apu/pdb
PDB entry 3apu coloured by chain, front view.
PDB entry 3apu coloured by chain, side view.
PDB entry 3apu coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural insights into differences in drug-binding selectivity between two forms of human alpha1-acid glycoprotein genetic variants, the A and F1*S forms.
Nishi K, Ono T, Nakamura T, Fukunaga N, Izumi M, Watanabe H, Suenaga A, Maruyama T, Yamagata Y, Curry S, Otagiri M
J Biol Chem 286 14427-34 (2011)
PMID: 21349832

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-148678 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-1-acid glycoprotein 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 190 amino acids
Theoretical weight: 22.69 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P19652 (Residues: 19-201; Coverage: 100%)
Gene names: AGP2, ORM2
Sequence domains: Lipocalin / cytosolic fatty-acid binding protein family
Structure domains: Lipocalin

Ligands and Environments

1 bound ligand:
Ligand PG4 2 x PG4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44XU
Spacegroup: C2
Unit cell:
a: 67.107Å b: 44.862Å c: 120.784Å
α: 90° β: 91.88° γ: 90°
R-values:
R R work R free
0.201 0.2 0.232
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Pharmacokinetic and Pharmacodynamic Considerations for Drugs Binding to Alpha-1-Acid Glycoprotein.
Smith et al. (2018)
4 more

9 mentions without citation

All-atom ensemble modeling to analyze small-angle x-ray scattering of glycosylated proteins.
Guttman et al. (2013)
8 more