› 1zed

X-ray diffraction
1.57Å resolution

Alkaline phosphatase from human placenta in complex with p-nitrophenyl-phosphonate

Released:
DOI: 10.2210/pdb1zed/pdb
PDB entry 1zed coloured by chain, front view.
PDB entry 1zed coloured by chain, side view.
PDB entry 1zed coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural studies of human placental alkaline phosphatase in complex with functional ligands.
Llinas P, Stura EA, Ménez A, Kiss Z, Stigbrand T, Millán JL, Le Du MH
J Mol Biol 350 441-51 (2005)
PMID: 15946677

Function and Biology Details

Reaction catalysed: 
A phosphate monoester + H(2)O = an alcohol + phosphate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138581 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alkaline phosphatase, placental type Chain: A
Molecule details ›
Chain: A
Length: 484 amino acids
Theoretical weight: 52.81 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P05187 (Residues: 23-506; Coverage: 94%)
Gene names: ALPP, PLAP
Sequence domains: Alkaline phosphatase
Structure domains: Alkaline Phosphatase, subunit A

Ligands and Environments

6 bound ligands:
Ligand NAG 2 x NAG
Ligand ZN 2 x ZN
Ligand MG 1 x MG
Ligand CA 1 x CA
Ligand PO3 1 x PO3
Ligand PNP 2 x PNP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: C2221
Unit cell:
a: 88.346Å b: 114.573Å c: 106.568Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.151 0.149 0.188

Quick links

Citations

8 review citations

Cellular function and molecular structure of ecto-nucleotidases.
Zimmermann et al. (2012)
7 more

8 mentions without citation

Catalytic signature of a heat-stable, chimeric human alkaline phosphatase with therapeutic potential.
Kiffer-Moreira et al. (2014)
7 more