PDBe 3mk0

X-ray diffraction
1.9Å resolution

Refinement of placental alkaline phosphatase complexed with nitrophenyl

Released:
Source organism: Homo sapiens
Primary publication:
Refined structures of placental alkaline phosphatase show a consistent pattern of interactions at the peripheral site.
Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 66 866-70 (2010)
PMID: 20693656

Function and Biology Details

Reaction catalysed:
A phosphate monoester + H(2)O = an alcohol + phosphate. 
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alkaline phosphatase, placental type Chain: A
Molecule details ›
Chain: A
Length: 484 amino acids
Theoretical weight: 52.89 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

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2221
Unit cell:
a: 89.022Å b: 113.894Å c: 106.594Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.137 0.135 0.19