› 3q3q

X-ray diffraction
1.95Å resolution

Crystal Structure of SPAP: an novel alkaline phosphatase from bacterium Sphingomonas sp. strain BSAR-1

Released:
DOI: 10.2210/pdb3q3q/pdb
PDB entry 3q3q coloured by chain, front view.
PDB entry 3q3q coloured by chain, side view.
PDB entry 3q3q coloured by chain, top view.
Source organism: Sphingomonas sp. BSAR-1
Primary publication:
X-ray structure reveals a new class and provides insight into evolution of alkaline phosphatases.
Bihani SC, Das A, Nilgiriwala KS, Prashar V, Pirocchi M, Apte SK, Ferrer JL, Hosur MV
PLoS One 6 e22767 (2011)
PMID: 21829507

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-106760 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alkaline phosphatase PhoK Chain: A
Molecule details ›
Chain: A
Length: 565 amino acids
Theoretical weight: 60.88 KDa
Source organism: Sphingomonas sp. BSAR-1
Expression system: Escherichia coli
UniProt:
  • Canonical: A1YYW7 (Residues: 1-559; Coverage: 100%)
Gene name: phoK
Sequence domains: Type I phosphodiesterase / nucleotide pyrophosphatase
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand ZN 2 x ZN
Ligand CA 1 x CA
Ligand GOL 5 x GOL
Ligand KOP 1 x KOP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM30A
Spacegroup: P41212
Unit cell:
a: 87.37Å b: 87.37Å c: 168.16Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.157 0.155 0.186
Expression system: Escherichia coli

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Citations

11 citation in other articles

A novel psychrophilic alkaline phosphatase from the metagenome of tidal flat sediments.
Lee et al. (2015)
10 more

2 mentions without citation

X-ray structure reveals a new class and provides insight into evolution of alkaline phosphatases.
Bihani et al. (2011)
1 more