› 2wu0

X-ray diffraction
2.57Å resolution

Crystal Structure Analysis of Klebsiella sp ASR1 Phytase

Released:
DOI: 10.2210/pdb2wu0/pdb
PDB entry 2wu0 coloured by chain, front view.
PDB entry 2wu0 coloured by chain, side view.
PDB entry 2wu0 coloured by chain, top view.
Source organism: Klebsiella pneumoniae
Primary publication:
Crystal structure of Klebsiella sp. ASR1 phytase suggests substrate binding to a preformed active site that meets the requirements of a plant rhizosphere enzyme.
Böhm K, Herter T, Müller JJ, Borriss R, Heinemann U
FEBS J 277 1284-96 (2010)
PMID: 20392204

Function and Biology Details

Reaction catalysed: 
Myo-inositol hexakisphosphate + H(2)O = 1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-183024 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3-phytase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 418 amino acids
Theoretical weight: 46.05 KDa
Source organism: Klebsiella pneumoniae
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q84CN9 (Residues: 29-421; Coverage: 100%)
Gene name: phyK
Sequence domains: Histidine phosphatase superfamily (branch 2)
Structure domains: Phosphoglycerate mutase-like

Ligands and Environments

1 bound ligand:
Ligand SO4 16 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X13
Spacegroup: P212121
Unit cell:
a: 81.713Å b: 122.929Å c: 205.402Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.201 0.198 0.243
Expression system: Escherichia coli BL21(DE3)

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Citations

2 review citations

Phytase, a new life for an "old" enzyme.
Lei et al. (2013)
1 more