› 4hxv

X-ray diffraction
2.6Å resolution

Crystal structure of 3'(2'),5'-bisphosphate nucleotidase1 from Entamoeba histolytica in complex with AMP and metal ions

Released:
DOI: 10.2210/pdb4hxv/pdb
PDB entry 4hxv coloured by chain, front view.
PDB entry 4hxv coloured by chain, side view.
PDB entry 4hxv coloured by chain, top view.
Source organism: Entamoeba histolytica
Primary publication:
Structural elucidation of a dual-activity PAP phosphatase-1 from Entamoeba histolytica capable of hydrolysing both 3'-phosphoadenosine 5'-phosphate and inositol 1,4-bisphosphate.
Faisal Tarique K, Arif Abdul Rehman S, Gourinath S
Acta Crystallogr D Biol Crystallogr 70 2019-31 (2014)
PMID: 25004978

Function and Biology Details

Reactions catalysed: 
1D-myo-inositol 1,4-bisphosphate + H(2)O = 1D-myo-inositol 4-phosphate + phosphate
Adenosine 3',5'-bisphosphate + H(2)O = adenosine 5'-phosphate + phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-111343 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3',5'-bisphosphate nucleotidase Chain: A
Molecule details ›
Chain: A
Length: 325 amino acids
Theoretical weight: 36.15 KDa
Source organism: Entamoeba histolytica
Expression system: Escherichia coli
UniProt:
  • Canonical: C4M4T9 (Residues: 1-317; Coverage: 100%)
Gene name: EHI_193350
Sequence domains: Inositol monophosphatase family
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand MG 1 x MG
Ligand AMP 1 x AMP
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BRUKER AXS MICROSTAR
Spacegroup: P212121
Unit cell:
a: 39.618Å b: 63.877Å c: 117.845Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.233 0.23 0.283
Expression system: Escherichia coli

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Citations

1 review citation

Why Nature Chose Potassium.
Danchin et al. (2019)
1 other article