› 1hpu

X-ray diffraction
1.85Å resolution

5'-NUCLEOTIDASE (CLOSED FORM), COMPLEX WITH AMPCP

Released:
DOI: 10.2210/pdb1hpu/pdb
PDB entry 1hpu coloured by chain, front view.
PDB entry 1hpu coloured by chain, side view.
PDB entry 1hpu coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Mechanism of hydrolysis of phosphate esters by the dimetal center of 5'-nucleotidase based on crystal structures.
Knöfel T, Sträter N
J Mol Biol 309 239-54 (2001)
PMID: 11491293

Function and Biology Details

Reactions catalysed: 
A 5'-ribonucleotide + H(2)O = a ribonucleoside + phosphate
UDP-sugar + H(2)O = UMP + alpha-D-aldose 1-phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139351 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein UshA Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 525 amino acids
Theoretical weight: 58.28 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P07024 (Residues: 26-550; Coverage: 100%)
Gene names: JW0469, b0480, ushA
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand MN 8 x MN
Ligand A12 4 x A12
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7B
Spacegroup: P1
Unit cell:
a: 89.4Å b: 89.96Å c: 96.26Å
α: 110.79° β: 106.43° γ: 107.76°
R-values:
R R work R free
0.207 0.207 0.234
Expression system: Escherichia coli

Quick links

Citations

5 review citations

The 5'-nucleotidases as regulators of nucleotide and drug metabolism.
Hunsucker et al. (2005)
4 more

15 mentions without citation

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