› 1l1r

X-ray diffraction
1.95Å resolution

Crystal Structure of APRTase from Giardia lamblia Complexed with 9-deazaadenine, Mg2+ and PRPP

Released:
DOI: 10.2210/pdb1l1r/pdb
Model geometry
Fit model/data
Data not deposited
PDB entry 1l1r coloured by chain, front view.
PDB entry 1l1r coloured by chain, side view.
PDB entry 1l1r coloured by chain, top view.
Source organism: Giardia intestinalis
Primary publication:
Closed site complexes of adenine phosphoribosyltransferase from Giardia lamblia reveal a mechanism of ribosyl migration.
Shi W, Sarver AE, Wang CC, Tanaka KS, Almo SC, Schramm VL
J Biol Chem 277 39981-8 (2002)
PMID: 12171925

Function and Biology Details

Reaction catalysed: 
AMP + diphosphate = adenine + 5-phospho-alpha-D-ribose 1-diphosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-188322 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
adenine phosphoribosyltransferase Chain: A
Molecule details ›
Chain: A
Length: 186 amino acids
Theoretical weight: 20.29 KDa
Source organism: Giardia intestinalis
Expression system: Escherichia coli
UniProt:
  • Canonical: Q967M2 (Residues: 1-180; Coverage: 100%)
Gene name: DHA2_112885
Sequence domains: Phosphoribosyl transferase domain
Structure domains: Rossmann fold

Ligands and Environments

3 bound ligands:
Ligand MG 1 x MG
Ligand 9DA 1 x 9DA
Ligand PRP 1 x PRP
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: NSLS BEAMLINE X9B
Spacegroup: P3121
Unit cell:
a: 54.325Å b: 54.325Å c: 108.744Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.222 0.218 0.262
Expression system: Escherichia coli

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Citations

2 review citations

Potential chemotherapeutic targets in the purine metabolism of parasites.
el Kouni MH. (2003)
1 more

5 mentions without citation

Peptide toxins and small-molecule blockers of BK channels.
Yu et al. (2016)
4 more