› 3eth

X-ray diffraction
1.6Å resolution

Crystal structure of E. coli Purk in complex with MgATP

Released:
DOI: 10.2210/pdb3eth/pdb
PDB entry 3eth coloured by chain, front view.
PDB entry 3eth coloured by chain, side view.
PDB entry 3eth coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Structural analysis of the active site geometry of N5-carboxyaminoimidazole ribonucleotide synthetase from Escherichia coli.
Thoden JB, Holden HM, Firestine SM
Biochemistry 47 13346-53 (2008)
PMID: 19053251

Function and Biology Details

Reaction catalysed: 
ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole + HCO(3)(-) = ADP + phosphate + 5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140530 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
N5-carboxyaminoimidazole ribonucleotide synthase Chains: A, B
Molecule details ›
Chains: A, B
Length: 355 amino acids
Theoretical weight: 39.53 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P09029 (Residues: 1-355; Coverage: 100%)
Gene names: JW0511, b0522, purK
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand ATP 2 x ATP
Ligand MG 4 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P1
Unit cell:
a: 57.101Å b: 57.109Å c: 59.215Å
α: 77.46° β: 82.39° γ: 77.26°
R-values:
R R work R free
0.178 0.175 0.228
Expression system: Escherichia coli

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Citations

3 review citations

The enzymes of biotin dependent CO₂ metabolism: what structures reveal about their reaction mechanisms.
Waldrop et al. (2012)
2 more

8 mentions without citation

Unlocking the sugar "steric gate" of DNA polymerases.
Brown et al. (2011)
7 more