› 3v4s

X-ray diffraction
2.02Å resolution

Crystal Structure of ADP-ATP complex of purK: N5-carboxyaminoimidazole ribonucleotide synthetase

Released:
DOI: 10.2210/pdb3v4s/pdb
PDB entry 3v4s coloured by chain, front view.
PDB entry 3v4s coloured by chain, side view.
PDB entry 3v4s coloured by chain, top view.
Source organism: Bacillus anthracis str. A0248
Primary publication:
Elucidation of the bicarbonate binding site and insights into the carboxylation mechanism of (N(5))-carboxyaminoimidazole ribonucleotide synthase (PurK) from Bacillus anthracis.
Tuntland ML, Santarsiero BD, Johnson ME, Fung LW
Acta Crystallogr D Biol Crystallogr 70 3057-65 (2014)
PMID: 25372694

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-164151 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphoribosylaminoimidazole carboxylase, ATPase subunit Chains: A, B
Molecule details ›
Chains: A, B
Length: 387 amino acids
Theoretical weight: 42.92 KDa
Source organism: Bacillus anthracis str. A0248
Expression system: Escherichia coli
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand ADP 1 x ADP
Ligand MG 3 x MG
Ligand CO3 2 x CO3
Ligand ATP 1 x ATP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P212121
Unit cell:
a: 57.744Å b: 82.87Å c: 167.928Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.174 0.172 0.215
Expression system: Escherichia coli

Quick links

Citations

1 citations in other articles

Catalytic and structural properties of ATP-dependent caprolactamase from Pseudomonas jessenii.
Marjanovic et al. (2021)