› 2r7k

X-ray diffraction
2.1Å resolution

Crystal structure of FAICAR synthetase (PurP) from M. jannaschii complexed with AMPPCP and AICAR

Released:
DOI: 10.2210/pdb2r7k/pdb
PDB entry 2r7k coloured by chain, front view.
PDB entry 2r7k coloured by chain, side view.
PDB entry 2r7k coloured by chain, top view.
Source organism: Methanocaldococcus jannaschii
Primary publication:
Crystal structure and function of 5-formaminoimidazole-4-carboxamide ribonucleotide synthetase from Methanocaldococcus jannaschii.
Zhang Y, White RH, Ealick SE
Biochemistry 47 205-17 (2008)
PMID: 18069798

Function and Biology Details

Reaction catalysed: 
ATP + formate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide = ADP + phosphate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-176442 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
5-formaminoimidazole-4-carboxamide-1-(beta)-D-ribofuranosyl 5'-monophosphate synthetase Chain: A
Molecule details ›
Chain: A
Length: 361 amino acids
Theoretical weight: 40.87 KDa
Source organism: Methanocaldococcus jannaschii
Expression system: Escherichia coli
UniProt:
  • Canonical: Q57600 (Residues: 1-361; Coverage: 100%)
Gene names: MJ0136, purP
Sequence domains:
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand SO4 1 x SO4
Ligand CL 2 x CL
Ligand ACP 1 x ACP
Ligand AMZ 1 x AMZ
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: R32
Unit cell:
a: 109.435Å b: 109.435Å c: 255.994Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.21 0.208 0.248
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Structural biology of the purine biosynthetic pathway.
Zhang et al. (2008)
1 more

2 mentions without citation

Divergence and convergence in enzyme evolution.
Galperin et al. (2012)
1 more