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X-ray diffraction
2.5Å resolution

X-RAY CRYSTAL STRUCTURE OF AMINOIMIDAZOLE RIBONUCLEOTIDE SYNTHETASE (PURM), FROM THE E. COLI PURINE BIOSYNTHETIC PATHWAY, AT 2.5 A RESOLUTION

Released:

Function and Biology Details

Reaction catalysed:
ATP + 2-(formamido)-N(1)-(5-phospho-D-ribosyl)acetamidine = ADP + phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole
Biochemical function:
Cellular component:

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo tetramer
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphoribosylformylglycinamidine cyclo-ligase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 345 amino acids
Theoretical weight: 36.86 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P08178 (Residues: 1-345; Coverage: 100%)
Gene names: JW2484, b2499, purG, purM
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE F2
Spacegroup: P212121
Unit cell:
a: 71.17Å b: 211.68Å c: 94.45Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.192 0.192 0.264
Expression system: Escherichia coli BL21