2ntm

X-ray diffraction
2.6Å resolution

Crystal structure of PurO from Methanothermobacter thermoautotrophicus

Released:

Function and Biology Details

Reaction catalysed:
IMP + H(2)O = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Biochemical function:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-127874 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
IMP cyclohydrolase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 222 amino acids
Theoretical weight: 24.03 KDa
Source organism: Methanothermobacter thermautotrophicus
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: O27099 (Residues: 1-202; Coverage: 100%)
Gene names: MTH_1020, purO
Sequence domains: IMP cyclohydrolase-like protein
Structure domains: Inosine monophosphate cyclohydrolase-like

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P32
Unit cell:
a: 84.277Å b: 84.277Å c: 124.77Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.225 0.225 0.274
Expression system: Escherichia coli BL21