1g8m

X-ray diffraction
1.75Å resolution

CRYSTAL STRUCTURE OF AVIAN ATIC, A BIFUNCTIONAL TRANSFORMYLASE AND CYCLOHYDROLASE ENZYME IN PURINE BIOSYNTHESIS AT 1.75 ANG. RESOLUTION

Released:

Function and Biology Details

Reactions catalysed:
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide = tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
IMP + H(2)O = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bifunctional purine biosynthesis protein ATIC Chains: A, B
Molecule details ›
Chains: A, B
Length: 593 amino acids
Theoretical weight: 64.97 KDa
Source organism: Gallus gallus
Expression system: Escherichia coli
UniProt:
  • Canonical: P31335 (Residues: 1-593; Coverage: 100%)
Gene names: ATIC, PURH
Sequence domains: AICARFT/IMPCHase bienzyme
Structure domains:

Ligands and Environments

2 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: P21
Unit cell:
a: 65.1Å b: 106Å c: 103.5Å
α: 90° β: 108° γ: 90°
R-values:
R R work R free
0.2 0.2 0.216
Expression system: Escherichia coli