› 1zcz

X-ray diffraction
1.88Å resolution

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:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194753 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bifunctional purine biosynthesis protein PurH Chains: A, B
Molecule details ›
Chains: A, B
Length: 464 amino acids
Theoretical weight: 51.39 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9X0X6 (Residues: 1-452; Coverage: 100%)
Gene names: TM_1249, purH
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand K 2 x K
Ligand PG4 2 x PG4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.1
Spacegroup: P1
Unit cell:
a: 62.084Å b: 58.63Å c: 72.749Å
α: 99.26° β: 96.89° γ: 106.13°
R-values:
R R work R free
0.158 0.156 0.197
Expression system: Escherichia coli

Quick links

Citations

4 citation in other articles

Plasticity in the purine-thiamine metabolic network of Salmonella.
Bazurto et al. (2011)
3 more

3 mentions without citation

Isotope-Labeled RNA Building Blocks for NMR Structure and Dynamics Studies.
Olenginski et al. (2021)
2 more