› 1vq3

X-ray diffraction
1.9Å resolution

Function and Biology Details

Reaction catalysed: 
ATP + N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide + L-glutamine + H(2)O = ADP + phosphate + 2-(formamido)-N(1)-(5-phospho-D-ribosyl)acetamidine + L-glutamate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assemblies composition:
homo tetramer
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194749 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphoribosylformylglycinamidine synthase subunit PurS Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 94 amino acids
Theoretical weight: 11.1 KDa
Source organism: Thermotoga maritima MSB8
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9X0X1 (Residues: 1-82; Coverage: 100%)
Gene names: THEMA_08115, TM_1244, Tmari_1249, purS
Sequence domains: Phosphoribosylformylglycinamidine (FGAM) synthase
Structure domains: Phosphoribosylformylglycinamidine synthase subunit PurS

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.1
Spacegroup: P212121
Unit cell:
a: 58.27Å b: 73.433Å c: 92.567Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.18 0.178 0.234
Expression system: Escherichia coli

Quick links

Citations

1 review citation

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

5 mentions without citation

The JCSG MR pipeline: optimized alignments, multiple models and parallel searches.
Schwarzenbacher et al. (2008)
4 more