› 2hry

X-ray diffraction
2.8Å resolution

T. maritima PurL complexed with AMPPCP

Released:
DOI: 10.2210/pdb2hry/pdb
PDB entry 2hry coloured by chain, front view.
PDB entry 2hry coloured by chain, side view.
PDB entry 2hry coloured by chain, top view.
Source organism: Thermotoga maritima
Primary publication:
Complexed structures of formylglycinamide ribonucleotide amidotransferase from Thermotoga maritima describe a novel ATP binding protein superfamily.
Morar M, Anand R, Hoskins AA, Stubbe J, Ealick SE
Biochemistry 45 14880-95 (2006)
PMID: 17154526

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 domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194752 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphoribosylformylglycinamidine synthase subunit PurL Chain: A
Molecule details ›
Chain: A
Length: 603 amino acids
Theoretical weight: 65.98 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9X0X3 (Residues: 1-603; Coverage: 100%)
Gene names: TM_1246, purL
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand MG 2 x MG
Ligand PO4 1 x PO4
Ligand ACP 1 x ACP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P212121
Unit cell:
a: 56.617Å b: 69.997Å c: 133.476Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.185 0.185 0.283
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Structural biology of the purine biosynthetic pathway.
Zhang et al. (2008)
2 more

2 mentions without citation

Structural studies of tri-functional human GART.
Welin et al. (2010)
1 more