5vk4

X-ray diffraction
2.65Å resolution

Crystal structure of a phosphoribosylformylglycinamidine cyclo-ligase from Neisseria gonorrhoeae bound to AMPPNP and magnesium

Released:
Source organism: Neisseria gonorrhoeae
Entry author: Seattle Structural Genomics Center for Infectious Disease (SSGCID)

Function and Biology Details

Reaction catalysed:
ATP + 2-(formamido)-N(1)-(5-phospho-D-ribosyl)acetamidine = ADP + phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphoribosylformylglycinamidine cyclo-ligase Chains: A, B
Molecule details ›
Chains: A, B
Length: 352 amino acids
Theoretical weight: 37.98 KDa
Source organism: Neisseria gonorrhoeae
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5F973 (Residues: 1-344; Coverage: 100%)
Gene names: NGO0526, purM
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: P212121
Unit cell:
a: 54.25Å b: 79.61Å c: 150.07Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.188 0.185 0.244
Expression system: Escherichia coli