3gar

X-ray diffraction
1.9Å resolution

A PH-DEPENDENT STABLIZATION OF AN ACTIVE SITE LOOP OBSERVED FROM LOW AND HIGH PH CRYSTAL STRUCTURES OF MUTANT MONOMERIC GLYCINAMIDE RIBONUCLEOTIDE TRANSFORMYLASE

Released:

Function and Biology Details

Reaction catalysed:
10-formyltetrahydrofolate + N(1)-(5-phospho-D-ribosyl)glycinamide = tetrahydrofolate + N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-139986 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphoribosylglycinamide formyltransferase Chain: A
Molecule details ›
Chain: A
Length: 212 amino acids
Theoretical weight: 23.21 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P08179 (Residues: 1-212; Coverage: 100%)
Gene names: JW2485, b2500, purN
Sequence domains: Formyl transferase
Structure domains: Formyl transferase, N-terminal domain

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: P6122
Unit cell:
a: 50.4Å b: 50.4Å c: 275.5Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.215 0.215 0.274
Expression system: Escherichia coli