PDBe 1c2t

X-ray diffraction
2.1Å resolution

NEW INSIGHTS INTO INHIBITOR DESIGN FROM THE CRYSTAL STRUCTURE AND NMR STUDIES OF E. COLI GAR TRANSFORMYLASE IN COMPLEX WITH BETA-GAR AND 10-FORMYL-5,8,10-TRIDEAZAFOLIC ACID.

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:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphoribosylglycinamide formyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 212 amino acids
Theoretical weight: 23.27 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: Formyltransferase

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-1
Spacegroup: P21
Unit cell:
a: 40.25Å b: 112.79Å c: 46.96Å
α: 90° β: 101.5° γ: 90°
R-values:
R R work R free
0.227 0.227 0.265
Expression system: Escherichia coli