X-ray diffraction
1.85Å resolution

Anthranilate bound at active site of anthranilate phosphoribosyl transferase from Acinetobacter (AnPRT; TrpD)

Source organism: Acinetobacter sp. ADP1
Entry authors: Evans GL, Newton MS, Norris GE, Patrick WM

Function and Biology Details

Reaction catalysed:
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate = anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
Biochemical function:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Anthranilate phosphoribosyltransferase Chain: A
Molecule details ›
Chain: A
Length: 365 amino acids
Theoretical weight: 39.45 KDa
Source organism: Acinetobacter sp. ADP1
Expression system: Escherichia coli
  • Canonical: P00500 (Residues: 2-349; Coverage: 100%)
Gene names: ACIAD2462, trpD
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: C2221
Unit cell:
a: 60.997Å b: 70.83Å c: 169.156Å
α: 90° β: 90° γ: 90°
R R work R free
0.225 0.223 0.258
Expression system: Escherichia coli