› 2gvq

X-ray diffraction
2.43Å resolution

Anthranilate phosphoribosyl-transferase (TRPD) from S. solfataricus in complex with anthranilate

Released:
DOI: 10.2210/pdb2gvq/pdb
PDB entry 2gvq coloured by chain, front view.
PDB entry 2gvq coloured by chain, side view.
PDB entry 2gvq coloured by chain, top view.
Source organism: Saccharolobus solfataricus
Primary publication:
Structural and mutational analysis of substrate complexation by anthranilate phosphoribosyltransferase from Sulfolobus solfataricus.
Marino M, Deuss M, Svergun DI, Konarev PV, Sterner R, Mayans O
J Biol Chem 281 21410-21421 (2006)
PMID: 16714288

Function and Biology Details

Reaction catalysed: 
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate = anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156171 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Anthranilate phosphoribosyltransferase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 345 amino acids
Theoretical weight: 37.62 KDa
Source organism: Saccharolobus solfataricus
Expression system: Escherichia coli
UniProt:
  • Canonical: P50384 (Residues: 1-345; Coverage: 100%)
Gene names: SSO0890, trpD
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand BE2 7 x BE2
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P2
Unit cell:
a: 91.814Å b: 65.621Å c: 115.607Å
α: 90° β: 107.39° γ: 90°
R-values:
R R work R free
0.199 0.199 0.242
Expression system: Escherichia coli

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Citations

3 review citations

Phosphoribosyl Diphosphate (PRPP): Biosynthesis, Enzymology, Utilization, and Metabolic Significance.
Hove-Jensen et al. (2017)
2 more

3 mentions without citation

Structure, mechanism and inhibition of anthranilate phosphoribosyltransferase.
Scully et al. (2023)
2 more