› 1o17

X-ray diffraction
2.05Å resolution

ANTHRANILATE PHOSPHORIBOSYL-TRANSFERASE (TRPD)

Released:
DOI: 10.2210/pdb1o17/pdb
PDB entry 1o17 coloured by chain, front view.
PDB entry 1o17 coloured by chain, side view.
PDB entry 1o17 coloured by chain, top view.
Source organism: Saccharolobus solfataricus
Primary publication:
Structural analysis of two enzymes catalysing reverse metabolic reactions implies common ancestry.
Mayans O, Ivens A, Nissen LJ, Kirschner K, Wilmanns M
EMBO J 21 3245-54 (2002)
PMID: 12093726

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

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7B
Spacegroup: P2
Unit cell:
a: 92.34Å b: 65.85Å c: 116.44Å
α: 90° β: 107.56° γ: 90°
R-values:
R R work R free
0.213 0.213 0.26
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Ancient origin of the tryptophan operon and the dynamics of evolutionary change.
Xie et al. (2003)
2 more

3 mentions without citation

H2r: identification of evolutionary important residues by means of an entropy based analysis of multiple sequence alignments.
Merkl et al. (2008)
2 more