› 1nsj

X-ray diffraction
2Å resolution

CRYSTAL STRUCTURE OF PHOSPHORIBOSYL ANTHRANILATE ISOMERASE FROM THERMOTOGA MARITIMA

Released:
DOI: 10.2210/pdb1nsj/pdb
PDB entry 1nsj coloured by chain, front view.
PDB entry 1nsj coloured by chain, side view.
PDB entry 1nsj coloured by chain, top view.
Source organism: Thermotoga maritima
Primary publication:
Crystal structure at 2.0 A resolution of phosphoribosyl anthranilate isomerase from the hyperthermophile Thermotoga maritima: possible determinants of protein stability.
Hennig M, Sterner R, Kirschner K, Jansonius JN
Biochemistry 36 6009-16 (1997)
PMID: 9166771

Function and Biology Details

Reaction catalysed: 
N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-176366 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
N-(5'-phosphoribosyl)anthranilate isomerase Chain: A
Molecule details ›
Chain: A
Length: 205 amino acids
Theoretical weight: 23.07 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
  • Canonical: Q56320 (Residues: 1-205; Coverage: 100%)
Gene names: TM_0139, trpF
Sequence domains: N-(5'phosphoribosyl)anthranilate (PRA) isomerase
Structure domains: Aldolase class I

Ligands and Environments

1 bound ligand:
Ligand PO4 1 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ELLIOTT GX-18
Spacegroup: P6122
Unit cell:
a: 68.4Å b: 68.4Å c: 185.4Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.192 0.192 0.243
Expression system: Escherichia coli

Quick links

Citations

9 review citations

Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability.
Vieille et al. (2001)
8 more

5 mentions without citation

Correspondences between low-energy modes in enzymes: dynamics-based alignment of enzymatic functional families.
Zen et al. (2008)
4 more