› 1ax4

X-ray diffraction
2.1Å resolution

TRYPTOPHANASE FROM PROTEUS VULGARIS

Released:
DOI: 10.2210/pdb1ax4/pdb
PDB entry 1ax4 coloured by chain, front view.
PDB entry 1ax4 coloured by chain, side view.
PDB entry 1ax4 coloured by chain, top view.
Source organism: Proteus vulgaris
Primary publication:
Crystal structure of tryptophanase.
Isupov MN, Antson AA, Dodson EJ, Dodson GG, Dementieva IS, Zakomirdina LN, Wilson KS, Dauter Z, Lebedev AA, Harutyunyan EH
J Mol Biol 276 603-23 (1998)
PMID: 9551100

Function and Biology Details

Reaction catalysed: 
(1a) L-tryptophan = indole + 2-aminoprop-2-enoate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151290 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tryptophanase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 467 amino acids
Theoretical weight: 52.79 KDa
Source organism: Proteus vulgaris
Expression system: Escherichia coli
UniProt:
  • Canonical: P28796 (Residues: 1-467; Coverage: 100%)
Gene name: tnaA
Sequence domains: Beta-eliminating lyase
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand K 4 x K
1 modified residue:
Ligand LLP 4 x LLP

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7B
Spacegroup: P212121
Unit cell:
a: 114.99Å b: 118.23Å c: 153.68Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.187 0.187 0.227
Expression system: Escherichia coli

Quick links

Citations

9 review citations

Structure, evolution and action of vitamin B6-dependent enzymes.
Jansonius JN. (1998)
8 more

8 mentions without citation

Evolutionarily conserved regions and hydrophobic contacts at the superfamily level: The case of the fold-type I, pyridoxal-5'-phosphate-dependent enzymes.
Paiardini et al. (2004)
7 more