PDBe 1kfe

X-ray diffraction
1.75Å resolution

CRYSTAL STRUCTURE OF ALPHAT183V MUTANT OF TRYPTOPHAN SYNTHASE FROM SALMONELLA TYPHIMURIUM WITH L-Ser Bound To The Beta Site

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Tryptophan synthase beta chain Chain: B
Molecule details ›
Chain: B
Length: 394 amino acids
Theoretical weight: 42.55 KDa
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A2K1 (Residues: 2-395; Coverage: 99%)
Gene names: STM1726, trpB
Sequence domains: Pyridoxal-phosphate dependent enzyme
Structure domains: Rossmann fold
Tryptophan synthase alpha chain Chain: A
Molecule details ›
Chain: A
Length: 268 amino acids
Theoretical weight: 28.7 KDa
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium
Expression system: Escherichia coli
UniProt:
  • Canonical: P00929 (Residues: 1-86, 88-268; Coverage: 100%)
Gene names: STM1727, trpA
Sequence domains: Tryptophan synthase alpha chain
Structure domains: Aldolase class I

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7B
Spacegroup: C2
Unit cell:
a: 182.224Å b: 59.985Å c: 67.072Å
α: 90° β: 94.68° γ: 90°
R-values:
R R work R free
0.192 0.192 0.225
Expression system: Escherichia coli