› 1a5s

X-ray diffraction
2.3Å resolution

CRYSTAL STRUCTURE OF WILD-TYPE TRYPTOPHAN SYNTHASE COMPLEXED WITH 5-FLUOROINDOLE PROPANOL PHOSPHATE AND L-SER BOUND AS AMINO ACRYLATE TO THE BETA SITE

Released:
DOI: 10.2210/pdb1a5s/pdb
PDB entry 1a5s coloured by chain, front view.
PDB entry 1a5s coloured by chain, side view.
PDB entry 1a5s coloured by chain, top view.
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium
Primary publication:
Loop closure and intersubunit communication in tryptophan synthase.
Schneider TR, Gerhardt E, Lee M, Liang PH, Anderson KS, Schlichting I
Biochemistry 37 5394-406 (1998)
PMID: 9548921

Function and Biology Details

Reaction catalysed: 
(1a) 1-C-(indol-3-yl)glycerol 3-phosphate = indole + D-glyceraldehyde 3-phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133696 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
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: 1-268; Coverage: 100%)
Gene names: STM1727, trpA
Sequence domains: Tryptophan synthase alpha chain
Structure domains: Aldolase class I
Tryptophan synthase beta chain Chain: B
Molecule details ›
Chain: B
Length: 397 amino acids
Theoretical weight: 42.99 KDa
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A2K1 (Residues: 1-397; Coverage: 100%)
Gene names: STM1726, trpB
Sequence domains: Pyridoxal-phosphate dependent enzyme
Structure domains: Rossmann fold

Ligands and Environments


Cofactor: Ligand PLP 1 x PLP
3 bound ligands:
Ligand FIP 1 x FIP
Ligand NA 1 x NA
Ligand SER 1 x SER
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12C
Spacegroup: C2
Unit cell:
a: 182.7Å b: 60.8Å c: 67.5Å
α: 90° β: 94.6° γ: 90°
R-values:
R R work R free
0.177 0.177 0.247
Expression system: Escherichia coli

Quick links

Citations

13 review citations

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

2 mentions without citation

Quantitative prediction of protein-protein binding affinity with a potential of mean force considering volume correction.
Su et al. (2009)
1 more