PDBe 3nav

X-ray diffraction
2.1Å resolution

Crystal structure of an alpha subunit of tryptophan synthase from Vibrio cholerae O1 biovar El Tor str. N16961

Released:
Entry authors: Nocek B, Makowska-Grzyska M, Kwon K, Anderson A, Joachimiak A, Center for Structural Genomics of Infectious Diseases (CSGID)

Function and Biology Details

Reaction catalysed:
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H(2)O. 
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tryptophan synthase alpha chain Chains: A, B
Molecule details ›
Chains: A, B
Length: 271 amino acids
Theoretical weight: 28.79 KDa
Source organism: Vibrio cholerae O1 biovar El Tor str. N16961
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q9KST7 (Residues: 1-268; Coverage: 100%)
Gene names: VC_1169, trpA
Sequence domains: Tryptophan synthase alpha chain
Structure domains: Aldolase class I

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P212121
Unit cell:
a: 57.594Å b: 60.38Å c: 141.197Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.182 0.179 0.233
Expression system: Escherichia coli BL21