PDBe 4w1y

X-ray diffraction
3.2Å resolution

Crystal structure of Escherichia coli Tryptophanase in 'semi-holo' form

Released:
Source organism: Escherichia coli K-12
Primary publication:
Structures of Escherichia coli tryptophanase in holo and `semi-holo' forms.
Acta Crystallogr F Struct Biol Commun 71 286-90 (2015)
PMID: 25760702

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Tryptophanase Chain: A
Molecule details ›
Chain: A
Length: 467 amino acids
Theoretical weight: 52.54 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A853 (Residues: 5-471; Coverage: 99%)
Gene names: JW3686, b3708, ind, tnaA
Sequence domains: Beta-eliminating lyase
Tryptophanase Chain: B
Molecule details ›
Chain: B
Length: 467 amino acids
Theoretical weight: 52.31 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A853 (Residues: 5-471; Coverage: 99%)
Gene names: JW3686, b3708, ind, tnaA
Sequence domains: Beta-eliminating lyase

Ligands and Environments

1 bound ligand:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: P43212
Unit cell:
a: 109.971Å b: 109.971Å c: 238.403Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.218 0.214 0.29
Expression system: Escherichia coli