› 5hy5

X-ray diffraction
2.68Å resolution

Crystal Structure of a Tryptophan 6-halogenase (SttH) from Streptomyces toxytricini

Released:
DOI: 10.2210/pdb5hy5/pdb
PDB entry 5hy5 coloured by chain, front view.
PDB entry 5hy5 coloured by chain, side view.
PDB entry 5hy5 coloured by chain, top view.
Source organism: Streptomyces toxytricini
Primary publication:
A Structure-Guided Switch in the Regioselectivity of a Tryptophan Halogenase.
Shepherd SA, Menon BR, Fisk H, Struck AW, Levy C, Leys D, Micklefield J
Chembiochem 17 821-4 (2016)
PMID: 26840773

Function and Biology Details

Reaction catalysed: 
D-tryptophan + FADH(2) + chloride + O(2) + H(+) = 6-chloro-D-tryptophan + FAD + 2 H(2)O
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-123191 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tryptophan 6-halogenase SttH Chains: A, B
Molecule details ›
Chains: A, B
Length: 523 amino acids
Theoretical weight: 58.79 KDa
Source organism: Streptomyces toxytricini
Expression system: Escherichia coli
UniProt:
  • Canonical: E9P162 (Residues: 1-523; Coverage: 100%)
Gene name: sttH
Sequence domains: Tryptophan halogenase
Structure domains: FAD/NAD(P)-binding domain

Ligands and Environments

2 bound ligands:
Ligand FAD 2 x FAD
Ligand CL 2 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I24
Spacegroup: C2
Unit cell:
a: 171.66Å b: 101.57Å c: 83.12Å
α: 90° β: 99.08° γ: 90°
R-values:
R R work R free
0.198 0.196 0.232
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Enzymatic site-selectivity enabled by structure-guided directed evolution.
Wang et al. (2017)
7 more

10 mentions without citation

Enzymatic Halogenation and Dehalogenation Reactions: Pervasive and Mechanistically Diverse.
Agarwal et al. (2017)
9 more