› 3e1t

X-ray diffraction
2.05Å resolution

Structure and action of the myxobacterial chondrochloren halogenase CndH, a new variant of FAD-dependent halogenases

Released:
DOI: 10.2210/pdb3e1t/pdb
PDB entry 3e1t coloured by chain, front view.
PDB entry 3e1t coloured by chain, side view.
PDB entry 3e1t coloured by chain, top view.
Source organism: Chondromyces crocatus
Primary publication:
Structure and action of the myxobacterial chondrochloren halogenase CndH: a new variant of FAD-dependent halogenases.
Buedenbender S, Rachid S, Müller R, Schulz GE
J Mol Biol 385 520-30 (2009)
PMID: 19000696

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-163501 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Halogenase Chain: A
Molecule details ›
Chain: A
Length: 512 amino acids
Theoretical weight: 57.28 KDa
Source organism: Chondromyces crocatus
Expression system: Escherichia coli
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand CL 1 x CL
Ligand FAD 1 x FAD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P212121
Unit cell:
a: 51.918Å b: 99.213Å c: 101.774Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.223 0.222 0.271
Expression system: Escherichia coli

Quick links

Citations

9 review citations

Explorations of catalytic domains in non-ribosomal peptide synthetase enzymology.
Hur et al. (2012)
8 more

8 mentions without citation

Halogenases: a palette of emerging opportunities for synthetic biology-synthetic chemistry and C-H functionalisation.
Crowe et al. (2021)
7 more