› 6t70

X-ray diffraction
1.58Å resolution

Structure of the Bottromycin epimerase BotH in complex with Bottromycin A2 derivative

Released:
DOI: 10.2210/pdb6t70/pdb
PDB entry 6t70 coloured by chain, front view.
PDB entry 6t70 coloured by chain, side view.
PDB entry 6t70 coloured by chain, top view.
Source organism: Streptomyces sp. BC16019
Primary publication:
The bottromycin epimerase BotH defines a group of atypical α/β-hydrolase-fold enzymes.
Sikandar A, Franz L, Adam S, Santos-Aberturas J, Horbal L, Luzhetskyy A, Truman AW, Kalinina OV, Koehnke J
Nat Chem Biol 16 1013-1018 (2020)
PMID: 32601484

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-125550 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
AB hydrolase-1 domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 310 amino acids
Theoretical weight: 33.09 KDa
Source organism: Streptomyces sp. BC16019
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: K4MHV9 (Residues: 2-293; Coverage: 100%)
Gene name: botH
Sequence domains: alpha/beta hydrolase fold

Ligands and Environments

5 bound ligands:
Ligand CL 1 x CL
Ligand GOL 2 x GOL
Ligand SO4 1 x SO4
Ligand ZN 1 x ZN
Ligand MQZ 1 x MQZ
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06DA
Spacegroup: I222
Unit cell:
a: 66.544Å b: 79.43Å c: 88.444Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.168 0.166 0.2
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

New developments in RiPP discovery, enzymology and engineering.
Montalbán-López et al. (2021)
3 more