› 6t6x

X-ray diffraction
1.25Å resolution

Structure of the Bottromycin epimerase BotH in complex with substrate

Released:
DOI: 10.2210/pdb6t6x/pdb
PDB entry 6t6x coloured by chain, front view.
PDB entry 6t6x coloured by chain, side view.
PDB entry 6t6x 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

1 bound ligand:
Ligand MQW 1 x MQW
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PETRA III, DESY BEAMLINE P11
Spacegroup: I222
Unit cell:
a: 66.655Å b: 80.285Å c: 89.337Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.167 0.166 0.175
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