› 1md9

X-ray diffraction
2.8Å resolution

CRYSTAL STRUCTURE OF DhbE IN COMPLEX WITH DHB AND AMP

Released:
DOI: 10.2210/pdb1md9/pdb
PDB 1md9 coloured by chain and viewed from the front.
PDB 1md9 coloured by chain and viewed from the side.
PDB 1md9 coloured by chain and viewed from the top.
Source organism: Bacillus subtilis
Primary publication:
Crystal structure of DhbE, an archetype for aryl acid activating domains of modular nonribosomal peptide synthetases.
May JJ, Kessler N, Marahiel MA, Stubbs MT
Proc. Natl. Acad. Sci. U.S.A. 99 12120-5 (2002)
PMID: 12221282

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
2,3-dihydroxybenzoate-AMP ligase Chain: A
Molecule details ›
Chain: A
Length: 539 amino acids
Theoretical weight: 60.36 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
  • Canonical: P40871 (Residues: 1-539; Coverage: 100%)
Gene names: BSU31980, dhbE, entE
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand AMP 1 x AMP
Ligand DBH 1 x DBH
1 modified residue:
Ligand MSE 8 x MSE

Experiments and Validation Details

Entry percentile scores
Spacegroup: P31
Unit cell:
a: 66.9Å b: 66.9Å c: 114.8Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.232 0.232 0.288
Expression system: Escherichia coli

Quick links

Citations

22 review citations

Biosynthesis of depsipeptides, or Depsi: The peptides with varied generations.
Alonzo et al. (2020)
21 more

6 mentions without citation

Module evolution and substrate specificity of fungal nonribosomal peptide synthetases involved in siderophore biosynthesis.
Bushley et al. (2008)
5 more