› 6ulx

X-ray diffraction
2.31Å resolution

Adenylation domain of a keto acid-selecting NRPS module bound to keto acyl adenylate space group P43212

Released:
DOI: 10.2210/pdb6ulx/pdb
PDB 6ulx coloured by chain and viewed from the front.
PDB 6ulx coloured by chain and viewed from the side.
PDB 6ulx coloured by chain and viewed from the top.
Source organism: Bacillus stratosphericus LAMA 585
Primary publication:
Structural basis of keto acid utilization in nonribosomal depsipeptide synthesis.
Alonzo DA, Chiche-Lapierre C, Tarry MJ, Wang J, Schmeing TM
Nat Chem Biol 16 493-496 (2020)
PMID: 32066969

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Amino acid adenylation domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 576 amino acids
Theoretical weight: 63.94 KDa
Source organism: Bacillus stratosphericus LAMA 585
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: M5R382 (Residues: 83-649; Coverage: 17%)
Gene name: C883_1060
Sequence domains: AMP-binding enzyme

Ligands and Environments

2 bound ligands:
Ligand QA7 1 x QA7
Ligand SO4 17 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: P43212
Unit cell:
a: 103.274Å b: 103.274Å c: 172.747Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.223 0.222 0.249
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

The inherent flexibility of type I non-ribosomal peptide synthetase multienzymes drives their catalytic activities.
Bonhomme et al. (2021)
1 more