› 5es6

X-ray diffraction
2.46Å resolution

Crystal structure of the first two domains of the initiation module of LgrA

Released:
DOI: 10.2210/pdb5es6/pdb
Model geometry
Fit model/data
PDB entry 5es6 coloured by chain, front view.
PDB entry 5es6 coloured by chain, side view.
PDB entry 5es6 coloured by chain, top view.
Source organism: Brevibacillus parabrevis
Primary publication:
Synthetic cycle of the initiation module of a formylating nonribosomal peptide synthetase.
Reimer JM, Aloise MN, Harrison PM, Schmeing TM
Nature 529 239-42 (2016)
PMID: 26762462

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-180704 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Linear gramicidin synthase subunit A Chain: A
Molecule details ›
Chain: A
Length: 685 amino acids
Theoretical weight: 77.58 KDa
Source organism: Brevibacillus parabrevis
Expression system: Escherichia coli
UniProt:
  • Canonical: Q70LM7 (Residues: 2-684; Coverage: 30%)
Gene name: lgrA
Sequence domains:

Ligands and Environments

1 bound ligand:
Ligand FMT 3 x FMT
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: CLSI BEAMLINE 08ID-1
Spacegroup: P41212
Unit cell:
a: 161.32Å b: 161.32Å c: 138.19Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.224 0.222 0.251
Expression system: Escherichia coli

Quick links

Citations

21 review citations

Nonribosomal Peptide Synthesis-Principles and Prospects.
Süssmuth et al. (2017)
20 more

3 mentions without citation

Structural advances toward understanding the catalytic activity and conformational dynamics of modular nonribosomal peptide synthetases.
Patel et al. (2023)
2 more