› 5t3d

X-ray diffraction
2.8Å resolution

Crystal structure of holo-EntF a nonribosomal peptide synthetase in the thioester-forming conformation

Released:
DOI: 10.2210/pdb5t3d/pdb
PDB entry 5t3d coloured by chain, front view.
PDB entry 5t3d coloured by chain, side view.
PDB entry 5t3d coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Structures of two distinct conformations of holo-non-ribosomal peptide synthetases.
Drake EJ, Miller BR, Shi C, Tarrasch JT, Sundlov JA, Allen CL, Skiniotis G, Aldrich CC, Gulick AM
Nature 529 235-8 (2016)
PMID: 26762461

Function and Biology Details

Reactions catalysed: 
(1a) ATP + L-serine = diphosphate + (L-seryl)adenylate
6 ATP + 3 2,3-dihydroxybenzoate + 3 L-serine = enterobactin + 6 AMP + 6 diphosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145843 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Enterobactin synthase component F Chain: A
Molecule details ›
Chain: A
Length: 1295 amino acids
Theoretical weight: 142.31 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P11454 (Residues: 1-1293; Coverage: 100%)
Gene names: JW0578, b0586, entF
Sequence domains:

Ligands and Environments

1 bound ligand:
Ligand 75C 1 x 75C
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-B
Spacegroup: P41212
Unit cell:
a: 127.711Å b: 127.711Å c: 186.94Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.188 0.185 0.232
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

25 review citations

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

11 mentions without citation

Nonribosomal peptide synthetases and their biotechnological potential in Penicillium rubens.
Iacovelli et al. (2021)
10 more