› 4mdt

X-ray diffraction
2.59Å resolution

Structure of LpxC bound to the reaction product UDP-(3-O-(R-3-hydroxymyristoyl))-glucosamine

Released:
DOI: 10.2210/pdb4mdt/pdb
PDB entry 4mdt coloured by chain, front view.
PDB entry 4mdt coloured by chain, side view.
PDB entry 4mdt coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structure of the bacterial deacetylase LpxC bound to the nucleotide reaction product reveals mechanisms of oxyanion stabilization and proton transfer.
Clayton GM, Klein DJ, Rickert KW, Patel SB, Kornienko M, Zugay-Murphy J, Reid JC, Tummala S, Sharma S, Singh SB, Miesel L, Lumb KJ, Soisson SM
J Biol Chem 288 34073-34080 (2013)
PMID: 24108127

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-164812 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 305 amino acids
Theoretical weight: 33.98 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand ZN 4 x ZN
Ligand 24G 4 x 24G
Ligand PO4 4 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: C2
Unit cell:
a: 168.973Å b: 103.52Å c: 103.968Å
α: 90° β: 103.96° γ: 90°
R-values:
R R work R free
0.199 0.197 0.24
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

LpxC inhibitors: a patent review (2010-2016).
Kalinin et al. (2017)
2 more

7 mentions without citation

Targeting Metalloenzymes for Therapeutic Intervention.
Chen et al. (2019)
6 more