› 8uw6

X-ray diffraction
1.8Å resolution

Acetylornithine deacetylase from Escherichia coli, di-zinc form.

Released:
DOI: 10.2210/pdb8uw6/pdb
PDB entry 8uw6 coloured by chain, front view.
PDB entry 8uw6 coloured by chain, side view.
PDB entry 8uw6 coloured by chain, top view.
Source organism: Escherichia coli str. K-12 substr. MG1655
Primary publication:
N α -acetyl-L-ornithine deacetylase from Escherichia coli and a ninhydrin-based assay to enable inhibitor identification.
Kelley EH, Osipiuk J, Korbas M, Endres M, Bland A, Ehrman V, Joachimiak A, Olsen KW, Becker DP
Front Chem 12 1415644 (2024)
PMID: 39055043

Function and Biology Details

Reaction catalysed: 
N(2)-acetyl-L-ornithine + H(2)O = acetate + L-ornithine
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-199654 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acetylornithine deacetylase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 386 amino acids
Theoretical weight: 42.74 KDa
Source organism: Escherichia coli str. K-12 substr. MG1655
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P23908 (Residues: 1-383; Coverage: 100%)
Gene names: JW3929, argE, b3957
Sequence domains:

Ligands and Environments

4 bound ligands:
Ligand ZN 10 x ZN
Ligand SO4 5 x SO4
Ligand TRS 6 x TRS
Ligand EDO 2 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS-II BEAMLINE 17-ID-1
Spacegroup: P21
Unit cell:
a: 52.399Å b: 126.323Å c: 123.408Å
α: 90° β: 90.88° γ: 90°
R-values:
R R work R free
0.165 0.163 0.203
Expression system: Escherichia coli BL21(DE3)

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