› 4g9e

X-ray diffraction
1.09Å resolution

Crystal structures of N-acyl homoserine lactonase AidH complexed with N-butanoyl homoserine

Released:
DOI: 10.2210/pdb4g9e/pdb
PDB entry 4g9e coloured by chain, front view.
PDB entry 4g9e coloured by chain, side view.
PDB entry 4g9e coloured by chain, top view.
Source organism: Ochrobactrum sp. T63
Primary publication:
High-resolution structures of AidH complexes provide insights into a novel catalytic mechanism for N-acyl homoserine lactonase.
Gao A, Mei GY, Liu S, Wang P, Tang Q, Liu YP, Wen H, An XM, Zhang LQ, Yan XX, Liang DC
Acta Crystallogr D Biol Crystallogr 69 82-91 (2013)
PMID: 23275166

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-112364 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
AB hydrolase-1 domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 279 amino acids
Theoretical weight: 30.65 KDa
Source organism: Ochrobactrum sp. T63
Expression system: Escherichia coli
UniProt:
  • Canonical: D2J2T6 (Residues: 1-271; Coverage: 100%)
Gene name: aidH
Sequence domains: alpha/beta hydrolase fold
Structure domains: alpha/beta hydrolase

Ligands and Environments

1 bound ligand:
Ligand C4L 2 x C4L
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P21
Unit cell:
a: 42.164Å b: 129.523Å c: 44.312Å
α: 90° β: 111° γ: 90°
R-values:
R R work R free
0.15 0.127 0.152
Expression system: Escherichia coli

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Citations

4 review citations

Quorum quenching: role in nature and applied developments.
Grandclément et al. (2016)
3 more

1 mention without citation

High-resolution structures of AidH complexes provide insights into a novel catalytic mechanism for N-acyl homoserine lactonase.
Gao et al. (2013)