› 4g8b

X-ray diffraction
1.3Å resolution

Crystal structures of N-acyl homoserine lactonase AidH S102G mutant complexed with N-hexanoyl homoserine lactone

Released:
DOI: 10.2210/pdb4g8b/pdb
PDB entry 4g8b coloured by chain, front view.
PDB entry 4g8b coloured by chain, side view.
PDB entry 4g8b 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: 30.62 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 HL6 2 x HL6
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P21
Unit cell:
a: 42.385Å b: 130.075Å c: 44.254Å
α: 90° β: 110.68° γ: 90°
R-values:
R R work R free
0.15 0.122 0.159
Expression system: Escherichia coli

Quick links

Citations

4 review citations

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

5 mentions without citation

How the Same Core Catalytic Machinery Catalyzes 17 Different Reactions: the Serine-Histidine-Aspartate Catalytic Triad of α/β-Hydrolase Fold Enzymes.
Rauwerdink et al. (2015)
4 more