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Ligands
Code Name Style Show Link
EDO 1,2-ethanediol
MYR Myristic acid
Non-standard Residues
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Glycosylation
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Code : 3SRA   PDBj   RCSB PDB   PDBe
Header : HYDROLASE
Title : Structure of Pseudomonas aerugionsa PvdQ covalently acylated with myristic acid from PVDIq
Release Data : 2011-09-21
Compound :
mol_id molecule chains synonym
1 Acyl-homoserine lactone acylase PvdQ subunit alpha A Acyl-HSL acylase PvdQ subunit alpha
fragment: alpha subunit (UNP residues 29-191)
mol_id molecule chains synonym
2 Acyl-homoserine lactone acylase PvdQ subunit beta B Acyl-HSL acylase PvdQ subunit beta
fragment: beta subunit (UNP residues 217-762)
Source :
mol_id organism_scientific expression_system
1 Pseudomonas aeruginosa PAO1  (taxid:208964) Escherichia coli  (taxid:469008)
strain: PAO1
gene: pvdQ, qsc112, PA2385
expression_system_strain: BL21(DE3)
expression_system_vector_type: pET15bTEV
expression_system_plasmid: pED485
mol_id organism_scientific expression_system
2 Pseudomonas aeruginosa PAO1  (taxid:208964) Escherichia coli  (taxid:469008)
strain: PAO1
gene: pvdQ, qsc112, PA2385
expression_system_strain: BL21(DE3)
expression_system_vector_type: pET15bTEV
expression_system_plasmid: pED485
Authors : Gulick, A.M., Drake, E.J.
Keywords : nrps tailoring, acylase, HYDROLASE
Exp. method : X-RAY DIFFRACTION ( 2.30 Å )
Citation :

Structural Characterization and High-Throughput Screening of Inhibitors of PvdQ, an NTN Hydrolase Involved in Pyoverdine Synthesis.

Drake, E.J.,Gulick, A.M.
(2011)  Acs Chem.Biol.  6 : 1277 - 1286

PubMed: 21892836
DOI: 10.1021/cb2002973

Chain : B
UniProt : Q9I194 (PVDQ_PSEAE)
Reaction: EC: Evidence:
Physiological Direction:
an N-acyl-L-homoserine lactone + H2O = a carboxylate + L- homoserine lactone 3.5.1.97 -
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