Structure of PDB 4j5h Chain A

Receptor sequence
>4j5hA (length=250) Species: 1428 (Bacillus thuringiensis) [Search protein sequence]
MTVKKLYFIPAGRCMLDHSSVNSALTPGKLLNLPVWCYLLETEEGPILVD
TGMPESAVNNEGLFNGTFVEGQILPKMTEEDRIVNILKRVGYEPDDLLYI
ISSHLHWDHAGGNGAFTNTPIIVQRTEYEAALHREEYMKECILPHLNYKI
IEGDYEVVPGVQLLYTPGHSPGHQSLFIETEQSGSVLLTIDASYTKENFE
DEVPFAGFDPELALSSIKRLKEVVKKEKPIIFFGHDIEQEKSCRVFPEYI
3D structure
PDB4j5h A phenylalanine clamp controls substrate specificity in the quorum-quenching metallo-gamma-lactonase from Bacillus thuringiensis.
ChainA
Resolution1.45 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.1.1.81: quorum-quenching N-acyl-homoserine lactonase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 ZN A H109 D191 H235 H109 D191 H235
BS02 ZN A H104 H106 H169 D191 H104 H106 H169 D191
BS03 1K4 A T67 F68 H106 W107 D108 H109 H169 D191 Y194 T67 F68 H106 W107 D108 H109 H169 D191 Y194
Gene Ontology
Molecular Function
GO:0016787 hydrolase activity
GO:0046872 metal ion binding
GO:0102007 acyl-L-homoserine-lactone lactonohydrolase activity
Biological Process
GO:1901335 lactone catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:4j5h, PDBe:4j5h, PDBj:4j5h
PDBsum4j5h
PubMed23387521
UniProtA3FJ64|AHLL_BACTU N-acyl homoserine lactonase (Gene Name=aiiA)

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