Structure of PDB 5eht Chain A

Receptor sequence
>5ehtA (length=253) Species: 1428 (Bacillus thuringiensis) [Search protein sequence]
GHMATVKKLYFVPAGRCMLDHSFVNSALTPGKLLNVPVWCYLLETEEGPI
LVDTGMPESAVNNEGLCNGTFGEGQILPKMTEEDRIVNILKRVGYEPDDL
LYIISSHLHFDHAGGNGAFTNTPIIVQRTEYEAALHREEYMTECILPHLN
YKIIEGDYEVVPGVQLLYTPGHSPGHQSLFIETEQSGSVLLTIDASYTKE
NFEDEVPFAGFDPELALSSIKRLKEVVKKEKPMIFFGHDIEQEKSCRVFP
EYI
3D structure
PDB5eht Conformational Tinkering Drives Evolution of a Promiscuous Activity through Indirect Mutational Effects.
ChainA
Resolution1.29 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 D108 H109 D191 H235 D111 H112 D194 H238
BS02 ZN A H104 H106 H169 H107 H109 H172
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

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:5eht, PDBe:5eht, PDBj:5eht
PDBsum5eht
PubMed27444875
UniProtA3FJ64|AHLL_BACTU N-acyl homoserine lactonase (Gene Name=aiiA)

[Back to BioLiP]