Structure of PDB 8h09 Chain B Binding Site BS03

Receptor Information
>8h09 Chain B (length=386) Species: 663 (Vibrio alginolyticus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SAAEVVSAQENQTYTYVRCWYRTSHSKDDAATDWKWAKNQDGSDFTIDGY
WWSSVSFKNMFYTNTSQNVIRQRCEETLDLANENADITFFAADNRYSYNH
TIWSNDAAMQPDQINKVVALGDSLSDTGNIFNASQWRFPNPNSWFLGHFS
NGFVWTEYVAKAKNLPLYNWAVGGAAGENQYIALTGVGEQVSSYLTYTKL
AKNYNPANTLFTLEFGLNDFMNYNRSVPEVKADYAEALIRLTDAGAKNFM
LMTLPDATKAPQFKYSTQEEIETIRAKVLKMNEFIKAQAMYYKAQGYNIA
LFDTHALFEKLTSAPEEHGFVNASDPCLDINRSSSVDYMYTHSLRSECAA
SGADKFVFWDVTHPTTATHRYVAEKMLESSNNLEEF
Ligand information
Ligand IDMG
InChIInChI=1S/Mg/q+2
InChIKeyJLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mg+2]
CACTVS 3.341[Mg++]
FormulaMg
NameMAGNESIUM ION
ChEMBL
DrugBankDB01378
ZINC
PDB chain8h09 Chain B Residue 507 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB8h09 Catalytic site flexibility facilitates the substrate and catalytic promiscuity of Vibrio dual lipase/transferase.
Resolution1.81 Å
Binding residue
(original residue number in PDB)
E208 D263
Binding residue
(residue number reindexed from 1)
E178 D233
Annotation score4
Enzymatic activity
Enzyme Commision number ?
Gene Ontology
Molecular Function
GO:0016298 lipase activity
GO:0016788 hydrolase activity, acting on ester bonds
Biological Process
GO:0006629 lipid metabolic process

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Molecular Function

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Biological Process
External links
PDB RCSB:8h09, PDBe:8h09, PDBj:8h09
PDBsum8h09
PubMed37558668
UniProtA0A7Y4B3E8

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