Structure of PDB 6vkz Chain A Binding Site BS02

Receptor Information
>6vkz Chain A (length=429) Species: 37319 (Pseudo-nitzschia multiseries) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ESPKEVLSRVQDAGLTLTNPNDLYWMVDFLKEKYYDNGDYYYPIKTVCDG
ESIDVKFYCPFEPSLSPHYLELYGSRDERASIYETTMKKYNRINSEKTSA
ICTPYSSYGDTQIVAYFYSMMYYINDQTAHLKLPESEIESELIDILNDDI
LIYLNEFMSIFEPEDAQDLERIWDFLDFYQPYFSKVDGKIVLDEKYLVRT
PSQMPLIKTICEYVSEQFAPSKNITQVIWEVVRYIKGVKDEIHIRGDKSF
TLSLQEYDDFRDKVTASPMAHAVSDLTHERFSYEAYTNPAFMELENRCSE
IITYFNDVCTSDRERLDEDPFNSVFILMDLDPSLNFAKSCDVVVEHAYNK
MQAFLKLKEEILESASDEEERLALARMIKTREDSLIGYVLHEVCCVEDGY
ARDHKPLMKAFLEEEITKSLAEKVKFNPV
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 chain6vkz Chain A Residue 502 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB6vkz Algal neurotoxin biosynthesis repurposes the terpene cyclase structural fold into anN-prenyltransferase.
Resolution2.1 Å
Binding residue
(original residue number in PDB)		E359 F366
Binding residue
(residue number reindexed from 1)		E314 F321
Annotation score1
Enzymatic activity
Enzyme Commision number 2.5.1.-
Gene Ontology
Molecular Function
GO:0016740 transferase activity
GO:0046872 metal ion binding
Biological Process
GO:0016036 cellular response to phosphate starvation
GO:0071244 cellular response to carbon dioxide

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Molecular Function
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Biological Process
External links
PDB RCSB:6vkz, PDBe:6vkz, PDBj:6vkz
PDBsum6vkz
PubMed32457155
UniProtA0A386KZ50|DABA_PSEMU Magnesium-dependent glutamate N-prenyltransferase (Gene Name=dabA)

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