Structure of PDB 6vl0 Chain A Binding Site BS01

Receptor Information
>6vl0 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 IDMN
InChIInChI=1S/Mn/q+2
InChIKeyWAEMQWOKJMHJLA-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mn+2]
CACTVS 3.341[Mn++]
FormulaMn
NameMANGANESE (II) ION
ChEMBL
DrugBankDB06757
ZINC
PDB chain6vl0 Chain A Residue 501 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB6vl0 Algal neurotoxin biosynthesis repurposes the terpene cyclase structural fold into anN-prenyltransferase.
Resolution2.2 Å
Binding residue
(original residue number in PDB)
N351 T355 E359
Binding residue
(residue number reindexed from 1)
N306 T310 E314
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:6vl0, PDBe:6vl0, PDBj:6vl0
PDBsum6vl0
PubMed32457155
UniProtA0A386KZ50|DABA_PSEMU Magnesium-dependent glutamate N-prenyltransferase (Gene Name=dabA)

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