Structure of PDB 6vl0 Chain A Binding Site BS01
Receptor Information
>6vl0 Chain A (length=429) Species:
37319
(Pseudo-nitzschia multiseries) [
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ESPKEVLSRVQDAGLTLTNPNDLYWMVDFLKEKYYDNGDYYYPIKTVCDG
ESIDVKFYCPFEPSLSPHYLELYGSRDERASIYETTMKKYNRINSEKTSA
ICTPYSSYGDTQIVAYFYSMMYYINDQTAHLKLPESEIESELIDILNDDI
LIYLNEFMSIFEPEDAQDLERIWDFLDFYQPYFSKVDGKIVLDEKYLVRT
PSQMPLIKTICEYVSEQFAPSKNITQVIWEVVRYIKGVKDEIHIRGDKSF
TLSLQEYDDFRDKVTASPMAHAVSDLTHERFSYEAYTNPAFMELENRCSE
IITYFNDVCTSDRERLDEDPFNSVFILMDLDPSLNFAKSCDVVVEHAYNK
MQAFLKLKEEILESASDEEERLALARMIKTREDSLIGYVLHEVCCVEDGY
ARDHKPLMKAFLEEEITKSLAEKVKFNPV
Ligand information
Ligand ID
MN
InChI
InChI=1S/Mn/q+2
InChIKey
WAEMQWOKJMHJLA-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mn+2]
CACTVS 3.341
[Mn++]
Formula
Mn
Name
MANGANESE (II) ION
ChEMBL
DrugBank
DB06757
ZINC
PDB chain
6vl0 Chain A Residue 501 [
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Receptor-Ligand Complex Structure
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PDB
6vl0
Algal neurotoxin biosynthesis repurposes the terpene cyclase structural fold into anN-prenyltransferase.
Resolution
2.2 Å
Binding residue
(original residue number in PDB)
N351 T355 E359
Binding residue
(residue number reindexed from 1)
N306 T310 E314
Annotation score
1
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
PDBsum
6vl0
PubMed
32457155
UniProt
A0A386KZ50
|DABA_PSEMU Magnesium-dependent glutamate N-prenyltransferase (Gene Name=dabA)
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