Structure of PDB 6vl0 Chain A

Receptor sequence
>6vl0A (length=429) Species: 37319 (Pseudo-nitzschia multiseries) [Search protein sequence]
ESPKEVLSRVQDAGLTLTNPNDLYWMVDFLKEKYYDNGDYYYPIKTVCDG
ESIDVKFYCPFEPSLSPHYLELYGSRDERASIYETTMKKYNRINSEKTSA
ICTPYSSYGDTQIVAYFYSMMYYINDQTAHLKLPESEIESELIDILNDDI
LIYLNEFMSIFEPEDAQDLERIWDFLDFYQPYFSKVDGKIVLDEKYLVRT
PSQMPLIKTICEYVSEQFAPSKNITQVIWEVVRYIKGVKDEIHIRGDKSF
TLSLQEYDDFRDKVTASPMAHAVSDLTHERFSYEAYTNPAFMELENRCSE
IITYFNDVCTSDRERLDEDPFNSVFILMDLDPSLNFAKSCDVVVEHAYNK
MQAFLKLKEEILESASDEEERLALARMIKTREDSLIGYVLHEVCCVEDGY
ARDHKPLMKAFLEEEITKSLAEKVKFNPV
3D structure
PDB6vl0 Algal neurotoxin biosynthesis repurposes the terpene cyclase structural fold into anN-prenyltransferase.
ChainA
Resolution2.2 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.5.1.-
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 MN A N351 T355 E359 N306 T310 E314
BS02 GST A T143 Y163 M166 Y167 N170 R306 N351 R358 E359 Y433 R447 T98 Y118 M121 Y122 N125 R261 N306 R313 E314 Y388 R402
BS03 MG A E359 F366 E314 F321
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
View graph for
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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