Structure of PDB 8qn3 Chain A

Receptor sequence
>8qn3A (length=364) Species: 4081 (Solanum lycopersicum) [Search protein sequence]
NPLFSPYKMGKFNLSHRVVLAPMTRCRALNNIPQAALGEYYEQRATAGGF
LITEGTMISPTSAGFPHVPGIFTKEQVREWKKIVDVVHAKGAVIFCQLWH
VGRASHEVYQPAGAAPISSTEKPISNRWRILMPDGTHGIYPKPRAIGTYE
ISQVVEDYRRSALNAIEAGFDGIEIHGAHGYLIDQFLKDGINDRTDEYGG
SLANRCKFITQVVQAVVSAIGADRVGVRVSPAIDHLDAMDSNPLSLGLAV
VERLNKIQLHSGSKLAYLHVTQPRYVAYGQTARLMRTLRNAYQGTFICSG
GYTRELGIEAVAQGDADLVSYGRLFISNPDLVMRIKLNAPLNKYNRKTFY
TQDPVVGYTDYPFL
3D structure
PDB8qn3 Loop 6 and the beta-hairpin flap are structural hotspots that determine cofactor specificity in the FMN-dependent family of ene-reductases
ChainA
Resolution1.75 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.3.1.42: 12-oxophytodienoate reductase.
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 FMN A P31 M32 T33 Q106 H185 H188 R237 S319 G320 G321 G342 R343 Y370 P22 M23 T24 Q97 H176 H179 R228 S299 G300 G301 G322 R323 Y350
BS02 WI6 A W108 H185 H188 Y190 H244 R283 W99 H176 H179 Y181 H235 R274
Gene Ontology
Molecular Function
GO:0010181 FMN binding
GO:0016491 oxidoreductase activity
GO:0016629 12-oxophytodienoate reductase activity
GO:0042802 identical protein binding
Biological Process
GO:0006633 fatty acid biosynthetic process
GO:0009695 jasmonic acid biosynthetic process
GO:0031408 oxylipin biosynthetic process
Cellular Component
GO:0005777 peroxisome

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:8qn3, PDBe:8qn3, PDBj:8qn3
PDBsum8qn3
PubMed38263933
UniProtQ9FEW9|OPR3_SOLLC 12-oxophytodienoate reductase 3 (Gene Name=OPR3)

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