Structure of PDB 2hsa Chain B Binding Site BS01

Receptor Information
>2hsa Chain B (length=374) Species: 4081 (Solanum lycopersicum) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
PLFSPYKMGKFNLSHRVVLAPMTRCRALNNIPQAALGEYYEQRATAGGFL
ITEGTMISPTSAGFPHVPGIFTKEQVREWKKIVDVVHAKGAVIFCQLWHV
GRASHEVYQPAGAAPISSTEKPISNRWRILMPDGTHGIYPKPRAIGTYEI
SQVVEDYRRSALNAIEAGFDGIEIHGAHGYLIDQFLKDGINDRTDEYGGS
LANRCKFITQVVQAVVSAIGADRVGVRVSPAIDHLDAMDSNPLSLGLAVV
ERLNKIQLHSGSKLAYLHVTQPRYVAYGQTEAGRLGSEEEEARLMRTLRN
AYQGTFICSGGYTRELGIEAVAQGDADLVSYGRLFISNPDLVMRIKLNAP
LNKYNRKTFYTQDPVVGYTDYPFL
Ligand information
Ligand IDFMN
InChIInChI=1S/C17H21N4O9P/c1-7-3-9-10(4-8(7)2)21(15-13(18-9)16(25)20-17(26)19-15)5-11(22)14(24)12(23)6-30-31(27,28)29/h3-4,11-12,14,22-24H,5-6H2,1-2H3,(H,20,25,26)(H2,27,28,29)/t11-,12+,14-/m0/s1
InChIKeyFVTCRASFADXXNN-SCRDCRAPSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.6Cc1cc2c(cc1C)N(C3=NC(=O)NC(=O)C3=N2)CC(C(C(COP(=O)(O)O)O)O)O
OpenEye OEToolkits 1.7.6Cc1cc2c(cc1C)N(C3=NC(=O)NC(=O)C3=N2)C[C@@H]([C@@H]([C@@H](COP(=O)(O)O)O)O)O
ACDLabs 12.01N=2C(=O)NC(=O)C3=Nc1cc(C)c(C)cc1N(C=23)CC(O)C(O)C(O)COP(=O)(O)O
CACTVS 3.385Cc1cc2N=C3C(=O)NC(=O)N=C3N(C[CH](O)[CH](O)[CH](O)CO[P](O)(O)=O)c2cc1C
CACTVS 3.385Cc1cc2N=C3C(=O)NC(=O)N=C3N(C[C@H](O)[C@H](O)[C@H](O)CO[P](O)(O)=O)c2cc1C
FormulaC17 H21 N4 O9 P
NameFLAVIN MONONUCLEOTIDE;
RIBOFLAVIN MONOPHOSPHATE
ChEMBLCHEMBL1201794
DrugBankDB03247
ZINCZINC000003831425
PDB chain2hsa Chain B Residue 401 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB2hsa Crystal structure of 12-oxophytodienoate reductase 3 from tomato: Self-inhibition by dimerization.
Resolution1.5 Å
Binding residue
(original residue number in PDB)		A30 P31 M32 T33 G64 Q106 H185 R237 S319 G320 G321 G342 R343 Y370
Binding residue
(residue number reindexed from 1)		A20 P21 M22 T23 G54 Q96 H175 R227 S309 G310 G311 G332 R333 Y360
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) T33 H185 H188 Y190 R237 L245 Q289
Catalytic site (residue number reindexed from 1) T23 H175 H178 Y180 R227 L235 Q279
Enzyme Commision number 1.3.1.42: 12-oxophytodienoate reductase.
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:2hsa, PDBe:2hsa, PDBj:2hsa
PDBsum2hsa
PubMed16983071
UniProtQ9FEW9|OPR3_SOLLC 12-oxophytodienoate reductase 3 (Gene Name=OPR3)

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