Structure of PDB 1jnq Chain A Binding Site BS02

Receptor Information
>1jnq Chain A (length=849) Species: 3847 (Glycine max) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
GHKIKGTVVLMRKNVLDVNSVTSVGGIIGQGLDLVGSTLDTLTAFLGRSV
SLQLISATKADANGKGKLGKATFLEGIITSLPTLGAGQSAFKINFEWDDG
SGIPGAFYIKNFMQTEFFLVSLTLEDIPNHGSIHFVCNSWIYNAKLFKSD
RIFFANQTYLPSETPAPLVKYREEELHNLRGDGTGERKEWERIYDYDVYN
DLGDPDKGENHARPVLGGNDTFPYPRRGRTGRKPTRKDPNSESRSNDVYL
PRDEAFGHLKSSDFLTYGLKSVSQNVLPLLQSAFDLNFTPREFDSFDEVH
GLYSGGIKLPTDIISKISPLPVLKEIFRTDGEQALKFPPPKVIQVSKSAW
MTDEEFAREMLAGVNPNLIRCLKDFPPRSKLDSQVYGDHTSQITKEHLEP
NLEGLTVDEAIQNKRLFLLDHHDPIMPYLRRINATSTKAYATRTILFLKN
DGTLRPLAIELSLPHPQGDQSGAFSQVFLPADEGVESSIWLLAKAYVVVN
DSCYHQLVSHWLNTHAVVEPFIIATNRHLSVVHPIYKLLHPHYRDTMNIN
GLARLSLVNDGGVIEQTFLWGRYSVEMSAVVYKDWVFTDQALPADLIKRG
MAIEDPSCPHGIRLVIEDYPYTVDGLEIWDAIKTWVHEYVFLYYKSDDTL
REDPELQACWKELVEVGHGDKKNEPWWPKMQTREELVEACAIIIWTASAL
HAAVNFGQYPYGGLILNRPTLSRRFMPEKGSAEYEELRKNPQKAYLKTIT
PKFQTLIDLSVIEILSRHASDEVYLGERDNPNWTSDTRALEAFKRFGNKL
AQIENKLSERNNDEKLRNRCGPVQMPYTLLLPSSKEGLTFRGIPNSISI
Ligand information
Ligand IDEGT
InChIInChI=1S/C15H14O7/c16-7-3-9(17)8-5-12(20)15(22-13(8)4-7)6-1-10(18)14(21)11(19)2-6/h1-4,12,15-21H,5H2/t12-,15-/m1/s1
InChIKeyXMOCLSLCDHWDHP-IUODEOHRSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1c(cc(c(c1O)O)O)[C@@H]2[C@@H](Cc3c(cc(cc3O2)O)O)O
CACTVS 3.341O[C@@H]1Cc2c(O)cc(O)cc2O[C@@H]1c3cc(O)c(O)c(O)c3
ACDLabs 10.04Oc1cc(cc(O)c1O)C3Oc2cc(O)cc(O)c2CC3O
OpenEye OEToolkits 1.5.0c1c(cc(c(c1O)O)O)C2C(Cc3c(cc(cc3O2)O)O)O
CACTVS 3.341O[CH]1Cc2c(O)cc(O)cc2O[CH]1c3cc(O)c(O)c(O)c3
FormulaC15 H14 O7
Name2-(3,4,5-TRIHYDROXY-PHENYL)-CHROMAN-3,5,7-TRIOL;
EPIGALLOCATECHIN
ChEMBLCHEMBL47386
DrugBankDB03823
ZINCZINC000003870336
PDB chain1jnq Chain A Residue 871 [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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PDB1jnq Inhibition of lipoxygenase by (-)-epigallocatechin gallate: X-ray analysis at 2.1 A reveals degradation of EGCG and shows soybean LOX-3 complex with EGC instead.
Resolution2.1 Å
Binding residue
(original residue number in PDB)		Q514 H518 W519 H523 I557 L565 I572 F576 Q716 L773 I857
Binding residue
(residue number reindexed from 1)		Q506 H510 W511 H515 I549 L557 I564 F568 Q708 L765 I849
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) H518 H523 H709 N713 I857
Catalytic site (residue number reindexed from 1) H510 H515 H701 N705 I849
Enzyme Commision number 1.13.11.58: linoleate 9S-lipoxygenase.
Gene Ontology
Molecular Function
GO:0016491 oxidoreductase activity
GO:0016702 oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
GO:0046872 metal ion binding
GO:0051213 dioxygenase activity
GO:1990136 linoleate 9S-lipoxygenase activity
Biological Process
GO:0006633 fatty acid biosynthetic process
GO:0031408 oxylipin biosynthetic process
GO:0034440 lipid oxidation
Cellular Component
GO:0005737 cytoplasm

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1jnq, PDBe:1jnq, PDBj:1jnq
PDBsum1jnq
PubMed12964012
UniProtP09186|LOX3_SOYBN Seed linoleate 9S-lipoxygenase-3 (Gene Name=LOX1.3)

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