Structure of PDB 1n8q Chain A

Receptor sequence
>1n8qA (length=849) Species: 3847 (Glycine max) [Search protein sequence]
GHKIKGTVVLMRKNVLDVNSVTSVGGIIGQGLDLVGSTLDTLTAFLGRSV
SLQLISATKADANGKGKLGKATFLEGIITSLPTLGAGQSAFKINFEWDDG
SGIPGAFYIKNFMQTEFFLVSLTLEDIPNHGSIHFVCNSWIYNAKLFKSD
RIFFANQTYLPSETPAPLVKYREEELHNLRGDGTGERKEWERIYDYDVYN
DLGDPDKGENHARPVLGGNDTFPYPRRGRTGRKPTRKDPNSESRSNDVYL
PRDEAFGHLKSSDFLTYGLKSVSQNVLPLLQSAFDLNFTPREFDSFDEVH
GLYSGGIKLPTDIISKISPLPVLKEIFRTDGEQALKFPPPKVIQVSKSAW
MTDEEFAREMLAGVNPNLIRCLKDFPPRSKLDSQVYGDHTSQITKEHLEP
NLEGLTVDEAIQNKRLFLLDHHDPIMPYLRRINATSTKAYATRTILFLKN
DGTLRPLAIELSLPHPQGDQSGAFSQVFLPADEGVESSIWLLAKAYVVVN
DSCYHQLVSHWLNTHAVVEPFIIATNRHLSVVHPIYKLLHPHYRDTMNIN
GLARLSLVNDGGVIEQTFLWGRYSVEMSAVVYKDWVFTDQALPADLIKRG
MAIEDPSCPHGIRLVIEDYPYTVDGLEIWDAIKTWVHEYVFLYYKSDDTL
REDPELQACWKELVEVGHGDKKNEPWWPKMQTREELVEACAIIIWTASAL
HAAVNFGQYPYGGLILNRPTLSRRFMPEKGSAEYEELRKNPQKAYLKTIT
PKFQTLIDLSVIEILSRHASDEVYLGERDNPNWTSDTRALEAFKRFGNKL
AQIENKLSERNNDEKLRNRCGPVQMPYTLLLPSSKEGLTFRGIPNSISI
3D structure
PDB1n8q Lipoxygenase interactions with natural flavonoid, quercetin, reveal a complex with protocatechuic acid in its X-ray structure at 2.1 A resolution.
ChainA
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
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 FE2 A H518 H523 H709 N713 I857 H510 H515 H701 N705 I849
BS02 DHB A Q514 H518 W519 H523 V566 I572 L773 I857 Q506 H510 W511 H515 V558 I564 L765 I849
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1n8q, PDBe:1n8q, PDBj:1n8q
PDBsum1n8q
PubMed14705020
UniProtP09186|LOX3_SOYBN Seed linoleate 9S-lipoxygenase-3 (Gene Name=LOX1.3)

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