Structure of PDB 1no3 Chain A

Receptor sequence
>1no3A (length=851) Species: 3847 (Glycine max) [Search protein sequence]
HRGHKIKGTVVLMRKNVLDVNSVTSVGGIIGQGLDLVGSTLDTLTAFLGR
SVSLQLISATKADANGKGKLGKATFLEGIITSLPTLGAGQSAFKINFEWD
DGSGIPGAFYIKNFMQTEFFLVSLTLEDIPNHGSIHFVCNSWIYNAKLFK
SDRIFFANQTYLPSETPAPLVKYREEELHNLRGDGTGERKEWERIYDYDV
YNDLGDPDKGENHARPVLGGNDTFPYPRRGRTGRKPTRKDPNSESRSNDV
YLPRDEAFGHLKSSDFLTYGLKSVSQNVLPLLQSAFDLNFTPREFDSFDE
VHGLYSGGIKLPTDIISKISPLPVLKEIFRTDGEQALKFPPPKVIQVSKS
AWMTDEEFAREMLAGVNPNLIRCLKDFPPRSKLDSQVYGDHTSQITKEHL
EPNLEGLTVDEAIQNKRLFLLDHHDPIMPYLRRINATSTKAYATRTILFL
KNDGTLRPLAIELSLPHPQGDQSGAFSQVFLPADEGVESSIWLLAKAYVV
VNDSCYHQLVSHWLNTHAVVEPFIIATNRHLSVVHPIYKLLHPHYRDTMN
INGLARLSLVNDGGVIEQTFLWGRYSVEMSAVVYKDWVFTDQALPADLIK
RGMAIEDPSCPHGIRLVIEDYPYTVDGLEIWDAIKTWVHEYVFLYYKSDD
TLREDPELQACWKELVEVGHGDKKNEPWWPKMQTREELVEACAIIIWTAS
ALHAAVNFGQYPYGGLILNRPTLSRRFMPEKGSAEYEELRKNPQKAYLKT
ITPKFQTLIDLSVIEILSRHASDEVYLGERDNPNWTSDTRALEAFKRFGN
KLAQIENKLSERNNDEKLRNRCGPVQMPYTLLLPSSKEGLTFRGIPNSIS
I
3D structure
PDB1no3 Soybean lipoxygenase-3 in complex with 4-nitrocatechol.
ChainA
Resolution2.15 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) H512 H517 H703 N707 I851
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 FE A H518 H523 H709 N713 I857 H512 H517 H703 N707 I851
BS02 4NC A Q514 H518 W519 H523 I557 L565 L773 I857 Q508 H512 W513 H517 I551 L559 L767 I851
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:1no3, PDBe:1no3, PDBj:1no3
PDBsum1no3
PubMed14993710
UniProtP09186|LOX3_SOYBN Seed linoleate 9S-lipoxygenase-3 (Gene Name=LOX1.3)

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