Structure of PDB 1rrl Chain B Binding Site BS01

Receptor Information
>1rrl Chain B (length=850) Species: 3847 (Glycine max) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
RGHKIKGTVVLMRKNVLDVNSVTSVGGIIGQGLDLVGSTLDTLTAFLGRS
VSLQLISATKADANGKGKLGKATFLEGIITSLPTLGAGQSAFKINFEWDD
GSGIPGAFYIKNFMQTEFFLVSLTLEDIPNHGSIHFVCNSWIYNAKLFKS
DRIFFANQTYLPSETPAPLVKYREEELHNLRGDGTGERKEWERIYDYDVY
NDLGDPDKGENHARPVLGGNDTFPYPRRGRTGRKPTRKDPNSESRSNDVY
LPRDEAFGHLKSSDFLTYGLKSVSQNVLPLLQSAFDLNFTPREFDSFDEV
HGLYSGGIKLPTDIISKISPLPVLKEIFRTDGEQALKFPPPKVIQVSKSA
WMTDEEFAREMLAGVNPNLIRCLKDFPPRSKLDSQVYGDHTSQITKEHLE
PNLEGLTVDEAIQNKRLFLLDHHDPIMPYLRRINATSTKAYATRTILFLK
NDGTLRPLAIELSLPHPQGDQSGAFSQVFLPADEGVESSIWLLAKAYVVV
NDSCYHQLVSHWLNTHAVVEPFIIATNRHLSVVHPIYKLLHPHYRDTMNI
NGLARLSLVNDGGVIEQTFLWGRYSVEMSAVVYKDWVFTDQALPADLIKR
GMAIEDPSCPHGIRLVIEDYPYTVDGLEIWDAIKTWVHEYVFLYYKSDDT
LREDPELQACWKELVEVGHGDKKNEPWWPKMQTREELVEACAIIIWTASA
LHAAVNFGQYPYGGLILNRPTLSRRFMPEKGSAEYEELRKNPQKAYLKTI
TPKFQTLIDLSVIEILSRHASDEVYLGERDNPNWTSDTRALEAFKRFGNK
LAQIENKLSERNNDEKLRNRCGPVQMPYTLLLPSSKEGLTFRGIPNSISI
Ligand information
Ligand IDFE2
InChIInChI=1S/Fe/q+2
InChIKeyCWYNVVGOOAEACU-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Fe+2]
CACTVS 3.341[Fe++]
FormulaFe
NameFE (II) ION
ChEMBL
DrugBankDB14510
ZINC
PDB chain1rrl Chain B Residue 858 [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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PDB1rrl Effect of crystal freezing and small-molecule binding on internal cavity size in a large protein: X-ray and docking studies of lipoxygenase at ambient and low temperature at 2.0 A resolution.
Resolution2.09 Å
Binding residue
(original residue number in PDB)		H518 H523 H709 N713 I857
Binding residue
(residue number reindexed from 1)		H511 H516 H702 N706 I850
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) H518 H523 H709 N713 I857
Catalytic site (residue number reindexed from 1) H511 H516 H702 N706 I850
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
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Biological Process
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Cellular Component
External links
PDB RCSB:1rrl, PDBe:1rrl, PDBj:1rrl
PDBsum1rrl
PubMed16790932
UniProtP09186|LOX3_SOYBN Seed linoleate 9S-lipoxygenase-3 (Gene Name=LOX1.3)

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