Structure of PDB 5tr0 Chain A Binding Site BS01

Receptor Information
>5tr0 Chain A (length=820) Species: 3847 (Glycine max) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
HKIKGTVVLMPKNELEVNNLNAFLGRSVSLQLISATKADAHGKGKVGKDT
FLEGINTSLPTLGAGESAFNIHFEWDGSMGIPGAFYIKNYMQVEFFLKSL
TLEAISNQGTIRFVCNSWVYNTKLYKSVRIFFANHTYVPSETPAPLVEYR
EEELKSLRGNGTGERKEYDRIYDYDVYNDLGNPDKSEKLARPVLGGSSTF
PYPRRGRTGRGPTVTDPNTEKQGEVFYVPRDENLGHLKSKDALEIGTKSL
SQIVQPAFESAFDLKSTPIEFHSFQDVHDLYEGGIKLPRDVISTIIPLPV
IKELYRTDGQHILKFPQPHVVQVSQSAWMTDEEFAREMIAGVNPCVIRGL
EEFPPKSNLDPAIYGDQSSKITADSLDLDGYTMDEALGSRRLFMLDYHDI
FMPYVRQINQLNSAKTYATRTILFLREDGTLKPVAIELSLPHAVSQVVLP
AKEGVESTIWLLAKAYVIVNDSCYHQLMSHWLNTHAAMEPFVIATHRHLS
VLHPIYKLLTPHYRNNMNINALARQSLINANGIIETTFLPSKYSVEMSSA
VYKNWVFTDQALPADLIKRGVAIKDPSTPHGVRLLIEDYPYAADGLEIWA
AIKTWVQEYVPLYYARDDDVKNDSELQHWWKEAVEKGHGDLKDKPWWPKL
QTLEDLVEVCLIIIWIASALHAAVNFGQYPYGGLIMNRPTASRRLLPEKG
TPEYEEMINNHEKAYLRTITSKLPTLISLSVIEIASTHASDEVYLGQRDN
PHWTSDSKALQAFQKFGNKLKEIEEKLVRRNNDPSLQGNRLGPVQLPYTL
LYPSSEEGLTFRGIPNSISI
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 chain5tr0 Chain A Residue 901 [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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PDB5tr0 Biophysical Characterization of a Disabled Double Mutant of Soybean Lipoxygenase: The "Undoing" of Precise Substrate Positioning Relative to Metal Cofactor and an Identified Dynamical Network.
Resolution1.85 Å
Binding residue
(original residue number in PDB)		H499 H504 H690 N694 I839
Binding residue
(residue number reindexed from 1)		H480 H485 H671 N675 I820
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) H499 H504 H690 N694 I839
Catalytic site (residue number reindexed from 1) H480 H485 H671 N675 I820
Enzyme Commision number 1.13.11.12: linoleate 13S-lipoxygenase.
Gene Ontology
Molecular Function
GO:0005506 iron ion binding
GO:0016165 linoleate 13S-lipoxygenase activity
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:0102299 linolenate 9R-lipoxygenase activity
Biological Process
GO:0006633 fatty acid biosynthetic process
GO:0019395 fatty acid oxidation
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:5tr0, PDBe:5tr0, PDBj:5tr0
PDBsum5tr0
PubMed30645119
UniProtP08170|LOX1_SOYBN Seed linoleate 13S-lipoxygenase-1 (Gene Name=LOX1.1)

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