Structure of PDB 4wha Chain A Binding Site BS01

Receptor Information
>4wha Chain A (length=822) Species: 3847 (Glycine max) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
HKIKGTVVLMPKNELENLNAFLGRSVSLQLISATKADAHGKGKVGKDTFL
EGINTSLPTLGAGESAFNIHFEWDGSMGIPGAFYIKNYMQVEFFLKSLTL
EAISTIRFVCNSWVYNTKLYKSVRIFFANHTYVPSETPAPLVEYREEELK
SLRGNGTGERKEYDRIYDYDVYNDLGNPDKSEKLARPVLGGSSTFPYPRR
GRTGRGPTVTDPNTEKQGEVFYVPRDENLGHLKSKDALEIGTKSLSQIVQ
PAFESAFDLKSTPIEFHSFQDVHDLYEGGIKLPRDVISTIIPLPVIKELY
RTDGQHILKFPQPHVVQVSQSAWMTDEEFAREMIAGVNPCVIRGLEEFPP
KSNLDPAIYGDQSSKITADSLDLDGYTMDEALGSRRLFMLDYHDIFMPYV
RQINQLNSAKTYATRTILFLREDGTLKPVAIELSLPHSAGDLSAAVSQVV
LPAKEGVESTIWLLAKAYVIVNDSCYHQLMSHWLNTHAAMEPFVIATHRH
LSVLHPIYKLLTPHYRNNMNINALARQSAINANGIIETTFLPSKYSVEMS
SAVYKNWVFTDQALPADLIKRGVAIKDPSTPHGVRLLIEDYPYAADGLEI
WAAIKTWVQEYVPLYYARDDDVKNDSELQHWWKEAVEKGHGDLKDKPWWP
KLQTLEDLVEVCLIIIWIASALHAAVNFGQYPYGGLIMNRPTASRRLLPE
KGTPEYEEMINNHEKAYLRTITSKLPTLISLSVIEIASTHASDEVYLGQR
DNPHWTSDSKALQAFQKFGNKLKEIEEKLVRRNNDPSLQGNRLGPVQLPY
TLLYPSSEEGLTFRGIPNSISI
Ligand information
Ligand IDFE
InChIInChI=1S/Fe/q+3
InChIKeyVTLYFUHAOXGGBS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
CACTVS 3.341
OpenEye OEToolkits 1.5.0		[Fe+3]
FormulaFe
NameFE (III) ION
ChEMBL
DrugBankDB13949
ZINC
PDB chain4wha 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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PDB4wha Extremely elevated room-temperature kinetic isotope effects quantify the critical role of barrier width in enzymatic C-H activation.
Resolution1.7 Å
Binding residue
(original residue number in PDB)		H499 H504 H690 N694 I839
Binding residue
(residue number reindexed from 1)		H482 H487 H673 N677 I822
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) H499 H504 H690 N694 I839
Catalytic site (residue number reindexed from 1) H482 H487 H673 N677 I822
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

View graph for
Molecular Function
View graph for
Biological Process
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Cellular Component
External links
PDB RCSB:4wha, PDBe:4wha, PDBj:4wha
PDBsum4wha
PubMed24884374
UniProtP08170|LOX1_SOYBN Seed linoleate 13S-lipoxygenase-1 (Gene Name=LOX1.1)

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