Structure of PDB 5t5v Chain A

Receptor sequence
>5t5vA (length=820) Species: 3847 (Glycine max) [Search protein sequence]
HKIKGTVVLMPKNELEVVDNLNAFLGRSVSLQLISATKADAHGKGKVGKD
TFLEGINTSLPTLGAGESAFNIHFEWDGSMGIPGAFYIKNYMQVEFFLKS
LTLEAISNQGTIRFVCNSWVYNTKLYKSVRIFFANHTYVPSETPAPLVEY
REEELKSLRGNGTGERKEYDRIYDYDVYNDLGNPDKSEKLARPVLGGSST
FPYPRRGRTGRGPTVTDPNTEKQGEVFYVPRDENLGHLKSKDALEIGTKS
LSQIVQPAFESAFDLKSTPIEFHSFQDVHDLYEGGIKLPRDVISTIIPLP
VIKELYRTDGQHILKFPQPHVVQVSQSAWMTDEEFAREMIAGVNPCVIRG
LEEFPPKSNLDPAIYGDQSSKITADSLDLDGYTMDEALGSRRLFMLDYHD
IFMPYVRQINQLNSAKTYATRTILFLREDGTLKPVAIELSLPHVSQVVLP
AKEGVESTIWLLAKAYVIVNDSCYHQLMSHWLNTHAAMEPFVIATHRHLS
VLHPIYKLLTPHYRNNMNINALARQSLINANGIIETTFLPSKYSVEMSSA
VYKNWVFTDQALPADLIKRGVAIKDPSTPHGVRLLIEDYPYAADGLEIWA
AIKTWVQEYVPLYYARDDDVKNDSELQHWWKEAVEKGHGDLKDKPWWPKL
QTLEDLVEVCLIIIWIASALHAAVNFGQYPYGGLIMNRPTASRRLLPEKG
TPEYEEMINNHEKAYLRTITSKLPTLISLSVIEILSTHASDEVYLGQRDN
PHWTSDSKALQAFQKFGNKLKEIEEKLVRRNNDPSLQGNRLGPVQLPYTL
LYPSSEEGLTFRGIPNSISI
3D structure
PDB5t5v Hydrogen-Deuterium Exchange of Lipoxygenase Uncovers a Relationship between Distal, Solvent Exposed Protein Motions and the Thermal Activation Barrier for Catalytic Proton-Coupled Electron Tunneling.
ChainA
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
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 H499 H504 H690 N694 I839 H480 H485 H671 N675 I820
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:5t5v, PDBe:5t5v, PDBj:5t5v
PDBsum5t5v
PubMed28691068
UniProtP08170|LOX1_SOYBN Seed linoleate 13S-lipoxygenase-1 (Gene Name=LOX1.1)

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