Structure of PDB 1lox Chain A

Receptor sequence
>1loxA (length=647) Species: 9986 (Oryctolagus cuniculus) [Search protein sequence]
GVYRVCVSTGASIYAGSKNKVELWLVGQHGEVELGSCLRPTRNKEEEFKV
NVSKYLGSLLFVRLRKKHFLKEDAWFCNWISVQALGAAEDKYWFPCYRWV
VGDGVQSLPVGTGCTTVGDPQGLFQKHREQELEERRKLYQWGSWKEGLIL
NVAGSKLTDLPVDERFLEDKKIDFELKNSLNILAPWKTLDDFNRIFWRSK
LARRVRDSWQEDSLFGYQFLNGANPMLLRRSVQLPARLVFPPGMEELQAQ
LEKELKAGTLFEADFALLDNIKANVILYCQQYLAAPLVMLKLQPDGKLMP
MVIQLHLPKIGSSPPPLFLPTDPPMVWLLAKCWVRSSDFQVHELNSHLLR
GHLMAEVFTVATMRCLPSIHPVFKLIVPHLRYTLEINVRARNGLVSDFGI
FDQIMSTGGGGHVQLLQQAGAFLTYRSFCPPDDLADRGLLGVESSFYAQD
ALRLWEIISRYVQGIMGLYYKTDEAVRDDLELQSWCREITEIGLQGAQKQ
GFPTSLQSVAQACHFVTMCIFTCTGQHSSIHLGQLDWFTWVPNAPCTMRL
PPPTTKDATLETVMATLPNLKQSSLQMSIVWQLGRDIMVPLGQHQEEYFS
GPEPRAVLEKFREELAIMDKEIEVRNEKLDIPYEYLRPSIVENSVAI
3D structure
PDB1lox The structure of mammalian 15-lipoxygenase reveals similarity to the lipases and the determinants of substrate specificity.
ChainA
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) H361 H366 H541 H545 I663
Catalytic site (residue number reindexed from 1) H347 H352 H527 H531 I647
Enzyme Commision number 1.13.11.-
1.13.11.12: linoleate 13S-lipoxygenase.
1.13.11.31: arachidonate 12-lipoxygenase.
1.13.11.33: arachidonate 15-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 FE2 A H361 H366 H541 H545 I663 H347 H352 H527 H531 I647
BS02 RS7 A E357 H361 L362 H366 L408 F415 H545 Q548 I593 L597 E343 H347 L348 H352 L394 F401 H531 Q534 I579 L583 MOAD: Ki=3uM
PDBbind-CN: -logKd/Ki=5.52,Ki=3uM
Gene Ontology
Molecular Function
GO:0004052 arachidonate 12(S)-lipoxygenase activity
GO:0005506 iron ion binding
GO:0005546 phosphatidylinositol-4,5-bisphosphate binding
GO:0008289 lipid binding
GO:0016165 linoleate 13S-lipoxygenase 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:0050473 arachidonate 15-lipoxygenase activity
GO:0051213 dioxygenase activity
Biological Process
GO:0001503 ossification
GO:0002820 negative regulation of adaptive immune response
GO:0006629 lipid metabolic process
GO:0006631 fatty acid metabolic process
GO:0006646 phosphatidylethanolamine biosynthetic process
GO:0010811 positive regulation of cell-substrate adhesion
GO:0019369 arachidonate metabolic process
GO:0019372 lipoxygenase pathway
GO:0019395 fatty acid oxidation
GO:0030282 bone mineralization
GO:0030838 positive regulation of actin filament polymerization
GO:0034440 lipid oxidation
GO:0034976 response to endoplasmic reticulum stress
GO:0035358 regulation of peroxisome proliferator activated receptor signaling pathway
GO:0035963 cellular response to interleukin-13
GO:0042060 wound healing
GO:0043277 apoptotic cell clearance
GO:0043651 linoleic acid metabolic process
GO:0050727 regulation of inflammatory response
GO:0051122 hepoxilin biosynthetic process
GO:0070374 positive regulation of ERK1 and ERK2 cascade
GO:0071277 cellular response to calcium ion
GO:1901074 regulation of engulfment of apoptotic cell
GO:2001303 lipoxin A4 biosynthetic process
Cellular Component
GO:0005737 cytoplasm
GO:0005811 lipid droplet
GO:0005829 cytosol
GO:0005886 plasma membrane
GO:0009898 cytoplasmic side of plasma membrane
GO:0016020 membrane

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1lox, PDBe:1lox, PDBj:1lox
PDBsum1lox
PubMed9406550
UniProtP12530|LOX15_RABIT Polyunsaturated fatty acid lipoxygenase ALOX15 (Gene Name=ALOX15)

[Back to BioLiP]