Structure of PDB 3d3l Chain B

Receptor sequence
>3d3lB (length=447) Species: 9606 (Homo sapiens) [Search protein sequence]
WTLKAGALEMALKRVYTLLSSWNCLEDFDQIFWGQKSALAEKVRQCWQDD
ELFSYQFLNGANPMLLRRSTSLPSRLVLPSGMEELRAQLEKELQNGSLFE
ADFILLDGIPAQYLAAPLVMLKMEPNGKLQPMVIQIQPPNPSSPTPTLFL
PSDPPLAWLLAKSWVRNSDFQLHEIQYHLLNTHLVAEVIAVATMRCLPGL
HPIFKFLIPHIGGHVQLLRRAAAQLTYCSLCPPDDLADRGLLGLPGALYA
HDALRLWEIIARYVEGIVHLFYQRDDIVKGDPELQAWCREITEVGLCQAQ
DRGFPVSFQSQSQLCHFLTMCVFTCTAQHAAINQGQLDWYAWVPNAPCTM
RMPPPTTKEDVTMATVMGSLPDVRQACLQMAISWHLSRMVPLGHHKEKYF
SGPKPKAVLNQFRTDLEKLEKEITARNEQLDWPYEYLKPSCIENSVT
3D structure
PDB3d3l Crystal structure of the lipoxygenase domain of human Arachidonate 12-lipoxygenase, 12S-type.
ChainB
Resolution2.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H360 H365 H540 N544
Catalytic site (residue number reindexed from 1) H178 H183 H329 N333
Enzyme Commision number 1.13.11.-
1.13.11.31: arachidonate 12-lipoxygenase.
1.13.11.33: arachidonate 15-lipoxygenase.
3.3.2.-
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 B H360 H365 H540 N544 H178 H183 H329 N333
Gene Ontology
Molecular Function
GO:0005506 iron ion binding
GO:0016702 oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
GO:0046872 metal ion binding
Biological Process
GO:0034440 lipid oxidation

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Molecular Function
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Biological Process
External links
PDB RCSB:3d3l, PDBe:3d3l, PDBj:3d3l
PDBsum3d3l
PubMed
UniProtP18054|LOX12_HUMAN Polyunsaturated fatty acid lipoxygenase ALOX12 (Gene Name=ALOX12)

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