Structure of PDB 4nre Chain A

Receptor sequence
>4nreA (length=675) Species: 9606 (Homo sapiens) [Search protein sequence]
AEFRVRVSTGEAFGAGTWDKVSVSIVGTRGESPPLPLDNLGKEFTAGAEE
DFQVTLPEDVGRVLLLRVHKAPPVLPLLGPLAPDAWFCRWFQLTPPRGGH
LLFPCYQWLEGAGTLVLQEGTAKVSWADHHPVLQQQRQEELQARQEMYQW
KAYNPGWPHCLDEKTVEDLELNIKYSTAKNANFYLQAGSAFAEMKIKGLL
DRKGLWRSLNEMKRIFNFRRTPAAEHAFEHWQEDAFFASQFLNGLNPVLI
RRCHYLPKNFPVTDAMVASVLGPGTSLQAELEKGSLFLVDHGILSGIQTN
VINGKPQFSAAPMTLLYQSPGCGPLLPLAIQLSQTPGPNSPIFLPTDDKW
DWLLAKTWVRNAEFSFHEALTHLLHSHLLPEVFTLATLRQLPHCHPLFKL
LIPHTRYTLHINTLARELLIVPGQVVDRSTGIGIEGFSELIQRNMKQLNY
SLLCLPEDIRTRGVEDIPGYYYRDDGMQIWGAVERFVSEIIGIYYPSDES
VQDDRELQAWVREIFSKGFLNQESSGIPSSLETREALVQYVTMVIFTCSA
KHAAVSAGQFDSCAWMPNLPPSMQLPPPTSKGLATCEGFIATLPPVNATC
DVILALWLLSKEPGDQRPLGTYPDEHFTEEAPRRSIATFQSRLAQISRGI
QERNQGLVLPYTYLDPPLIENSVSI
3D structure
PDB4nre The structure of human 15-lipoxygenase-2 with a substrate mimic.
ChainA
Resolution2.63 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) H373 H378 H553 S557 I676
Catalytic site (residue number reindexed from 1) H372 H377 H552 S556 I675
Enzyme Commision number 1.13.11.-
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 H373 H378 H553 I676 H372 H377 H552 I675
BS02 C8E A E369 H373 H378 I412 A416 L420 A606 L607 L610 E368 H372 H377 I411 A415 L419 A605 L606 L609
BS03 C8E A S190 E194 S189 E193
BS04 CA A G15 G17 D85 A86 G14 G16 D84 A85
BS05 CA A D39 N40 G42 E44 D38 N39 G41 E43
Gene Ontology
Molecular Function
GO:0005506 iron ion binding
GO:0005509 calcium ion binding
GO:0005515 protein 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:0036403 arachidonate 8(S)-lipoxygenase activity
GO:0046872 metal ion binding
GO:0050473 arachidonate 15-lipoxygenase activity
GO:0051213 dioxygenase activity
GO:1990136 linoleate 9S-lipoxygenase activity
Biological Process
GO:0001676 long-chain fatty acid metabolic process
GO:0006629 lipid metabolic process
GO:0006644 phospholipid metabolic process
GO:0006690 icosanoid metabolic process
GO:0006915 apoptotic process
GO:0008285 negative regulation of cell population proliferation
GO:0010744 positive regulation of macrophage derived foam cell differentiation
GO:0019369 arachidonate metabolic process
GO:0019372 lipoxygenase pathway
GO:0030336 negative regulation of cell migration
GO:0030850 prostate gland development
GO:0030856 regulation of epithelial cell differentiation
GO:0032722 positive regulation of chemokine production
GO:0034440 lipid oxidation
GO:0035360 positive regulation of peroxisome proliferator activated receptor signaling pathway
GO:0043651 linoleic acid metabolic process
GO:0045618 positive regulation of keratinocyte differentiation
GO:0045786 negative regulation of cell cycle
GO:0045926 negative regulation of growth
GO:0051122 hepoxilin biosynthetic process
GO:0071926 endocannabinoid signaling pathway
GO:1901696 cannabinoid biosynthetic process
GO:2001303 lipoxin A4 biosynthetic process
Cellular Component
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0005856 cytoskeleton
GO:0005886 plasma membrane
GO:0005912 adherens junction
GO:0005925 focal adhesion
GO:0016020 membrane
GO:0070062 extracellular exosome
GO:0070161 anchoring junction

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:4nre, PDBe:4nre, PDBj:4nre
PDBsum4nre
PubMed24497644
UniProtO15296|LX15B_HUMAN Polyunsaturated fatty acid lipoxygenase ALOX15B (Gene Name=ALOX15B)

[Back to BioLiP]