Structure of PDB 8ghd Chain D
Receptor sequence
>8ghdD (length=662) Species:
9606
(Homo sapiens) [
Search protein sequence
]
GRYRIRVATGAWLFSGSYNRVQLWLVGTRGEAELELQLRPARGEEEEFDH
DVAEDLGLLQFVRLRKHHWLVDDAWFCDRITVQGPGACAEVAFPCYRWVQ
GEDILSLPEGTARLPGDNALDMFQKHREKELKDRQQIYCWATWKEGLPLT
IAADRKDDLPPNMRFHEEKRLDFEWTLKAGALEMALKRVYTLLSSWNCLE
DFDQIFWGQKSALAEKVRQCWQDDELFSYQFLNGANPMLLRRSTSLPSRL
VLPSGMEELQAQLEKELQNGSLFEADFILLDGIPANVIRGEKQYLAAPLV
MLKMEPNGKLQPMVIQIQPPSPSSPTPTLFLPSDPPLAWLLAKSWVRNSD
FQLHEIQYHLLNTHLVAEVIAVATMRCLPGLHPIFKFLIPHIRYTMEINT
RARTQLISDGGIFDKAVSTGGGGHVQLLRRAAAQLTYCSLCPPDDLADRG
LLGLPGALYAHDALRLWEIIARYVEGIVHLFYQRDDIVKGDPELQAWCRE
ITEVGLCQAQDRGFPVSFQSQSQLCHFLTMCVFTCTAQHAAINQGQLDWY
AWVPNAPCTMRMPPPTTKEDVTMATVMGSLPDVRQACLQMAISWHLSRRQ
PDMVPLGHHKEKYFSGPKPKAVLNQFRTDLEKLEKEITARNEQLDWPYEY
LKPSCIENSVTI
3D structure
PDB
8ghd
Cryo-EM structures of human arachidonate 12S-lipoxygenase bound to endogenous and exogenous inhibitors.
Chain
D
Resolution
2.2 Å
3D
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
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
FE2
D
H360 H365 H540 N544 I663
H359 H364 H539 N543 I662
BS02
ZR5
D
L178 G181 A182 R189 I413 K416 R585 L589 A592 I593 H596
L177 G180 A181 R188 I412 K415 R584 L588 A591 I592 H595
BS03
ACD
D
F174 F352 E356 H360 L361 H365 I399 R402 A403 L407 F414 I593 S594 L597
F173 F351 E355 H359 L360 H364 I398 R401 A402 L406 F413 I592 S593 L596
Gene Ontology
Molecular Function
GO:0004052
arachidonate 12(S)-lipoxygenase activity
GO:0005506
iron ion binding
GO:0005515
protein 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:0016787
hydrolase activity
GO:0046872
metal ion binding
GO:0047977
hepoxilin-epoxide hydrolase activity
GO:0050473
arachidonate 15-lipoxygenase activity
GO:0051213
dioxygenase activity
Biological Process
GO:0001676
long-chain fatty acid metabolic process
GO:0006629
lipid metabolic process
GO:0006631
fatty acid metabolic process
GO:0006690
icosanoid metabolic process
GO:0010656
negative regulation of muscle cell apoptotic process
GO:0019369
arachidonate metabolic process
GO:0019372
lipoxygenase pathway
GO:0019395
fatty acid oxidation
GO:0033559
unsaturated fatty acid metabolic process
GO:0034440
lipid oxidation
GO:0042554
superoxide anion generation
GO:0043651
linoleic acid metabolic process
GO:0051122
hepoxilin biosynthetic process
GO:0061436
establishment of skin barrier
GO:0090331
negative regulation of platelet aggregation
GO:1901751
leukotriene A4 metabolic process
GO:2001303
lipoxin A4 biosynthetic process
GO:2001306
lipoxin B4 biosynthetic process
Cellular Component
GO:0005737
cytoplasm
GO:0005829
cytosol
GO:0016020
membrane
GO:0042383
sarcolemma
GO:0070062
extracellular exosome
View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB
RCSB:8ghd
,
PDBe:8ghd
,
PDBj:8ghd
PDBsum
8ghd
PubMed
37506345
UniProt
P18054
|LOX12_HUMAN Polyunsaturated fatty acid lipoxygenase ALOX12 (Gene Name=ALOX12)
[
Back to BioLiP
]