Structure of PDB 1is2 Chain B

Receptor sequence
>1is2B (length=629) Species: 10116 (Rattus norvegicus) [Search protein sequence]
MNPDLRKERASATFNPELITHILDGSPENTRRRREIENLILNDPDFQHED
YNFLTRSQRYEVAVKKSATMVKKMREYGISDPEEIMWFKNSVHRGHPEPL
DLHLGMFLPTLLHQATAEQQERFFMPAWNLEITGTYAQTEMGHGTHLRGL
ETTATYDPKTQEFILNSPTVTSIKWWPGGLGKTSNHAIVLAQLITQGECY
GLHAFVVPIREIGTHKPLPGITVGDIGPKFGYEEMDNGYLKMDNYRIPRE
NMLMKYAQVKPDGTYVKMVFVRSFLVGNAAQSLSKACTIAIRYSAVRRQS
EIKQSEPEPQILDFQTQQYKLFPLLATAYAFHFVGRYMKETYLRINESIG
QGDLSELPELHALTAGLKAFTTWTANAGIEECRMACGGHGYSHSSGIPNI
YVTFTPACTFEGENTVMMLQTARFLMKIYDQVRSGKLVGGMVSYLNDLVD
INSLEGLTEAYKLRAARLVEIAAKNLQTHVSHRKSKEVAWNLTSVDLVRA
SEAHCHYVVVKVFSDKLPKIQDKAVQAVLRNLCLLYSLYGISQKGGDFLE
GSIITGAQLSQVNARILELLTLIRPNAVALVDAFDFKDMTLGSVLGRYDG
NVYENLFEWAKKSPLNKTEVHESYHKHLK
3D structure
PDB1is2 Three-dimensional structure of the flavoenzyme acyl-CoA oxidase-II from rat liver, the peroxisomal counterpart of mitochondrial acyl-CoA dehydrogenase.
ChainB
Resolution2.2 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.3.3.6: acyl-CoA oxidase.
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 FAD B R307 Q309 S310 F324 Q327 A395 G397 G398 Y401 R297 Q299 S300 F314 Q317 A385 G387 G388 Y391
BS02 FAD B T139 G144 T145 W176 F420 E423 T139 G144 T145 W176 F410 E413
Gene Ontology
Molecular Function
GO:0003997 acyl-CoA oxidase activity
GO:0005504 fatty acid binding
GO:0016401 palmitoyl-CoA oxidase activity
GO:0016491 oxidoreductase activity
GO:0016627 oxidoreductase activity, acting on the CH-CH group of donors
GO:0030165 PDZ domain binding
GO:0042803 protein homodimerization activity
GO:0050660 flavin adenine dinucleotide binding
GO:0071949 FAD binding
Biological Process
GO:0000038 very long-chain fatty acid metabolic process
GO:0006091 generation of precursor metabolites and energy
GO:0006629 lipid metabolic process
GO:0006631 fatty acid metabolic process
GO:0006635 fatty acid beta-oxidation
GO:0006693 prostaglandin metabolic process
GO:0007283 spermatogenesis
GO:0009062 fatty acid catabolic process
GO:0019395 fatty acid oxidation
GO:0033540 fatty acid beta-oxidation using acyl-CoA oxidase
GO:0050665 hydrogen peroxide biosynthetic process
GO:0055088 lipid homeostasis
GO:0140493 very long-chain fatty acid beta-oxidation
Cellular Component
GO:0005737 cytoplasm
GO:0005777 peroxisome
GO:0005778 peroxisomal membrane
GO:0005782 peroxisomal matrix

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1is2, PDBe:1is2, PDBj:1is2
PDBsum1is2
PubMed11872165
UniProtP07872|ACOX1_RAT Peroxisomal acyl-coenzyme A oxidase 1 (Gene Name=Acox1)

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