Structure of PDB 2ddh Chain A

Receptor sequence
>2ddhA (length=622) Species: 10116 (Rattus norvegicus) [Search protein sequence]
MNPDLRKERASATFNPELITHILDGSPENTRRRREIENLILNDPDFQHED
YNFLTRSQRYEVAVKKSATMVKKMREYGISDPEEIMWFKNSVHRGHPEPL
DLHLGMFLPTLLQATAEQQERFFMPAWNLEITGTYAQTEMGHGTHLRGLE
TTATYDPKTQEFILNSPTVTSIKWWPGGLGKTSNHAIVLAQLITQGECYG
LHAFVVPIREIGTHKPLPGITVGDIGPKFGYEEMDNGYLKMDNYRIPREN
MLMKYAQVKPDGTYVKPLMVFVRSFLVGNAAQSLSKACTIAIRYSAVRRQ
SEIKQSEPEPQILDFQTQQYKLFPLLATAYAFHFVGRYMKETYLRSELPE
LHALTAGLKAFTTWTANAGIEECRMACGGHGYSHSSGIPNIYVTFTPACT
FEGENTVMMLQTARFLMKIYDQVRSGKLVGGMVSYLNDLPSVDINSLEGL
TEAYKLRAARLVEIAAKNLQTHVSHRKSKEVAWNLTSVDLVRASEAHCHY
VVVKVFSDKLPKIQDKAVQAVLRNLCLLYSLYGISQKGGDFLEGSIITGA
QLSQVNARILELLTLIRPNAVALVDAFDFKDMTLGSVLGRYDGNVYENLF
EWAKKSPLNKTEVHESYHKHLK
3D structure
PDB2ddh Three-Dimensional Structure of Rat-Liver Acyl-CoA Oxidase in Complex with a Fatty Acid: Insights into Substrate-Recognition and Reactivity toward Molecular Oxygen.
ChainA
Resolution2.07 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 1.3.3.6: 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 A T139 G144 T145 W176 P177 E423 T138 G143 T144 W175 P176 E404
BS02 HXD A D101 F284 F420 E421 D101 F275 F401 E402
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:2ddh, PDBe:2ddh, PDBj:2ddh
PDBsum2ddh
PubMed16672280
UniProtP07872|ACOX1_RAT Peroxisomal acyl-coenzyme A oxidase 1 (Gene Name=Acox1)

[Back to BioLiP]