Structure of PDB 2ix5 Chain C

Receptor sequence
>2ix5C (length=415) Species: 3702 (Arabidopsis thaliana) [Search protein sequence]
KSSYFDLPPMEMSVAFPQATPASTFPPCTSDYYHFNDLLTPEEQAIRKKV
RECMEKEVAPIMTEYWEKAEFPFHITPKLGAMGVAGGSIKGYGCPGLSIT
ANAIATAEIARVDASCSTFILVHSSLGMLTIALCGSEAQKEKYLPSLAQL
NTVACWALTEPDNGSDASGLGTTATKVEGGWKINGQKRWIGNSTFADLLI
IFARNTTTNQINGFIVKKDAPGLKATKIPNKIGLRMVQNGDILLQNVFVP
DEDRLPGVNSFQDTSKVLAVSRVMVAWQPIGISMGIYDMCHRYLKERKQF
GAPLAAFQLNQQKLVQMLGNVQAMFLMGWRLCKLYETGQMTPGQASLGKA
WISSKARETASLGRELLGGNGILADFLVAKAFCDLEPIYTYEGTYDINTL
VTGREVTGIASFKPA
3D structure
PDB2ix5 Controlling Electron Transfer in Acyl-Coa Oxidases and Dehydrogenases: A Structural View.
ChainC
Resolution2.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) L174 T175 S287 E408 R420
Catalytic site (residue number reindexed from 1) L158 T159 S271 E392 R404
Enzyme Commision number 1.3.3.6: acyl-CoA oxidase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0003995 acyl-CoA dehydrogenase activity
GO:0003997 acyl-CoA oxidase activity
GO:0016491 oxidoreductase activity
GO:0016627 oxidoreductase activity, acting on the CH-CH group of donors
GO:0050660 flavin adenine dinucleotide binding
GO:1901149 salicylic acid binding
Biological Process
GO:0006631 fatty acid metabolic process
GO:0006635 fatty acid beta-oxidation
GO:0009793 embryo development ending in seed dormancy
GO:0046459 short-chain fatty acid metabolic process
Cellular Component
GO:0005777 peroxisome
GO:0005829 cytosol
GO:0009514 glyoxysome

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2ix5, PDBe:2ix5, PDBj:2ix5
PDBsum2ix5
PubMed16887802
UniProtQ96329|ACOX4_ARATH Acyl-coenzyme A oxidase 4, peroxisomal (Gene Name=ACX4)

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