Structure of PDB 4y9j Chain A

Receptor sequence
>4y9jA (length=592) Species: 6239 (Caenorhabditis elegans) [Search protein sequence]
TITARHTQYSHAKTGGFSQTGPTLHNPYKDDPILDRTLRRLLPESEYMRV
AADLSKFGDRITSEVEHLGRQAELEQPRLEHQDAWGKRVDKLIVCNEWHK
LKQICAEEGVISIGYEDSVDPFVRRIHQVAKLFLFSPSAGLVSCPMAMTD
GAVKTLTSLNLYGKHKLATEAVDRLRSRDPSKAWTSGQWMTEKKGGSDVA
GGCDTYAVQIDKDTYRLHGYKWFSSAVDADVALTLARIVDSDGNALEGSR
GLSLFLLKIRDESGNLNGIQMVRLKNKLGTKQLPTAELLLDGAIAERIGD
QGRGVAGISNMLNITRIHNAVASLGYMRRIISLARDYSTKRVVFGQTQSK
WPLHTTTLAKMEVDTRGSMLLLFEAARLLGLSEAGKSSDVEAMMLRLITP
VLKLYAGKQAVPMVSEGIECFGGQGYMEDTGLPTLLRDAQVTPIWEGTTN
VLSLDVLRVFSGKENILLAFGKRVEQLLGNTKTEDEKLKKSKEAVESALK
QLQKLLVKASDSAIQGETRIDSVARHIAFTIARIYSGALLIDHASDSSVA
NQSDIEVAYRYCCEQPLIDLRWEWFASERVKADREIVFDNFT
3D structure
PDB4y9j Acyl-CoA Dehydrogenase Drives Heat Adaptation by Sequestering Fatty Acids
ChainA
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) M208 T209 T333 E464 R476
Catalytic site (residue number reindexed from 1) M190 T191 T315 E446 R458
Enzyme Commision number 1.3.99.-
Interaction with ligand
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0003995 acyl-CoA dehydrogenase activity
GO:0005504 fatty acid binding
GO:0016491 oxidoreductase activity
GO:0016627 oxidoreductase activity, acting on the CH-CH group of donors
Biological Process
GO:0006631 fatty acid metabolic process
GO:1990845 adaptive thermogenesis

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Molecular Function
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Biological Process
External links
PDB RCSB:4y9j, PDBe:4y9j, PDBj:4y9j
PDBsum4y9j
PubMed25981666
UniProtQ9XWZ2|ACD11_CAEEL Acyl-CoA dehydrogenase family member 11 (Gene Name=acdh-11)

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