Structure of PDB 1rx0 Chain D

Receptor sequence
>1rx0D (length=384) Species: 9606 (Homo sapiens) [Search protein sequence]
TSCIDPSMGLNEEQKEFQKVAFDFAAREMAPNMAEWDQKELFPVDVMRKA
AQLGFGGVYIQTDVGGSGLSRLDTSVIFEALATGCTSTTAYISIHNMCAW
MIDSFGNEEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSAKKQGD
HYILNGSKAFISGAGESDIYVVMCRTGGPGPKGISCIVVEKGTPGLSFGK
KEKKVGWNSQPTRAVIFEDCAVPVANRIGSEGQGFLIAVRGLNGGRINIA
SCSLGAAHASVILTRDHLNVRKQFGEPLASNQYLQFTLADMATRLVAARL
MVRNAAVALQEERKDAVALCSMAKLFATDECFAICNQALQMHGGYGYLKD
YAVQQYVRDSRVHQILEGSNEVMRILISRSLLQE
3D structure
PDB1rx0 Structures of Isobutyryl-CoA Dehydrogenase and Enzyme-Product Complex: COMPARISON WITH ISOVALERYL- AND SHORT-CHAIN ACYL-COA DEHYDROGENASES.
ChainD
Resolution1.77 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) L138 T139 G254 E376 R388
Catalytic site (residue number reindexed from 1) L129 T130 G245 E367 R379
Enzyme Commision number 1.3.8.5: short-chain 2-methylacyl-CoA dehydrogenase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0003995 acyl-CoA dehydrogenase activity
GO:0005515 protein binding
GO:0016491 oxidoreductase activity
GO:0016627 oxidoreductase activity, acting on the CH-CH group of donors
GO:0050660 flavin adenine dinucleotide binding
Biological Process
GO:0006574 valine catabolic process
GO:0006629 lipid metabolic process
GO:0009083 branched-chain amino acid catabolic process
Cellular Component
GO:0005739 mitochondrion
GO:0005759 mitochondrial matrix

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1rx0, PDBe:1rx0, PDBj:1rx0
PDBsum1rx0
PubMed14752098
UniProtQ9UKU7|ACAD8_HUMAN Isobutyryl-CoA dehydrogenase, mitochondrial (Gene Name=ACAD8)

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