Structure of PDB 1il0 Chain A

Receptor sequence
>1il0A (length=291) Species: 9606 (Homo sapiens) [Search protein sequence]
KIIVKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEES
LRKVAKKKFAENPKAGDEFVEKTLSTIATSTDAASVVHSTDLVVEAIVEN
LKVKNELFKRLDKFAAEHTIFASNTSSLQITSIANATTRQDRFAGLHFFN
PVPVMKLVQVIKTPMTSQKTFESLVDFSKALGKHPVSCKDTPGFIVNRLL
VPYLMEAIRLYERGDASKEDIDTAMKLGAGYPMGPFELLDYVGLDTTKFI
VDGWHEMDAENPLHQPSPSLNKLVAENKFGKKTGEGFYKYK
3D structure
PDB1il0 Glutamate 170 of human l-3-hydroxyacyl-CoA dehydrogenase is required for proper orientation of the catalytic histidine and structural integrity of the enzyme.
ChainA
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S137 H158 Q170 N208
Catalytic site (residue number reindexed from 1) S126 H147 Q159 N197
Enzyme Commision number 1.1.1.35: 3-hydroxyacyl-CoA dehydrogenase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0003857 3-hydroxyacyl-CoA dehydrogenase activity
GO:0016491 oxidoreductase activity
GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
GO:0016740 transferase activity
GO:0042802 identical protein binding
GO:0070403 NAD+ binding
Biological Process
GO:0006631 fatty acid metabolic process
GO:0006635 fatty acid beta-oxidation
GO:0007283 spermatogenesis
GO:0009410 response to xenobiotic stimulus
GO:0009725 response to hormone
GO:0014823 response to activity
GO:0030154 cell differentiation
GO:0032868 response to insulin
GO:0046676 negative regulation of insulin secretion
GO:0050796 regulation of insulin secretion
GO:0120162 positive regulation of cold-induced thermogenesis
Cellular Component
GO:0005654 nucleoplasm
GO:0005737 cytoplasm
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:1il0, PDBe:1il0, PDBj:1il0
PDBsum1il0
PubMed11451959
UniProtQ16836|HCDH_HUMAN Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial (Gene Name=HADH)

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