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4J0F

Crystal structure of 3-hydroxyacyl-CoA dehydrogenase from Caenorhadbitis elegans in P212121 space group

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0003857molecular_function3-hydroxyacyl-CoA dehydrogenase (NAD+) activity
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0006629biological_processlipid metabolic process
A0006631biological_processfatty acid metabolic process
A0006635biological_processfatty acid beta-oxidation
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0032787biological_processmonocarboxylic acid metabolic process
A0070403molecular_functionNAD+ binding
B0003824molecular_functioncatalytic activity
B0003857molecular_function3-hydroxyacyl-CoA dehydrogenase (NAD+) activity
B0005739cellular_componentmitochondrion
B0005759cellular_componentmitochondrial matrix
B0006629biological_processlipid metabolic process
B0006631biological_processfatty acid metabolic process
B0006635biological_processfatty acid beta-oxidation
B0016491molecular_functionoxidoreductase activity
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0032787biological_processmonocarboxylic acid metabolic process
B0070403molecular_functionNAD+ binding
Functional Information from PROSITE/UniProt
site_idPS00067
Number of Residues25
Details3HCDH 3-hydroxyacyl-CoA dehydrogenase signature. DspGFIvNRlliPYFfeaar.MYerG
ChainResidueDetails
AASP196-GLY220

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsSITE: Important for catalytic activity => ECO:0000250
ChainResidueDetails
AHIS153
BHIS153

237735

PDB entries from 2025-06-18

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