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3HDH

PIG HEART SHORT CHAIN L-3-HYDROXYACYL COA DEHYDROGENASE REVISITED: SEQUENCE ANALYSIS AND CRYSTAL STRUCTURE DETERMINATION

Functional Information from GO Data
ChainGOidnamespacecontents
A0003857molecular_function(3S)-3-hydroxyacyl-CoA dehydrogenase (NAD+) activity
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0006629biological_processlipid metabolic process
A0006631biological_processfatty acid metabolic process
A0006635biological_processfatty acid beta-oxidation
A0007283biological_processspermatogenesis
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0030154biological_processcell differentiation
A0042802molecular_functionidentical protein binding
A0050796biological_processregulation of insulin secretion
A0070403molecular_functionNAD+ binding
A0120162biological_processpositive regulation of cold-induced thermogenesis
B0003857molecular_function(3S)-3-hydroxyacyl-CoA dehydrogenase (NAD+) activity
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005759cellular_componentmitochondrial matrix
B0006629biological_processlipid metabolic process
B0006631biological_processfatty acid metabolic process
B0006635biological_processfatty acid beta-oxidation
B0007283biological_processspermatogenesis
B0016491molecular_functionoxidoreductase activity
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0030154biological_processcell differentiation
B0042802molecular_functionidentical protein binding
B0050796biological_processregulation of insulin secretion
B0070403molecular_functionNAD+ binding
B0120162biological_processpositive regulation of cold-induced thermogenesis
C0003857molecular_function(3S)-3-hydroxyacyl-CoA dehydrogenase (NAD+) activity
C0005654cellular_componentnucleoplasm
C0005737cellular_componentcytoplasm
C0005739cellular_componentmitochondrion
C0005759cellular_componentmitochondrial matrix
C0006629biological_processlipid metabolic process
C0006631biological_processfatty acid metabolic process
C0006635biological_processfatty acid beta-oxidation
C0007283biological_processspermatogenesis
C0016491molecular_functionoxidoreductase activity
C0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
C0030154biological_processcell differentiation
C0042802molecular_functionidentical protein binding
C0050796biological_processregulation of insulin secretion
C0070403molecular_functionNAD+ binding
C0120162biological_processpositive regulation of cold-induced thermogenesis
Functional Information from PDB Data
site_idAC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE NAD A 350
ChainResidue
ALEU25
ALYS115
AASN135
ASER137
AHIS158
APHE159
AMET26
AASP45
AGLN46
AALA107
AILE108
AVAL109
AGLU110
AVAL114

site_idAC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE NAD B 750
ChainResidue
BGLY24
BLEU25
BMET26
BASP45
BGLN46
BALA107
BILE108
BGLU110
BLYS115
BASN135
BSER137
BPHE159

site_idAC3
Number of Residues16
DetailsBINDING SITE FOR RESIDUE NAD C 1150
ChainResidue
CGLY22
CLEU25
CMET26
CASP45
CGLN46
CALA107
CILE108
CGLU110
CLYS115
CLEU118
CASN135
CTHR136
CSER137
CHIS158
CPHE159
CASN161

Functional Information from PROSITE/UniProt
site_idPS00067
Number of Residues25
Details3HCDH 3-hydroxyacyl-CoA dehydrogenase signature. DtpGFIvNRllvPYLieavr.LYerG
ChainResidueDetails
AASP201-GLY225

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues27
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"3479790","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q16836","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsSite: {"description":"Important for catalytic activity","evidences":[{"source":"UniProtKB","id":"Q16836","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues6
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q61425","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues26
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q61425","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues6
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q61425","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues3
DetailsModified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine","evidences":[{"source":"UniProtKB","id":"Q16836","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 2hdh
ChainResidueDetails
AASN208
ASER137
AHIS158

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 2hdh
ChainResidueDetails
BASN208
BSER137
BHIS158

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 2hdh
ChainResidueDetails
CASN208
CSER137
CHIS158

239803

PDB entries from 2025-08-06

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