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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

5ZQZ

Structure of human mitochondrial trifunctional protein, tetramer

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0003857molecular_function(3S)-3-hydroxyacyl-CoA dehydrogenase (NAD+) activity
A0003985molecular_functionacetyl-CoA C-acetyltransferase activity
A0004300molecular_functionenoyl-CoA hydratase activity
A0005515molecular_functionprotein binding
A0005739cellular_componentmitochondrion
A0005743cellular_componentmitochondrial inner membrane
A0006629biological_processlipid metabolic process
A0006631biological_processfatty acid metabolic process
A0006635biological_processfatty acid beta-oxidation
A0016491molecular_functionoxidoreductase activity
A0016507cellular_componentmitochondrial fatty acid beta-oxidation multienzyme complex
A0016509molecular_functionlong-chain (3S)-3-hydroxyacyl-CoA dehydrogenase (NAD+) activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0016740molecular_functiontransferase activity
A0016829molecular_functionlyase activity
A0018812molecular_function3-hydroxyacyl-CoA dehydratase activity
A0035965biological_processcardiolipin acyl-chain remodeling
A0042645cellular_componentmitochondrial nucleoid
A0052816molecular_functionlong-chain fatty acyl-CoA hydrolase activity
A0070403molecular_functionNAD+ binding
B0003723molecular_functionRNA binding
B0003857molecular_function(3S)-3-hydroxyacyl-CoA dehydrogenase (NAD+) activity
B0003985molecular_functionacetyl-CoA C-acetyltransferase activity
B0003988molecular_functionacetyl-CoA C-acyltransferase activity
B0004300molecular_functionenoyl-CoA hydratase activity
B0005515molecular_functionprotein binding
B0005739cellular_componentmitochondrion
B0005740cellular_componentmitochondrial envelope
B0005741cellular_componentmitochondrial outer membrane
B0005743cellular_componentmitochondrial inner membrane
B0005783cellular_componentendoplasmic reticulum
B0006629biological_processlipid metabolic process
B0006631biological_processfatty acid metabolic process
B0006635biological_processfatty acid beta-oxidation
B0010467biological_processgene expression
B0016507cellular_componentmitochondrial fatty acid beta-oxidation multienzyme complex
B0016740molecular_functiontransferase activity
B0016746molecular_functionacyltransferase activity
B0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
B0042645cellular_componentmitochondrial nucleoid
B0044877molecular_functionprotein-containing complex binding
B0050633molecular_functionacetyl-CoA C-myristoyltransferase activity
B0071222biological_processcellular response to lipopolysaccharide
B0106222molecular_functionlncRNA binding
C0003824molecular_functioncatalytic activity
C0003857molecular_function(3S)-3-hydroxyacyl-CoA dehydrogenase (NAD+) activity
C0003985molecular_functionacetyl-CoA C-acetyltransferase activity
C0004300molecular_functionenoyl-CoA hydratase activity
C0005515molecular_functionprotein binding
C0005739cellular_componentmitochondrion
C0005743cellular_componentmitochondrial inner membrane
C0006629biological_processlipid metabolic process
C0006631biological_processfatty acid metabolic process
C0006635biological_processfatty acid beta-oxidation
C0016491molecular_functionoxidoreductase activity
C0016507cellular_componentmitochondrial fatty acid beta-oxidation multienzyme complex
C0016509molecular_functionlong-chain (3S)-3-hydroxyacyl-CoA dehydrogenase (NAD+) activity
C0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
C0016740molecular_functiontransferase activity
C0016829molecular_functionlyase activity
C0018812molecular_function3-hydroxyacyl-CoA dehydratase activity
C0035965biological_processcardiolipin acyl-chain remodeling
C0042645cellular_componentmitochondrial nucleoid
C0052816molecular_functionlong-chain fatty acyl-CoA hydrolase activity
C0070403molecular_functionNAD+ binding
D0003723molecular_functionRNA binding
D0003857molecular_function(3S)-3-hydroxyacyl-CoA dehydrogenase (NAD+) activity
D0003985molecular_functionacetyl-CoA C-acetyltransferase activity
D0003988molecular_functionacetyl-CoA C-acyltransferase activity
D0004300molecular_functionenoyl-CoA hydratase activity
D0005515molecular_functionprotein binding
D0005739cellular_componentmitochondrion
D0005740cellular_componentmitochondrial envelope
D0005741cellular_componentmitochondrial outer membrane
D0005743cellular_componentmitochondrial inner membrane
D0005783cellular_componentendoplasmic reticulum
D0006629biological_processlipid metabolic process
D0006631biological_processfatty acid metabolic process
D0006635biological_processfatty acid beta-oxidation
D0010467biological_processgene expression
D0016507cellular_componentmitochondrial fatty acid beta-oxidation multienzyme complex
D0016740molecular_functiontransferase activity
D0016746molecular_functionacyltransferase activity
D0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
D0042645cellular_componentmitochondrial nucleoid
D0044877molecular_functionprotein-containing complex binding
D0050633molecular_functionacetyl-CoA C-myristoyltransferase activity
D0071222biological_processcellular response to lipopolysaccharide
D0106222molecular_functionlncRNA binding
Functional Information from PROSITE/UniProt
site_idPS00067
Number of Residues25
Details3HCDH 3-hydroxyacyl-CoA dehydrogenase signature. DgpGFYtTRclaPMMsevir.ILqeG
ChainResidueDetails
AASP541-GLY565
site_idPS00098
Number of Residues19
DetailsTHIOLASE_1 Thiolases acyl-enzyme intermediate signature. VTMaCISANqAMttgvglI
ChainResidueDetails
BVAL134-ILE152
site_idPS00099
Number of Residues14
DetailsTHIOLASE_3 Thiolases active site. GLVAACAAgGqGhA
ChainResidueDetails
BGLY453-ALA466
site_idPS00166
Number of Residues21
DetailsENOYL_COA_HYDRATASE Enoyl-CoA hydratase/isomerase signature. VAaINGsclGGGlevaIsCQY
ChainResidueDetails
AVAL138-TYR158
site_idPS00737
Number of Residues17
DetailsTHIOLASE_2 Thiolases signature 2. NnwGGsLSlGHPfGaTG
ChainResidueDetails
BASN418-GLY434
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"For hydroxyacyl-coenzyme A dehydrogenase activity","evidences":[{"source":"PubMed","id":"8770876","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues4
DetailsSite: {"description":"Important for long-chain enoyl-CoA hydratase activity","evidences":[{"source":"PubMed","id":"30850536","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues2
DetailsSite: {"description":"Important for hydroxyacyl-coenzyme A dehydrogenase activity","evidences":[{"source":"PubMed","id":"30850536","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues36
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q8BMS1","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues8
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q8BMS1","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues10
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q8BMS1","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q8BMS1","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues2
DetailsModified residue: {"description":"Omega-N-methylarginine","evidences":[{"source":"UniProtKB","id":"Q8BMS1","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q64428","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues2
DetailsActive site: {"description":"Acyl-thioester intermediate","evidences":[{"source":"PubMed","id":"30850536","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues2
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"30850536","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues2
DetailsSite: {"description":"Increases nucleophilicity of active site Cys","evidences":[{"source":"PubMed","id":"30850536","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues6
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q99JY0","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues4
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q99JY0","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues6
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q99JY0","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

248335

PDB entries from 2026-01-28

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