Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5ZQZ

Structure of human mitochondrial trifunctional protein, tetramer

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0003857	molecular_function	(3S)-3-hydroxyacyl-CoA dehydrogenase (NAD+) activity
A	0003985	molecular_function	acetyl-CoA C-acetyltransferase activity
A	0004300	molecular_function	enoyl-CoA hydratase activity
A	0005515	molecular_function	protein binding
A	0005739	cellular_component	mitochondrion
A	0005743	cellular_component	mitochondrial inner membrane
A	0006631	biological_process	fatty acid metabolic process
A	0006635	biological_process	fatty acid beta-oxidation
A	0016491	molecular_function	oxidoreductase activity
A	0016507	cellular_component	mitochondrial fatty acid beta-oxidation multienzyme complex
A	0016509	molecular_function	long-chain (3S)-3-hydroxyacyl-CoA dehydrogenase (NAD+) activity
A	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A	0018812	molecular_function	3-hydroxyacyl-CoA dehydratase activity
A	0035965	biological_process	cardiolipin acyl-chain remodeling
A	0042645	cellular_component	mitochondrial nucleoid
A	0052816	molecular_function	long-chain fatty acyl-CoA hydrolase activity
A	0070403	molecular_function	NAD+ binding
B	0003723	molecular_function	RNA binding
B	0003857	molecular_function	(3S)-3-hydroxyacyl-CoA dehydrogenase (NAD+) activity
B	0003985	molecular_function	acetyl-CoA C-acetyltransferase activity
B	0003988	molecular_function	acetyl-CoA C-acyltransferase activity
B	0004300	molecular_function	enoyl-CoA hydratase activity
B	0005515	molecular_function	protein binding
B	0005739	cellular_component	mitochondrion
B	0005740	cellular_component	mitochondrial envelope
B	0005741	cellular_component	mitochondrial outer membrane
B	0005743	cellular_component	mitochondrial inner membrane
B	0005783	cellular_component	endoplasmic reticulum
B	0006635	biological_process	fatty acid beta-oxidation
B	0010467	biological_process	gene expression
B	0016507	cellular_component	mitochondrial fatty acid beta-oxidation multienzyme complex
B	0016746	molecular_function	acyltransferase activity
B	0016747	molecular_function	acyltransferase activity, transferring groups other than amino-acyl groups
B	0042645	cellular_component	mitochondrial nucleoid
B	0044877	molecular_function	protein-containing complex binding
B	0050633	molecular_function	acetyl-CoA C-myristoyltransferase activity
B	0071222	biological_process	cellular response to lipopolysaccharide
B	0106222	molecular_function	lncRNA binding
C	0003824	molecular_function	catalytic activity
C	0003857	molecular_function	(3S)-3-hydroxyacyl-CoA dehydrogenase (NAD+) activity
C	0003985	molecular_function	acetyl-CoA C-acetyltransferase activity
C	0004300	molecular_function	enoyl-CoA hydratase activity
C	0005515	molecular_function	protein binding
C	0005739	cellular_component	mitochondrion
C	0005743	cellular_component	mitochondrial inner membrane
C	0006631	biological_process	fatty acid metabolic process
C	0006635	biological_process	fatty acid beta-oxidation
C	0016491	molecular_function	oxidoreductase activity
C	0016507	cellular_component	mitochondrial fatty acid beta-oxidation multienzyme complex
C	0016509	molecular_function	long-chain (3S)-3-hydroxyacyl-CoA dehydrogenase (NAD+) activity
C	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
C	0018812	molecular_function	3-hydroxyacyl-CoA dehydratase activity
C	0035965	biological_process	cardiolipin acyl-chain remodeling
C	0042645	cellular_component	mitochondrial nucleoid
C	0052816	molecular_function	long-chain fatty acyl-CoA hydrolase activity
C	0070403	molecular_function	NAD+ binding
D	0003723	molecular_function	RNA binding
D	0003857	molecular_function	(3S)-3-hydroxyacyl-CoA dehydrogenase (NAD+) activity
D	0003985	molecular_function	acetyl-CoA C-acetyltransferase activity
D	0003988	molecular_function	acetyl-CoA C-acyltransferase activity
D	0004300	molecular_function	enoyl-CoA hydratase activity
D	0005515	molecular_function	protein binding
D	0005739	cellular_component	mitochondrion
D	0005740	cellular_component	mitochondrial envelope
D	0005741	cellular_component	mitochondrial outer membrane
D	0005743	cellular_component	mitochondrial inner membrane
D	0005783	cellular_component	endoplasmic reticulum
D	0006635	biological_process	fatty acid beta-oxidation
D	0010467	biological_process	gene expression
D	0016507	cellular_component	mitochondrial fatty acid beta-oxidation multienzyme complex
D	0016746	molecular_function	acyltransferase activity
D	0016747	molecular_function	acyltransferase activity, transferring groups other than amino-acyl groups
D	0042645	cellular_component	mitochondrial nucleoid
D	0044877	molecular_function	protein-containing complex binding
D	0050633	molecular_function	acetyl-CoA C-myristoyltransferase activity
D	0071222	biological_process	cellular response to lipopolysaccharide
D	0106222	molecular_function	lncRNA binding

Functional Information from PROSITE/UniProt

site_id	PS00067
Number of Residues	25
Details	3HCDH 3-hydroxyacyl-CoA dehydrogenase signature. DgpGFYtTRclaPMMsevir.ILqeG

Chain	Residue	Details
A	ASP541-GLY565

site_id	PS00098
Number of Residues	19
Details	THIOLASE_1 Thiolases acyl-enzyme intermediate signature. VTMaCISANqAMttgvglI

Chain	Residue	Details
B	VAL134-ILE152

site_id	PS00099
Number of Residues	14
Details	THIOLASE_3 Thiolases active site. GLVAACAAgGqGhA

Chain	Residue	Details
B	GLY453-ALA466

site_id	PS00166
Number of Residues	21
Details	ENOYL_COA_HYDRATASE Enoyl-CoA hydratase/isomerase signature. VAaINGsclGGGlevaIsCQY

Chain	Residue	Details
A	VAL138-TYR158

site_id	PS00737
Number of Residues	17
Details	THIOLASE_2 Thiolases signature 2. NnwGGsLSlGHPfGaTG

Chain	Residue	Details
B	ASN418-GLY434

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"description":"For hydroxyacyl-coenzyme A dehydrogenase activity","evidences":[{"source":"PubMed","id":"8770876","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
Details	Site: {"description":"Important for long-chain enoyl-CoA hydratase activity","evidences":[{"source":"PubMed","id":"30850536","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	2
Details	Site: {"description":"Important for hydroxyacyl-coenzyme A dehydrogenase activity","evidences":[{"source":"PubMed","id":"30850536","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	36
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q8BMS1","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	8
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q8BMS1","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	10
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q8BMS1","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	4
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q8BMS1","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	2
Details	Modified residue: {"description":"Omega-N-methylarginine","evidences":[{"source":"UniProtKB","id":"Q8BMS1","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q64428","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	2
Details	Active site: {"description":"Acyl-thioester intermediate","evidences":[{"source":"PubMed","id":"30850536","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	2
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"30850536","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	2
Details	Site: {"description":"Increases nucleophilicity of active site Cys","evidences":[{"source":"PubMed","id":"30850536","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	6
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q99JY0","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI17
Number of Residues	4
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q99JY0","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI18
Number of Residues	6
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q99JY0","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)