Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4C2J

Crystal structure of human mitochondrial 3-ketoacyl-CoA thiolase in complex with CoA

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003723	molecular_function	RNA binding
A	0003985	molecular_function	acetyl-CoA C-acetyltransferase activity
A	0003986	molecular_function	acetyl-CoA hydrolase activity
A	0003988	molecular_function	acetyl-CoA C-acyltransferase activity
A	0005515	molecular_function	protein binding
A	0005739	cellular_component	mitochondrion
A	0005759	cellular_component	mitochondrial matrix
A	0006629	biological_process	lipid metabolic process
A	0006631	biological_process	fatty acid metabolic process
A	0006635	biological_process	fatty acid beta-oxidation
A	0006695	biological_process	cholesterol biosynthetic process
A	0016740	molecular_function	transferase activity
A	0016746	molecular_function	acyltransferase activity
A	0016747	molecular_function	acyltransferase activity, transferring groups other than amino-acyl groups
A	0016787	molecular_function	hydrolase activity
A	0047617	molecular_function	fatty acyl-CoA hydrolase activity
A	0071456	biological_process	cellular response to hypoxia
A	1901029	biological_process	negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway
A	1902109	biological_process	negative regulation of mitochondrial membrane permeability involved in apoptotic process
B	0003723	molecular_function	RNA binding
B	0003985	molecular_function	acetyl-CoA C-acetyltransferase activity
B	0003986	molecular_function	acetyl-CoA hydrolase activity
B	0003988	molecular_function	acetyl-CoA C-acyltransferase activity
B	0005515	molecular_function	protein binding
B	0005739	cellular_component	mitochondrion
B	0005759	cellular_component	mitochondrial matrix
B	0006629	biological_process	lipid metabolic process
B	0006631	biological_process	fatty acid metabolic process
B	0006635	biological_process	fatty acid beta-oxidation
B	0006695	biological_process	cholesterol biosynthetic process
B	0016740	molecular_function	transferase activity
B	0016746	molecular_function	acyltransferase activity
B	0016747	molecular_function	acyltransferase activity, transferring groups other than amino-acyl groups
B	0016787	molecular_function	hydrolase activity
B	0047617	molecular_function	fatty acyl-CoA hydrolase activity
B	0071456	biological_process	cellular response to hypoxia
B	1901029	biological_process	negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway
B	1902109	biological_process	negative regulation of mitochondrial membrane permeability involved in apoptotic process
C	0003723	molecular_function	RNA binding
C	0003985	molecular_function	acetyl-CoA C-acetyltransferase activity
C	0003986	molecular_function	acetyl-CoA hydrolase activity
C	0003988	molecular_function	acetyl-CoA C-acyltransferase activity
C	0005515	molecular_function	protein binding
C	0005739	cellular_component	mitochondrion
C	0005759	cellular_component	mitochondrial matrix
C	0006629	biological_process	lipid metabolic process
C	0006631	biological_process	fatty acid metabolic process
C	0006635	biological_process	fatty acid beta-oxidation
C	0006695	biological_process	cholesterol biosynthetic process
C	0016740	molecular_function	transferase activity
C	0016746	molecular_function	acyltransferase activity
C	0016747	molecular_function	acyltransferase activity, transferring groups other than amino-acyl groups
C	0016787	molecular_function	hydrolase activity
C	0047617	molecular_function	fatty acyl-CoA hydrolase activity
C	0071456	biological_process	cellular response to hypoxia
C	1901029	biological_process	negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway
C	1902109	biological_process	negative regulation of mitochondrial membrane permeability involved in apoptotic process
D	0003723	molecular_function	RNA binding
D	0003985	molecular_function	acetyl-CoA C-acetyltransferase activity
D	0003986	molecular_function	acetyl-CoA hydrolase activity
D	0003988	molecular_function	acetyl-CoA C-acyltransferase activity
D	0005515	molecular_function	protein binding
D	0005739	cellular_component	mitochondrion
D	0005759	cellular_component	mitochondrial matrix
D	0006629	biological_process	lipid metabolic process
D	0006631	biological_process	fatty acid metabolic process
D	0006635	biological_process	fatty acid beta-oxidation
D	0006695	biological_process	cholesterol biosynthetic process
D	0016740	molecular_function	transferase activity
D	0016746	molecular_function	acyltransferase activity
D	0016747	molecular_function	acyltransferase activity, transferring groups other than amino-acyl groups
D	0016787	molecular_function	hydrolase activity
D	0047617	molecular_function	fatty acyl-CoA hydrolase activity
D	0071456	biological_process	cellular response to hypoxia
D	1901029	biological_process	negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway
D	1902109	biological_process	negative regulation of mitochondrial membrane permeability involved in apoptotic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO A 1397

Chain	Residue
A	ASN131
A	PHE134
A	HOH2120
A	HOH2121
B	LYS25
B	ASP26

site_id	AC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE EDO D 1397

Chain	Residue
D	LEU3
D	GLY281
D	TYR282
D	LYS306
D	HOH2001
D	HOH2117
C	GLU110
C	HOH2092
D	MET1

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO C 1397

Chain	Residue
C	MET1
C	LEU3
C	GLY281
C	TYR282
C	LYS306
C	HOH2001
D	GLU110

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO A 1398

Chain	Residue
A	LEU3
A	GLY281
A	TYR282
A	LYS306
B	GLU110

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO C 1398

Chain	Residue
C	ARG76
C	GLY78
C	VAL170
C	LYS240

site_id	AC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE EDO D 1398

Chain	Residue
C	LYS25
C	ASP26
C	GLN124
C	HOH2099
D	ASN131
D	PHE134
D	HOH2066
D	HOH2069

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO B 1398

Chain	Residue
A	LYS25
A	ASP26
A	HOH2113
B	ASN131
B	PHE134
B	HOH2068

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO A 1399

Chain	Residue
A	ARG76
A	VAL170
A	LYS240

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO D 1399

Chain	Residue
D	TRP149
D	LEU152
D	THR153
D	PRO160
D	HOH2079

site_id	BC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE EDO C 1399

Chain	Residue
C	ASN131
C	PHE134
C	HOH2104
C	HOH2105
C	HOH2107
D	LYS25
D	SER123
D	GLN124

site_id	BC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO C 1400

Chain	Residue
C	LEU311
C	MET314
C	VAL317
C	LEU336
C	ASP337
C	LYS340
C	THR341

site_id	BC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO A 1400

Chain	Residue
A	TRP149
A	LEU152
A	THR153
A	PRO160
A	HOH2143

site_id	BC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO B 1399

Chain	Residue
B	TRP149
B	LEU152
B	THR153
B	PRO160
B	HOH2081

site_id	BC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO C 1401

Chain	Residue
C	TRP149
C	LEU152
C	THR153
C	PRO160
C	HOH2118

site_id	BC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO A 1401

Chain	Residue
A	PHE27
A	PHE35
A	ILE206
A	GLU207

site_id	BC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO B 1400

Chain	Residue
A	GLU110
B	MET1
B	LEU3
B	GLY281
B	TYR282
B	LYS306
B	HOH2002

site_id	BC8
Number of Residues	15
Details	BINDING SITE FOR RESIDUE COA A 1402

Chain	Residue
A	MET292
A	PHE323
A	HOH2170
A	HOH2207
A	HOH2217
A	HOH2218
A	HOH2219
A	HOH2261
A	HOH2262
A	HOH2264
A	ARG224
A	THR227
A	LEU235
A	ALA247
A	SER251

site_id	BC9
Number of Residues	16
Details	BINDING SITE FOR RESIDUE COA B 1401

Chain	Residue
B	LEU152
B	ARG224
B	THR227
B	LEU235
B	ALA247
B	GLY248
B	SER251
B	PHE323
B	HIS352
B	HOH2096
B	HOH2125
B	HOH2134
B	HOH2135
B	HOH2136
B	HOH2179
B	HOH2181

site_id	CC1
Number of Residues	12
Details	BINDING SITE FOR RESIDUE COA C 1402

Chain	Residue
C	ARG224
C	THR227
C	ALA247
C	SER251
C	PHE323
C	HOH2140
C	HOH2166
C	HOH2171
C	HOH2172
C	HOH2173
C	HOH2210
C	HOH2211

site_id	CC2
Number of Residues	12
Details	BINDING SITE FOR RESIDUE COA D 1400

Chain	Residue
D	ARG224
D	THR227
D	ALA247
D	GLY248
D	SER251
D	PHE323
D	HIS352
D	HOH2091
D	HOH2111
D	HOH2112
D	HOH2150
D	HOH2151

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ILE88-ILE106

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

Chain	Residue	Details
A	ALA377-ALA390

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

Chain	Residue	Details
A	ASN342-GLY358

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	60
Details	Transit peptide: {"description":"Mitochondrion; not cleaved"}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"description":"Acyl-thioester intermediate","evidences":[{"source":"PubMed","id":"25478839","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	4
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"25478839","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PubMed","id":"25478839","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4C2J","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	4
Details	Site: {"description":"Increases nucleophilicity of active site Cys","evidences":[{"source":"PubMed","id":"25478839","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	32
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q8BWT1","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	20
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q8BWT1","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	4
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	4
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	4
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q8BWT1","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	8
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	20
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q8BWT1","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q8BWT1","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)