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	0006631	biological_process	fatty acid metabolic process
A	0006635	biological_process	fatty acid beta-oxidation
A	0006695	biological_process	cholesterol biosynthetic process
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	0006631	biological_process	fatty acid metabolic process
B	0006635	biological_process	fatty acid beta-oxidation
B	0006695	biological_process	cholesterol biosynthetic process
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	0006631	biological_process	fatty acid metabolic process
C	0006635	biological_process	fatty acid beta-oxidation
C	0006695	biological_process	cholesterol biosynthetic process
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	0006631	biological_process	fatty acid metabolic process
D	0006635	biological_process	fatty acid beta-oxidation
D	0006695	biological_process	cholesterol biosynthetic process
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	4
Details	ACT_SITE: Acyl-thioester intermediate => ECO:0000305\|PubMed:25478839

Chain	Residue	Details
A	CSO92
B	CSO92
C	CSO92
D	CSO92

site_id	SWS_FT_FI2
Number of Residues	4
Details	ACT_SITE: Proton donor/acceptor => ECO:0000305\|PubMed:25478839

Chain	Residue	Details
A	CYS382
B	CYS382
C	CYS382
D	CYS382

site_id	SWS_FT_FI3
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269\|PubMed:25478839, ECO:0007744\|PDB:4C2J

Chain	Residue	Details
A	ARG224
D	ARG224
D	THR227
D	SER251
A	THR227
A	SER251
B	ARG224
B	THR227
B	SER251
C	ARG224
C	THR227
C	SER251

site_id	SWS_FT_FI4
Number of Residues	4
Details	SITE: Increases nucleophilicity of active site Cys => ECO:0000305\|PubMed:25478839

Chain	Residue	Details
A	HIS352
B	HIS352
C	HIS352
D	HIS352

site_id	SWS_FT_FI5
Number of Residues	36
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000250\|UniProtKB:Q8BWT1

Chain	Residue	Details
A	LYS25
B	LYS25
B	LYS137
B	LYS143
B	LYS171
B	LYS191
B	LYS209
B	LYS234
B	LYS305
B	LYS312
C	LYS25
A	LYS137
C	LYS137
C	LYS143
C	LYS171
C	LYS191
C	LYS209
C	LYS234
C	LYS305
C	LYS312
D	LYS25
D	LYS137
A	LYS143
D	LYS143
D	LYS171
D	LYS191
D	LYS209
D	LYS234
D	LYS305
D	LYS312
A	LYS171
A	LYS191
A	LYS209
A	LYS234
A	LYS305
A	LYS312

site_id	SWS_FT_FI6
Number of Residues	20
Details	MOD_RES: N6-succinyllysine => ECO:0000250\|UniProtKB:Q8BWT1

Chain	Residue	Details
A	LYS45
B	LYS240
C	LYS45
C	LYS211
C	LYS212
C	LYS214
C	LYS240
D	LYS45
D	LYS211
D	LYS212
D	LYS214
A	LYS211
D	LYS240
A	LYS212
A	LYS214
A	LYS240
B	LYS45
B	LYS211
B	LYS212
B	LYS214

site_id	SWS_FT_FI7
Number of Residues	4
Details	MOD_RES: Phosphothreonine => ECO:0007744\|PubMed:18669648

Chain	Residue	Details
A	THR119
B	THR119
C	THR119
D	THR119

site_id	SWS_FT_FI8
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:18669648

Chain	Residue	Details
A	SER121
B	SER121
C	SER121
D	SER121

site_id	SWS_FT_FI9
Number of Residues	4
Details	MOD_RES: Phosphotyrosine => ECO:0007744\|PubMed:18669648

Chain	Residue	Details
A	TYR127
B	TYR127
C	TYR127
D	TYR127

site_id	SWS_FT_FI10
Number of Residues	4
Details	MOD_RES: Phosphothreonine => ECO:0000250\|UniProtKB:Q8BWT1

Chain	Residue	Details
A	THR136
B	THR136
C	THR136
D	THR136

site_id	SWS_FT_FI11
Number of Residues	8
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:24275569

Chain	Residue	Details
A	SER140
A	SER333
B	SER140
B	SER333
C	SER140
C	SER333
D	SER140
D	SER333

site_id	SWS_FT_FI12
Number of Residues	20
Details	MOD_RES: N6-acetyllysine => ECO:0000250\|UniProtKB:Q8BWT1

Chain	Residue	Details
A	LYS241
B	LYS375
C	LYS241
C	LYS269
C	LYS270
C	LYS340
C	LYS375
D	LYS241
D	LYS269
D	LYS270
D	LYS340
A	LYS269
D	LYS375
A	LYS270
A	LYS340
A	LYS375
B	LYS241
B	LYS269
B	LYS270
B	LYS340

site_id	SWS_FT_FI13
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0000250\|UniProtKB:Q8BWT1

Chain	Residue	Details
A	SER310
B	SER310
C	SER310
D	SER310

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