Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3F5O

Crystal Structure of hTHEM2(undecan-2-one-CoA) complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005739	cellular_component	mitochondrion
A	0005759	cellular_component	mitochondrial matrix
A	0005819	cellular_component	spindle
A	0005829	cellular_component	cytosol
A	0005856	cellular_component	cytoskeleton
A	0006629	biological_process	lipid metabolic process
A	0016787	molecular_function	hydrolase activity
A	0046872	molecular_function	metal ion binding
A	0047617	molecular_function	fatty acyl-CoA hydrolase activity
A	0051289	biological_process	protein homotetramerization
A	0120163	biological_process	negative regulation of cold-induced thermogenesis
B	0005515	molecular_function	protein binding
B	0005634	cellular_component	nucleus
B	0005737	cellular_component	cytoplasm
B	0005739	cellular_component	mitochondrion
B	0005759	cellular_component	mitochondrial matrix
B	0005819	cellular_component	spindle
B	0005829	cellular_component	cytosol
B	0005856	cellular_component	cytoskeleton
B	0006629	biological_process	lipid metabolic process
B	0016787	molecular_function	hydrolase activity
B	0046872	molecular_function	metal ion binding
B	0047617	molecular_function	fatty acyl-CoA hydrolase activity
B	0051289	biological_process	protein homotetramerization
B	0120163	biological_process	negative regulation of cold-induced thermogenesis
C	0005515	molecular_function	protein binding
C	0005634	cellular_component	nucleus
C	0005737	cellular_component	cytoplasm
C	0005739	cellular_component	mitochondrion
C	0005759	cellular_component	mitochondrial matrix
C	0005819	cellular_component	spindle
C	0005829	cellular_component	cytosol
C	0005856	cellular_component	cytoskeleton
C	0006629	biological_process	lipid metabolic process
C	0016787	molecular_function	hydrolase activity
C	0046872	molecular_function	metal ion binding
C	0047617	molecular_function	fatty acyl-CoA hydrolase activity
C	0051289	biological_process	protein homotetramerization
C	0120163	biological_process	negative regulation of cold-induced thermogenesis
D	0005515	molecular_function	protein binding
D	0005634	cellular_component	nucleus
D	0005737	cellular_component	cytoplasm
D	0005739	cellular_component	mitochondrion
D	0005759	cellular_component	mitochondrial matrix
D	0005819	cellular_component	spindle
D	0005829	cellular_component	cytosol
D	0005856	cellular_component	cytoskeleton
D	0006629	biological_process	lipid metabolic process
D	0016787	molecular_function	hydrolase activity
D	0046872	molecular_function	metal ion binding
D	0047617	molecular_function	fatty acyl-CoA hydrolase activity
D	0051289	biological_process	protein homotetramerization
D	0120163	biological_process	negative regulation of cold-induced thermogenesis
E	0005515	molecular_function	protein binding
E	0005634	cellular_component	nucleus
E	0005737	cellular_component	cytoplasm
E	0005739	cellular_component	mitochondrion
E	0005759	cellular_component	mitochondrial matrix
E	0005819	cellular_component	spindle
E	0005829	cellular_component	cytosol
E	0005856	cellular_component	cytoskeleton
E	0006629	biological_process	lipid metabolic process
E	0016787	molecular_function	hydrolase activity
E	0046872	molecular_function	metal ion binding
E	0047617	molecular_function	fatty acyl-CoA hydrolase activity
E	0051289	biological_process	protein homotetramerization
E	0120163	biological_process	negative regulation of cold-induced thermogenesis
F	0005515	molecular_function	protein binding
F	0005634	cellular_component	nucleus
F	0005737	cellular_component	cytoplasm
F	0005739	cellular_component	mitochondrion
F	0005759	cellular_component	mitochondrial matrix
F	0005819	cellular_component	spindle
F	0005829	cellular_component	cytosol
F	0005856	cellular_component	cytoskeleton
F	0006629	biological_process	lipid metabolic process
F	0016787	molecular_function	hydrolase activity
F	0046872	molecular_function	metal ion binding
F	0047617	molecular_function	fatty acyl-CoA hydrolase activity
F	0051289	biological_process	protein homotetramerization
F	0120163	biological_process	negative regulation of cold-induced thermogenesis
G	0005515	molecular_function	protein binding
G	0005634	cellular_component	nucleus
G	0005737	cellular_component	cytoplasm
G	0005739	cellular_component	mitochondrion
G	0005759	cellular_component	mitochondrial matrix
G	0005819	cellular_component	spindle
G	0005829	cellular_component	cytosol
G	0005856	cellular_component	cytoskeleton
G	0006629	biological_process	lipid metabolic process
G	0016787	molecular_function	hydrolase activity
G	0046872	molecular_function	metal ion binding
G	0047617	molecular_function	fatty acyl-CoA hydrolase activity
G	0051289	biological_process	protein homotetramerization
G	0120163	biological_process	negative regulation of cold-induced thermogenesis
H	0005515	molecular_function	protein binding
H	0005634	cellular_component	nucleus
H	0005737	cellular_component	cytoplasm
H	0005739	cellular_component	mitochondrion
H	0005759	cellular_component	mitochondrial matrix
H	0005819	cellular_component	spindle
H	0005829	cellular_component	cytosol
H	0005856	cellular_component	cytoskeleton
H	0006629	biological_process	lipid metabolic process
H	0016787	molecular_function	hydrolase activity
H	0046872	molecular_function	metal ion binding
H	0047617	molecular_function	fatty acyl-CoA hydrolase activity
H	0051289	biological_process	protein homotetramerization
H	0120163	biological_process	negative regulation of cold-induced thermogenesis

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CL A 151

Chain	Residue
A	ASN50
A	HIS56
A	GLY57
B	UOC149
B	HOH187

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CL C 151

Chain	Residue
D	HOH175
C	ASN50
C	GLY57
D	UOC149
D	COA150

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CL D 151

Chain	Residue
C	UOC149
C	COA150
C	HOH164
D	ASN50
D	HIS56
D	GLY57

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CL E 151

Chain	Residue
E	ASN50
E	GLY57
F	UOC149
F	COA150
F	HOH190

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CL F 151

Chain	Residue
E	UOC149
E	COA150
E	HOH164
E	HOH165
F	ASN50
F	GLY57

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL G 151

Chain	Residue
G	ASN50
G	HIS56
G	GLY57
H	HOH158

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL H 151

Chain	Residue
G	UOC149
G	HOH159
H	ASN50
H	GLY57

site_id	AC8
Number of Residues	10
Details	BINDING SITE FOR RESIDUE UOC A 149

Chain	Residue
A	MET15
A	ASN66
A	MET70
A	LEU73
A	GLY81
A	SER83
A	LYS136
A	COA150
A	HOH1276
B	ASN50

site_id	AC9
Number of Residues	19
Details	BINDING SITE FOR RESIDUE COA A 150

Chain	Residue
A	VAL82
A	SER83
A	HIS137
A	GLY139
A	UOC149
B	TYR90
B	MET91
B	SER92
B	PRO93
C	LYS108
C	GLY110
C	LYS111
C	THR112
C	LEU113
C	PHE115
C	HOH163
C	HOH606
C	HOH1268
H	ARG19

site_id	BC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE UOC B 149

Chain	Residue
A	ASN50
A	ALA51
A	CL151
B	GLY81
B	VAL82
B	LYS136
B	COA150
B	P6G1001

site_id	BC2
Number of Residues	17
Details	BINDING SITE FOR RESIDUE COA B 150

Chain	Residue
A	TYR90
A	MET91
A	SER92
A	PRO93
A	HOH335
B	SER83
B	HIS137
B	UOC149
D	LYS108
D	GLY110
D	LYS111
D	THR112
D	LEU113
D	PHE115
D	HOH298
D	HOH586
D	HOH633

site_id	BC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE UOC C 149

Chain	Residue
C	GLY81
C	VAL82
C	LYS136
C	COA150
C	HOH611
D	ASN50
D	CL151

site_id	BC4
Number of Residues	25
Details	BINDING SITE FOR RESIDUE COA C 150

Chain	Residue
A	THR112
A	LEU113
A	PHE115
A	HOH157
A	HOH287
A	HOH332
A	HOH473
A	HOH1172
A	HOH1192
C	SER83
C	HIS137
C	GLY139
C	UOC149
D	LEU55
D	TYR90
D	MET91
D	SER92
D	PRO93
D	LYS95
D	CL151
D	HOH153
D	HOH357
A	LYS108
A	GLY110
A	LYS111

site_id	BC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE UOC D 149

Chain	Residue
C	ASN50
C	CL151
D	GLY81
D	LYS136
D	COA150
D	HOH338

site_id	BC6
Number of Residues	24
Details	BINDING SITE FOR RESIDUE COA D 150

Chain	Residue
B	LYS108
B	GLY110
B	LYS111
B	THR112
B	LEU113
B	PHE115
B	HOH154
B	HOH186
B	HOH210
B	HOH682
B	HOH750
B	HOH1080
B	HOH1233
C	TYR90
C	MET91
C	SER92
C	PRO93
C	CL151
C	HOH162
D	SER83
D	HIS137
D	UOC149
E	ARG19
F	GLU46

site_id	BC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE UOC E 149

Chain	Residue
E	ASN66
E	THR69
E	GLY81
E	LYS136
E	COA150
F	ASN50
F	CL151

site_id	BC8
Number of Residues	22
Details	BINDING SITE FOR RESIDUE COA E 150

Chain	Residue
E	SER83
E	HIS137
E	UOC149
F	TYR90
F	MET91
F	SER92
F	PRO93
F	CL151
F	HOH155
F	HOH1274
G	LYS108
G	GLY110
G	LYS111
G	THR112
G	LEU113
G	PHE115
G	HOH158
G	HOH229
G	HOH524
G	HOH649
G	HOH1123
G	HOH1197

site_id	BC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE UOC F 149

Chain	Residue
E	ASN50
E	ALA51
E	CL151
E	P6G1001
F	GLY81
F	LYS136
F	COA150

site_id	CC1
Number of Residues	22
Details	BINDING SITE FOR RESIDUE COA F 150

Chain	Residue
E	TYR90
E	MET91
E	SER92
E	PRO93
E	LYS95
E	CL151
E	HOH213
F	SER83
F	HIS137
F	GLY139
F	UOC149
H	LYS108
H	GLY110
H	LYS111
H	THR112
H	LEU113
H	PHE115
H	HOH350
H	HOH354
H	HOH489
H	HOH947
H	HOH1272

site_id	CC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE UOC G 149

Chain	Residue
G	PRO80
G	GLY81
G	LYS136
G	COA150
G	P6G1001
H	ASN50
H	CL151

site_id	CC3
Number of Residues	22
Details	BINDING SITE FOR RESIDUE COA G 150

Chain	Residue
E	LYS108
E	GLY110
E	LYS111
E	THR112
E	LEU113
E	PHE115
E	HOH161
E	HOH262
E	HOH448
E	HOH678
E	HOH893
E	HOH1202
G	SER83
G	HIS137
G	GLY139
G	UOC149
H	TYR90
H	MET91
H	SER92
H	PRO93
H	LYS95
H	HOH159

site_id	CC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE UOC H 149

Chain	Residue
G	ASN50
H	MET15
H	GLY81
H	LYS136
H	COA150
H	HOH468
H	HOH1204

site_id	CC5
Number of Residues	18
Details	BINDING SITE FOR RESIDUE COA H 150

Chain	Residue
F	LYS108
F	GLY110
F	LYS111
F	THR112
F	LEU113
F	PHE115
F	HOH478
F	HOH627
F	HOH1259
G	TYR90
G	MET91
G	SER92
G	PRO93
G	HOH421
H	VAL82
H	SER83
H	HIS137
H	UOC149

site_id	CC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE P6G B 1001

Chain	Residue
A	ALA51
B	VAL11
B	MET15
B	ASN20
B	UOC149

site_id	CC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE P6G C 1001

Chain	Residue
C	VAL11
C	ASN20
D	ALA51

site_id	CC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE P6G E 1001

Chain	Residue
E	ALA51
F	MET15
F	ALA18
F	ASN20
F	GLU22
F	UOC149

site_id	CC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE P6G G 1001

Chain	Residue
G	VAL11
G	ALA14
G	MET15
G	ASN20
G	GLU22
G	UOC149
H	ALA51

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	40
Details	BINDING: BINDING => ECO:0000269\|PubMed:19170545, ECO:0007744\|PDB:3F5O

Chain	Residue	Details
A	GLU46
B	HIS137
C	GLU46
C	SER83
C	TYR90
C	LYS108
C	HIS137
D	GLU46
D	SER83
D	TYR90
D	LYS108
A	SER83
D	HIS137
E	GLU46
E	SER83
E	TYR90
E	LYS108
E	HIS137
F	GLU46
F	SER83
F	TYR90
F	LYS108
A	TYR90
F	HIS137
G	GLU46
G	SER83
G	TYR90
G	LYS108
G	HIS137
H	GLU46
H	SER83
H	TYR90
H	LYS108
A	LYS108
H	HIS137
A	HIS137
B	GLU46
B	SER83
B	TYR90
B	LYS108

site_id	SWS_FT_FI2
Number of Residues	16
Details	BINDING: BINDING => ECO:0000305\|PubMed:19170545, ECO:0007744\|PDB:3F5O

Chain	Residue	Details
A	ASN50
E	GLY81
F	ASN50
F	GLY81
G	ASN50
G	GLY81
H	ASN50
H	GLY81
A	GLY81
B	ASN50
B	GLY81
C	ASN50
C	GLY81
D	ASN50
D	GLY81
E	ASN50

site_id	SWS_FT_FI3
Number of Residues	8
Details	MOD_RES: N-acetylmethionine => ECO:0007744\|PubMed:22223895, ECO:0007744\|PubMed:22814378, ECO:0007744\|PubMed:25944712

Chain	Residue	Details
A	MET1
B	MET1
C	MET1
D	MET1
E	MET1
F	MET1
G	MET1
H	MET1

site_id	SWS_FT_FI4
Number of Residues	8
Details	MOD_RES: N-acetylthreonine; in Acyl-coenzyme A thioesterase 13, N-terminally processed => ECO:0007744\|PubMed:19413330, ECO:0007744\|PubMed:22223895, ECO:0007744\|PubMed:22814378, ECO:0007744\|PubMed:25944712

Chain	Residue	Details
A	THR2
B	THR2
C	THR2
D	THR2
E	THR2
F	THR2
G	THR2
H	THR2

site_id	SWS_FT_FI5
Number of Residues	40
Details	MOD_RES: N6-acetyllysine => ECO:0000250\|UniProtKB:Q9CQR4

Chain	Residue	Details
A	LYS27
B	LYS127
C	LYS27
C	LYS37
C	LYS43
C	LYS108
C	LYS127
D	LYS27
D	LYS37
D	LYS43
D	LYS108
A	LYS37
D	LYS127
E	LYS27
E	LYS37
E	LYS43
E	LYS108
E	LYS127
F	LYS27
F	LYS37
F	LYS43
F	LYS108
A	LYS43
F	LYS127
G	LYS27
G	LYS37
G	LYS43
G	LYS108
G	LYS127
H	LYS27
H	LYS37
H	LYS43
H	LYS108
A	LYS108
H	LYS127
A	LYS127
B	LYS27
B	LYS37
B	LYS43
B	LYS108

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