Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2F0X

Crystal structure and function of human thioesterase superfamily member 2(THEM2)

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	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	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	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	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	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	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	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	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	9
Details	BINDING SITE FOR RESIDUE SO4 C 1001

Chain	Residue
C	ASP65
C	VAL82
C	SER83
C	HOH1031
C	HOH1044
D	ASN50
D	LEU55
D	HIS56
D	GLY57

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 1002

Chain	Residue
A	ASP65
A	SER83
A	HOH1064
B	ASN50
B	GLY57

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 B 1003

Chain	Residue
A	ARG23
B	ARG23
B	HOH1029
B	HOH1039

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 H 1004

Chain	Residue
G	ASN50
G	GLY57
H	ASP65
H	SER83

site_id	AC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SO4 F 1005

Chain	Residue
E	ASN50
E	LEU55
E	GLY57
F	ASP65
F	VAL82
F	SER83
F	HOH1042
F	HOH1069

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 G 1006

Chain	Residue
G	ASP65
G	SER83
H	ASN50
H	GLY57

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 B 1007

Chain	Residue
B	GLY110
B	LYS111
B	THR112
B	LEU113
D	HIS137

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 B 1008

Chain	Residue
A	ASN50
A	GLY57
B	ASP65
B	SER83

site_id	AC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 C 1009

Chain	Residue
C	LYS37
C	HIS105
G	SER3

site_id	BC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 G 1010

Chain	Residue
G	LYS111
G	THR112
G	LEU113

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 1011

Chain	Residue
A	GLY110
A	LYS111
A	THR112
A	LEU113
A	HOH1052

site_id	BC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 C 1012

Chain	Residue
B	HOH1023
C	GLY110
C	LYS111
C	THR112
C	LEU113
C	HOH1071

site_id	BC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 H 1013

Chain	Residue
F	HIS137
H	GLY110
H	LYS111
H	THR112
H	LEU113
H	HOH1014

site_id	BC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 F 1014

Chain	Residue
F	GLY110
F	LYS111
F	THR112
F	LEU113
F	HOH1045
F	HOH1075
H	HIS137

site_id	BC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 D 1015

Chain	Residue
D	GLY110
D	LYS111
D	THR112
D	LEU113
D	HOH1055

site_id	BC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 D 1016

Chain	Residue
C	ARG23
D	ARG23

site_id	BC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 E 1017

Chain	Residue
E	ARG23
E	HOH1055
F	ARG23

site_id	BC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 E 1018

Chain	Residue
E	GLY110
E	LYS111
E	THR112
E	LEU113

site_id	CC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 E 1019

Chain	Residue
E	ASP65
E	SER83
F	ASN50
F	GLY57

site_id	CC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 C 1020

Chain	Residue
C	ASN50
C	GLY57
D	ASP65
D	SER83

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"PubMed","id":"19170545","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3F5O","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"PubMed","id":"19170545","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"3F5O","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	8
Details	Modified residue: {"description":"N-acetylmethionine","evidences":[{"source":"PubMed","id":"22223895","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"25944712","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	8
Details	Modified residue: {"description":"N-acetylthreonine; in Acyl-coenzyme A thioesterase 13, N-terminally processed","evidences":[{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22223895","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"25944712","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	32
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9CQR4","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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