Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6LFC

E. coli Thioesterase I mutant DG

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004064	molecular_function	arylesterase activity
A	0004622	molecular_function	phosphatidylcholine lysophospholipase activity
A	0006508	biological_process	proteolysis
A	0006629	biological_process	lipid metabolic process
A	0008233	molecular_function	peptidase activity
A	0016297	molecular_function	fatty acyl-[ACP] hydrolase activity
A	0016298	molecular_function	lipase activity
A	0016787	molecular_function	hydrolase activity
A	0030288	cellular_component	outer membrane-bounded periplasmic space
A	0042597	cellular_component	periplasmic space
A	0042802	molecular_function	identical protein binding
A	0047617	molecular_function	fatty acyl-CoA hydrolase activity
A	0052816	molecular_function	long-chain fatty acyl-CoA hydrolase activity
B	0004064	molecular_function	arylesterase activity
B	0004622	molecular_function	phosphatidylcholine lysophospholipase activity
B	0006508	biological_process	proteolysis
B	0006629	biological_process	lipid metabolic process
B	0008233	molecular_function	peptidase activity
B	0016297	molecular_function	fatty acyl-[ACP] hydrolase activity
B	0016298	molecular_function	lipase activity
B	0016787	molecular_function	hydrolase activity
B	0030288	cellular_component	outer membrane-bounded periplasmic space
B	0042597	cellular_component	periplasmic space
B	0042802	molecular_function	identical protein binding
B	0047617	molecular_function	fatty acyl-CoA hydrolase activity
B	0052816	molecular_function	long-chain fatty acyl-CoA hydrolase activity
C	0004064	molecular_function	arylesterase activity
C	0004622	molecular_function	phosphatidylcholine lysophospholipase activity
C	0006508	biological_process	proteolysis
C	0006629	biological_process	lipid metabolic process
C	0008233	molecular_function	peptidase activity
C	0016297	molecular_function	fatty acyl-[ACP] hydrolase activity
C	0016298	molecular_function	lipase activity
C	0016787	molecular_function	hydrolase activity
C	0030288	cellular_component	outer membrane-bounded periplasmic space
C	0042597	cellular_component	periplasmic space
C	0042802	molecular_function	identical protein binding
C	0047617	molecular_function	fatty acyl-CoA hydrolase activity
C	0052816	molecular_function	long-chain fatty acyl-CoA hydrolase activity
D	0004064	molecular_function	arylesterase activity
D	0004622	molecular_function	phosphatidylcholine lysophospholipase activity
D	0006508	biological_process	proteolysis
D	0006629	biological_process	lipid metabolic process
D	0008233	molecular_function	peptidase activity
D	0016297	molecular_function	fatty acyl-[ACP] hydrolase activity
D	0016298	molecular_function	lipase activity
D	0016787	molecular_function	hydrolase activity
D	0030288	cellular_component	outer membrane-bounded periplasmic space
D	0042597	cellular_component	periplasmic space
D	0042802	molecular_function	identical protein binding
D	0047617	molecular_function	fatty acyl-CoA hydrolase activity
D	0052816	molecular_function	long-chain fatty acyl-CoA hydrolase activity
E	0004064	molecular_function	arylesterase activity
E	0004622	molecular_function	phosphatidylcholine lysophospholipase activity
E	0006508	biological_process	proteolysis
E	0006629	biological_process	lipid metabolic process
E	0008233	molecular_function	peptidase activity
E	0016297	molecular_function	fatty acyl-[ACP] hydrolase activity
E	0016298	molecular_function	lipase activity
E	0016787	molecular_function	hydrolase activity
E	0030288	cellular_component	outer membrane-bounded periplasmic space
E	0042597	cellular_component	periplasmic space
E	0042802	molecular_function	identical protein binding
E	0047617	molecular_function	fatty acyl-CoA hydrolase activity
E	0052816	molecular_function	long-chain fatty acyl-CoA hydrolase activity
F	0004064	molecular_function	arylesterase activity
F	0004622	molecular_function	phosphatidylcholine lysophospholipase activity
F	0006508	biological_process	proteolysis
F	0006629	biological_process	lipid metabolic process
F	0008233	molecular_function	peptidase activity
F	0016297	molecular_function	fatty acyl-[ACP] hydrolase activity
F	0016298	molecular_function	lipase activity
F	0016787	molecular_function	hydrolase activity
F	0030288	cellular_component	outer membrane-bounded periplasmic space
F	0042597	cellular_component	periplasmic space
F	0042802	molecular_function	identical protein binding
F	0047617	molecular_function	fatty acyl-CoA hydrolase activity
F	0052816	molecular_function	long-chain fatty acyl-CoA hydrolase activity

Functional Information from PROSITE/UniProt

site_id	PS01098
Number of Residues	11
Details	LIPASE_GDSL_SER Lipolytic enzymes "G-D-S-L" family, serine active site. LLILGDSLs.AG

Chain	Residue	Details
A	LEU4-GLY14

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI2
Number of Residues	6
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"15697222","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16515533","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12842470","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"12846577","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"8098033","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	12
Details	Active site: {"evidences":[{"source":"PubMed","id":"15697222","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16515533","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12842470","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"12846577","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15697222","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	5
Details	M-CSA 755

Chain	Residue	Details
A	SER10	covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor
A	GLY44	electrostatic stabiliser
A	ASN73	electrostatic stabiliser
A	ASP154	electrostatic stabiliser, increase basicity
A	HIS157	electrostatic stabiliser, proton acceptor, proton donor

site_id	MCSA2
Number of Residues	5
Details	M-CSA 755

Chain	Residue	Details
B	SER10	covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor
B	GLY44	electrostatic stabiliser
B	ASN73	electrostatic stabiliser
B	ASP154	electrostatic stabiliser, increase basicity
B	HIS157	electrostatic stabiliser, proton acceptor, proton donor

site_id	MCSA3
Number of Residues	5
Details	M-CSA 755

Chain	Residue	Details
C	SER10	covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor
C	GLY44	electrostatic stabiliser
C	ASN73	electrostatic stabiliser
C	ASP154	electrostatic stabiliser, increase basicity
C	HIS157	electrostatic stabiliser, proton acceptor, proton donor

site_id	MCSA4
Number of Residues	5
Details	M-CSA 755

Chain	Residue	Details
D	SER10	covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor
D	GLY44	electrostatic stabiliser
D	ASN73	electrostatic stabiliser
D	ASP154	electrostatic stabiliser, increase basicity
D	HIS157	electrostatic stabiliser, proton acceptor, proton donor

site_id	MCSA5
Number of Residues	5
Details	M-CSA 755

Chain	Residue	Details
E	SER10	covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor
E	GLY44	electrostatic stabiliser
E	ASN73	electrostatic stabiliser
E	ASP154	electrostatic stabiliser, increase basicity
E	HIS157	electrostatic stabiliser, proton acceptor, proton donor

site_id	MCSA6
Number of Residues	5
Details	M-CSA 755

Chain	Residue	Details
F	SER10	covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor
F	GLY44	electrostatic stabiliser
F	ASN73	electrostatic stabiliser
F	ASP154	electrostatic stabiliser, increase basicity
F	HIS157	electrostatic stabiliser, proton acceptor, proton donor

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