5TID

X-ray structure of acyl-CoA thioesterase I, TesA, mutant M141L/Y145K/L146K at pH 5 in complex with octanoic acid

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004064	molecular_function	arylesterase activity
A	0004622	molecular_function	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	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	0052689	molecular_function	carboxylic ester hydrolase activity
A	0052816	molecular_function	long-chain fatty acyl-CoA hydrolase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	11
Details	binding site for residue OCA A 201

Chain	Residue
A	ASP9
A	HOH303
A	HOH438
A	SER10
A	LEU11
A	GLY44
A	ASN73
A	ARG108
A	PRO110
A	HIS157
A	HOH302

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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

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Nucleophile => ECO:0000269|PubMed:15697222, ECO:0000269|PubMed:16515533, ECO:0000305|PubMed:12842470, ECO:0000305|PubMed:12846577, ECO:0000305|PubMed:8098033

Chain	Residue	Details
A	SER10

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site_id	SWS_FT_FI2
Number of Residues	2
Details	ACT_SITE: ACT_SITE => ECO:0000269|PubMed:15697222, ECO:0000269|PubMed:16515533, ECO:0000305|PubMed:12842470, ECO:0000305|PubMed:12846577

Chain	Residue	Details
A	ASP154
A	HIS157

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site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:15697222

Chain	Residue	Details
A	GLY44
A	ASN73

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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

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