1T2N

Structure of a thermostable triple mutant of Bacillus subtilis lipase obtained through directed evolution

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004806	molecular_function	triacylglycerol lipase activity
A	0005576	cellular_component	extracellular region
A	0006629	biological_process	lipid metabolic process
A	0016042	biological_process	lipid catabolic process
A	0016298	molecular_function	lipase activity
A	0016787	molecular_function	hydrolase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE K A 374

Chain	Residue
A	MET134
A	HIS156

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"11491291","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"11583117","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"12077437","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	2
Details	Active site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"11491291","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"11583117","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"12077437","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	5
Details	Annotated By Reference To The Literature 1r4z

Chain	Residue	Details
A	ASP133
A	HIS156
A	MET78
A	SER77
A	ILE12

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site_id	MCSA1
Number of Residues	5
Details	M-CSA 518

Chain	Residue	Details
A	ILE12	electrostatic stabiliser
A	SER77	covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor
A	MET78	electrostatic stabiliser
A	ASP133	electrostatic stabiliser, increase basicity, modifies pKa
A	HIS156	proton acceptor, proton donor

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