1ISP

Crystal structure of Bacillus subtilis lipase at 1.3A resolution

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004806	molecular_function	triglyceride 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	10
Details	BINDING SITE FOR RESIDUE GOL A 200

Chain	Residue
A	GLY11
A	HOH417
A	ILE12
A	GLY14
A	ASN18
A	HIS76
A	SER77
A	ILE157
A	LEU160
A	HOH316

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Nucleophile => ECO:0000305|PubMed:11491291, ECO:0000305|PubMed:11583117, ECO:0000305|PubMed:12077437

Chain	Residue	Details
A	SER77

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site_id	SWS_FT_FI2
Number of Residues	2
Details	ACT_SITE: Charge relay system => ECO:0000305|PubMed:11491291, ECO:0000305|PubMed:11583117, ECO:0000305|PubMed:12077437

Chain	Residue	Details
A	ASP133
A	HIS156

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Catalytic Information from CSA

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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