1THG

1.8 ANGSTROMS REFINED STRUCTURE OF THE LIPASE FROM GEOTRICHUM CANDIDUM

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	0016787	molecular_function	hydrolase activity

Functional Information from PDB Data

site_id	ACT
Number of Residues	3
Details	ACTIVE SITE

Chain	Residue
A	SER217
A	GLU354
A	HIS463

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Functional Information from PROSITE/UniProt

site_id	PS00122
Number of Residues	16
Details	CARBOXYLESTERASE_B_1 Carboxylesterases type-B serine active site. FGGdpdkVmIfGeSAG

Chain	Residue	Details
A	PHE204-GLY219

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site_id	PS00941
Number of Residues	11
Details	CARBOXYLESTERASE_B_2 Carboxylesterases type-B signature 2. EDCLYLNVFrP

Chain	Residue	Details
A	GLU103-PRO113

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"description":"Acyl-ester intermediate"}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	2
Details	Active site: {"description":"Charge relay system"}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	5
Details

Chain	Residue	Details
A	HIS463
A	GLU354
A	ALA218
A	ALA132
A	SER217

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site_id	MCSA1
Number of Residues	5
Details	M-CSA 520

Chain	Residue	Details
A	GLY136	electrostatic stabiliser
A	MET221	covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor
A	SER222	electrostatic stabiliser
A	PHE358	electrostatic stabiliser, increase basicity, modifies pKa
A	LEU467	proton acceptor, proton donor

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