1F6W

STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN BILE SALT ACTIVATED LIPASE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0006629	biological_process	lipid metabolic process
A	0016788	molecular_function	hydrolase activity, acting on ester bonds

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	PHE181-GLY196

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

Chain	Residue	Details
A	GLU78-PRO88

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Acyl-ester intermediate => ECO:0000255|PROSITE-ProRule:PRU10039, ECO:0000269|PubMed:1991511

Chain	Residue	Details
A	SER194

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site_id	SWS_FT_FI2
Number of Residues	2
Details	ACT_SITE: Charge relay system => ECO:0000269|PubMed:1991511

Chain	Residue	Details
A	ASP320
A	HIS435

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site_id	SWS_FT_FI3
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) (complex) asparagine

Chain	Residue	Details
A	ASN187

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	6
Details	Annotated By Reference To The Literature 1aql

Chain	Residue	Details
A	GLY107
A	HIS435
A	ALA195
A	ASP320
A	SER194
A	ALA108

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site_id	CSA2
Number of Residues	3
Details	Annotated By Reference To The Literature 1aql

Chain	Residue	Details
A	ASP294
A	HIS322
A	SER194

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site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1aql

Chain	Residue	Details
A	ASP292
A	HIS322
A	SER194

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