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1F6W

STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN BILE SALT ACTIVATED LIPASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0006629biological_processlipid metabolic process
A0016788molecular_functionhydrolase activity, acting on ester bonds
Functional Information from PROSITE/UniProt
site_idPS00122
Number of Residues16
DetailsCARBOXYLESTERASE_B_1 Carboxylesterases type-B serine active site. FGGdpdnItLfGeSAG
ChainResidueDetails
APHE181-GLY196

site_idPS00941
Number of Residues11
DetailsCARBOXYLESTERASE_B_2 Carboxylesterases type-B signature 2. EDCLYLNIWvP
ChainResidueDetails
AGLU78-PRO88

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues100
DetailsRegion: {"description":"Heparin-binding"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Acyl-ester intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU10039","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1991511","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsActive site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"1991511","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","featureId":"CAR_000141"}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues6
DetailsAnnotated By Reference To The Literature 1aql
ChainResidueDetails
AGLY107
AHIS435
AALA195
AASP320
ASER194
AALA108

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1aql
ChainResidueDetails
AASP294
AHIS322
ASER194

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1aql
ChainResidueDetails
AASP292
AHIS322
ASER194

238895

PDB entries from 2025-07-16

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