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1JMY

Truncated Recombinant Human Bile Salt Stimulated Lipase

Functional Information from GO Data
ChainGOidnamespacecontents
A0006629biological_processlipid metabolic process
A0016788molecular_functionhydrolase activity, acting on ester bonds
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 600
ChainResidue
ALYS62
AARG63
AHIS115

Functional Information from PROSITE/UniProt
site_idPS00122
Number of Residues16
DetailsCARBOXYLESTERASE_B_1 Carboxylesterases type-B serine active site. FGGdpnnItLfGeSAG
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 Residues1
DetailsACT_SITE: Acyl-ester intermediate => ECO:0000255|PROSITE-ProRule:PRU10039, ECO:0000269|PubMed:1991511
ChainResidueDetails
ASER194

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Charge relay system => ECO:0000269|PubMed:1991511
ChainResidueDetails
AASP320
AHIS435

site_idSWS_FT_FI3
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine
ChainResidueDetails
AASN187

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

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PDB entries from 2024-07-24

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