Structure of PDB 1aql Chain A Binding Site BS01

Receptor Information
>1aql Chain A (length=532) Species: 9913 (Bos taurus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
AKLGSVYTEGGFVEGVNKKLSLFGDSIDIFKGIPFAAAPKALEKPERHPG
WQGTLKAKSFKKRCLQATLTQDSTYGNEDCLYLNIWVPQGRKEVSHDLPV
MIWIYGGAFLMGASQGANFLSNYLYDGEEIATRGNVIVVTFNYRVGPLGF
LSTGDSNLPGNYGLWDQHMAIAWVKRNIEAFGGDPDNITLFGESAGGASV
SLQTLSPYNKGLIKRAISQSGVGLCPWAIQQDPLFWAKRIAEKVGCPVDD
TSKMAGCLKITDPRALTLAYKLPLGSTEYPKLHYLSFVPVIDGDFIPDDP
VNLYANAADVDYIAGTNDMDGHLFVGMDVPAINSNKQDVTEEDFYKLVSG
LTVTKGLRGANATYEVYTEPWAQDSSQETRKKTMVDLETDILFLIPTKIA
VAQHKSHAKSANTYTYLFSQPSRMPIYPKWMGADHADDLQYVFGKPFATP
LGYRAQDRTVSKAMIAYWTNFARTGDPNTGHSTVPANWDPYTLEDDNYLE
INKQMDSNSMKLHLRTNYLQFWTQTYQALPTV
Ligand information
Ligand IDTCH
InChIInChI=1S/C26H45NO7S/c1-15(4-7-23(31)27-10-11-35(32,33)34)18-5-6-19-24-20(14-22(30)26(18,19)3)25(2)9-8-17(28)12-16(25)13-21(24)29/h15-22,24,28-30H,4-14H2,1-3H3,(H,27,31)(H,32,33,34)/t15-,16+,17-,18-,19+,20+,21-,22+,24+,25+,26-/m1/s1
InChIKeyWBWWGRHZICKQGZ-HZAMXZRMSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.2CC(CCC(=O)NCCS(=O)(=O)O)C1CCC2C1(C(CC3C2C(CC4C3(CCC(C4)O)C)O)O)C
ACDLabs 12.01O=S(=O)(O)CCNC(=O)CCC(C3CCC2C1C(O)CC4CC(O)CCC4(C)C1CC(O)C23C)C
CACTVS 3.370C[C@H](CCC(=O)NCC[S](O)(=O)=O)[C@H]1CC[C@H]2[C@@H]3[C@H](O)C[C@@H]4C[C@H](O)CC[C@]4(C)[C@H]3C[C@H](O)[C@]12C
CACTVS 3.370C[CH](CCC(=O)NCC[S](O)(=O)=O)[CH]1CC[CH]2[CH]3[CH](O)C[CH]4C[CH](O)CC[C]4(C)[CH]3C[CH](O)[C]12C
OpenEye OEToolkits 1.7.2C[C@H](CCC(=O)NCCS(=O)(=O)O)[C@H]1CC[C@@H]2[C@@]1([C@H](C[C@H]3[C@H]2[C@@H](C[C@H]4[C@@]3(CC[C@H](C4)O)C)O)O)C
FormulaC26 H45 N O7 S
NameTAUROCHOLIC ACID
ChEMBLCHEMBL224867
DrugBankDB04348
ZINCZINC000008214684
PDB chain1aql Chain A Residue 601 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB1aql The crystal structure of bovine bile salt activated lipase: insights into the bile salt activation mechanism.
Resolution2.8 Å
Binding residue
(original residue number in PDB)		F119 N122 L124 T449
Binding residue
(residue number reindexed from 1)		F119 N122 L124 T449
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) G107 A108 G146 S194 A195 L285 F287 D320 H435
Catalytic site (residue number reindexed from 1) G107 A108 G146 S194 A195 L285 F287 D320 H435
Enzyme Commision number 3.1.1.13: sterol esterase.
3.1.1.3: triacylglycerol lipase.
3.1.1.6: acetylesterase.
Gene Ontology
Molecular Function
GO:0004771 sterol ester esterase activity
GO:0004806 triacylglycerol lipase activity
GO:0008126 acetylesterase activity
GO:0050253 retinyl-palmitate esterase activity
GO:0052689 carboxylic ester hydrolase activity
Biological Process
GO:0016042 lipid catabolic process
GO:0030157 pancreatic juice secretion
GO:0042572 retinol metabolic process
GO:0046514 ceramide catabolic process
Cellular Component
GO:0005576 extracellular region
GO:0005737 cytoplasm

View graph for
Molecular Function
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Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1aql, PDBe:1aql, PDBj:1aql
PDBsum1aql
PubMed9331420
UniProtP30122|CEL_BOVIN Bile salt-activated lipase (Fragment) (Gene Name=CEL)

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