Structure of PDB 1aql Chain A Binding Site BS02
Receptor Information
>1aql Chain A (length=532) Species:
9913
(Bos taurus) [
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AKLGSVYTEGGFVEGVNKKLSLFGDSIDIFKGIPFAAAPKALEKPERHPG
WQGTLKAKSFKKRCLQATLTQDSTYGNEDCLYLNIWVPQGRKEVSHDLPV
MIWIYGGAFLMGASQGANFLSNYLYDGEEIATRGNVIVVTFNYRVGPLGF
LSTGDSNLPGNYGLWDQHMAIAWVKRNIEAFGGDPDNITLFGESAGGASV
SLQTLSPYNKGLIKRAISQSGVGLCPWAIQQDPLFWAKRIAEKVGCPVDD
TSKMAGCLKITDPRALTLAYKLPLGSTEYPKLHYLSFVPVIDGDFIPDDP
VNLYANAADVDYIAGTNDMDGHLFVGMDVPAINSNKQDVTEEDFYKLVSG
LTVTKGLRGANATYEVYTEPWAQDSSQETRKKTMVDLETDILFLIPTKIA
VAQHKSHAKSANTYTYLFSQPSRMPIYPKWMGADHADDLQYVFGKPFATP
LGYRAQDRTVSKAMIAYWTNFARTGDPNTGHSTVPANWDPYTLEDDNYLE
INKQMDSNSMKLHLRTNYLQFWTQTYQALPTV
Ligand information
Ligand ID
TCH
InChI
InChI=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
InChIKey
WBWWGRHZICKQGZ-HZAMXZRMSA-N
SMILES
Software
SMILES
OpenEye OEToolkits 1.7.2
CC(CCC(=O)NCCS(=O)(=O)O)C1CCC2C1(C(CC3C2C(CC4C3(CCC(C4)O)C)O)O)C
ACDLabs 12.01
O=S(=O)(O)CCNC(=O)CCC(C3CCC2C1C(O)CC4CC(O)CCC4(C)C1CC(O)C23C)C
CACTVS 3.370
C[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 3.370
C[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 1.7.2
C[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
Formula
C26 H45 N O7 S
Name
TAUROCHOLIC ACID
ChEMBL
CHEMBL224867
DrugBank
DB04348
ZINC
ZINC000008214684
PDB chain
1aql Chain A Residue 602 [
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Receptor-Ligand Complex Structure
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PDB
1aql
The crystal structure of bovine bile salt activated lipase: insights into the bile salt activation mechanism.
Resolution
2.8 Å
Binding residue
(original residue number in PDB)
D299 L351 T352 V353 T354 I391 P396 I399
Binding residue
(residue number reindexed from 1)
D299 L351 T352 V353 T354 I391 P396 I399
Annotation score
1
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
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Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:1aql
,
PDBe:1aql
,
PDBj:1aql
PDBsum
1aql
PubMed
9331420
UniProt
P30122
|CEL_BOVIN Bile salt-activated lipase (Fragment) (Gene Name=CEL)
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