Structure of PDB 1r50 Chain A Binding Site BS01

Receptor Information
>1r50 Chain A (length=179) Species: 1423 (Bacillus subtilis) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
HNPVVMVHGIGGASFNFAGIKSYLVSQGWSRDKLYAVDFWDKTGTNYNNG
PVLSRFVQKVLDETGAKKVDIVAHSMGGANTLYYIKNLDGGNKVANVVTL
GGANRLTTGKALPGTDPNQKILYTSIYSSADMIVMNYLSRLDGARNVQIH
GVGHIGLLYSSQVNSLIKEGLNGGGQNTN
Ligand information
Ligand IDSIL
InChIInChI=1S/C12H23O5P/c1-4-5-6-7-8-18(13,14)16-10-11-9-15-12(2,3)17-11/h4,11H,1,5-10H2,2-3H3,(H,13,14)/t11-/m1/s1
InChIKeyBUTLRPVAJSANIT-LLVKDONJSA-N
SMILES
SoftwareSMILES
CACTVS 3.341CC1(C)OC[CH](CO[P](O)(=O)CCCCC=C)O1
ACDLabs 10.04O=P(OCC1OC(OC1)(C)C)(O)CCCC\C=C
OpenEye OEToolkits 1.5.0CC1(OCC(O1)COP(=O)(CCCCC=C)O)C
CACTVS 3.341CC1(C)OC[C@H](CO[P@@](O)(=O)CCCCC=C)O1
OpenEye OEToolkits 1.5.0CC1(OC[C@@H](O1)CO[P@](=O)(CCCCC=C)O)C
FormulaC12 H23 O5 P
Name[(4S)-2,2-DIMETHYL-1,3-DIOXOLAN-4-YL]METHYL HYDROGEN HEX-5-ENYLPHOSPHONATE;
O-[(S)-1,2-O-ISOPROPYLIDENE-SN-GLYCEROL]6-HEXENYL PHOSPHONATE;
O-[(S)-IPG] 6-HEXENYL PHOSPHONATE
ChEMBL
DrugBankDB08548
ZINCZINC000033821518
PDB chain1r50 Chain A Residue 277 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1r50 Directed Evolution of Bacillus subtilis Lipase A by Use of Enantiomeric Phosphonate Inhibitors: Crystal Structures and Phage Display Selection
Resolution1.45 Å
Binding residue
(original residue number in PDB)		G11 I12 G14 H76 S77 M78 I135 H156
Binding residue
(residue number reindexed from 1)		G9 I10 G12 H74 S75 M76 I133 H154
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) I12 S77 M78 D133 H156
Catalytic site (residue number reindexed from 1) I10 S75 M76 D131 H154
Enzyme Commision number 3.1.1.3: triacylglycerol lipase.
Gene Ontology
Molecular Function
GO:0004806 triacylglycerol lipase activity
GO:0016298 lipase activity
GO:0016787 hydrolase activity
Biological Process
GO:0016042 lipid catabolic process
Cellular Component
GO:0005576 extracellular region

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1r50, PDBe:1r50, PDBj:1r50
PDBsum1r50
PubMed16342303
UniProtP37957|ESTA_BACSU Lipase EstA (Gene Name=estA)

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