Structure of PDB 1isp Chain A Binding Site BS01

Receptor Information
>1isp 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]
EHNPVVMVHGIGGASFNFAGIKSYLVSQGWSRDKLYAVDFWDKTGTNYNN
GPVLSRFVQKVLDETGAKKVDIVAHSMGGANTLYYIKNLDGGNKVANVVT
LGGANRLTTGKALPGTDPNQKILYTSIYSSADMIVMNYLSRLDGARNVQI
HGVGHIGLLYSSQVNSLIKEGLNGGGQNT
Ligand information
Ligand IDGOL
InChIInChI=1S/C3H8O3/c4-1-3(6)2-5/h3-6H,1-2H2
InChIKeyPEDCQBHIVMGVHV-UHFFFAOYSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.0C(C(CO)O)O
ACDLabs 12.01
CACTVS 3.370		OCC(O)CO
FormulaC3 H8 O3
NameGLYCEROL;
GLYCERIN;
PROPANE-1,2,3-TRIOL
ChEMBLCHEMBL692
DrugBankDB09462
ZINCZINC000000895048
PDB chain1isp Chain A Residue 200 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1isp Alternate conformations observed in catalytic serine of Bacillus subtilis lipase determined at 1.3 A resolution.
Resolution1.3 Å
Binding residue
(original residue number in PDB)		G11 I12 G14 N18 H76
Binding residue
(residue number reindexed from 1)		G10 I11 G13 N17 H75
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) I12 S77 M78 D133 H156
Catalytic site (residue number reindexed from 1) I11 S76 M77 D132 H155
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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Cellular Component
External links
PDB RCSB:1isp, PDBe:1isp, PDBj:1isp
PDBsum1isp
PubMed12077437
UniProtP37957|ESTA_BACSU Lipase EstA (Gene Name=estA)

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