Structure of PDB 1gpl Chain A Binding Site BS01
Receptor Information
>1gpl Chain A (length=432) Species:
9606,10141
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AEVCYSHLGCFSDEKPWAGTSQRPIKSLPSDPKKINTRFLLYTNENQNSY
QLITATDIATIKASNFNLNRKTRFIIHGFTDSGENSWLSDMCKNMFQVEK
VNCICVDWKGGSKAQYSQASQNIRVVGAEVAYLVQVLSTSLNYAPENVHI
IGHSLGAHTAGEAGKRLNGLVGRITGLDPAEPYFQDTPEEVRLDPSDAKF
VDVIHTDISPILPSLGFGMSQKVGHMDFFPNGGKDMPGCKTGISCNHHRS
IEYYHSSILNPEGFLGYPCASYDEFQESGCFPCPAKGCPKMGHFADQYPG
KTNAVEQTFFLNTGASDNFTRWRYKVSVTLSGKKVTGHILVSLFGNKGNS
KQYEIFKGTLKPDSTHSNEFDSDVDVGDLQMVKFIWYNNVINPTLPRVGA
SKIIVETNVGKQFNFCSPETVREEVLLTLTPC
Ligand information
Ligand ID
CA
InChI
InChI=1S/Ca/q+2
InChIKey
BHPQYMZQTOCNFJ-UHFFFAOYSA-N
SMILES
Software
SMILES
CACTVS 3.341
[Ca++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Ca+2]
Formula
Ca
Name
CALCIUM ION
ChEMBL
DrugBank
DB14577
ZINC
PDB chain
1gpl Chain A Residue 500 [
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Receptor-Ligand Complex Structure
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PDB
1gpl
A pancreatic lipase with a phospholipase A1 activity: crystal structure of a chimeric pancreatic lipase-related protein 2 from guinea pig.
Resolution
2.01 Å
Binding residue
(original residue number in PDB)
E187 R190 D192 D195
Binding residue
(residue number reindexed from 1)
E189 R192 D194 D197
Annotation score
1
Enzymatic activity
Catalytic site (original residue number in PDB)
F77 S152 L153 D176 H263
Catalytic site (residue number reindexed from 1)
F79 S154 L155 D178 H247
Enzyme Commision number
3.1.1.26
: galactolipase.
3.1.1.3
: triacylglycerol lipase.
Gene Ontology
Molecular Function
GO:0004806
triacylglycerol lipase activity
GO:0016298
lipase activity
GO:0052689
carboxylic ester hydrolase activity
Biological Process
GO:0006629
lipid metabolic process
View graph for
Molecular Function
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Biological Process
External links
PDB
RCSB:1gpl
,
PDBe:1gpl
,
PDBj:1gpl
PDBsum
1gpl
PubMed
8939760
UniProt
P16233
|LIPP_HUMAN Pancreatic triacylglycerol lipase (Gene Name=PNLIP);
P81139
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