Structure of PDB 1gpl Chain A

Receptor sequence
>1gplA (length=432) Species: 9606,10141 [Search protein sequence]
AEVCYSHLGCFSDEKPWAGTSQRPIKSLPSDPKKINTRFLLYTNENQNSY
QLITATDIATIKASNFNLNRKTRFIIHGFTDSGENSWLSDMCKNMFQVEK
VNCICVDWKGGSKAQYSQASQNIRVVGAEVAYLVQVLSTSLNYAPENVHI
IGHSLGAHTAGEAGKRLNGLVGRITGLDPAEPYFQDTPEEVRLDPSDAKF
VDVIHTDISPILPSLGFGMSQKVGHMDFFPNGGKDMPGCKTGISCNHHRS
IEYYHSSILNPEGFLGYPCASYDEFQESGCFPCPAKGCPKMGHFADQYPG
KTNAVEQTFFLNTGASDNFTRWRYKVSVTLSGKKVTGHILVSLFGNKGNS
KQYEIFKGTLKPDSTHSNEFDSDVDVGDLQMVKFIWYNNVINPTLPRVGA
SKIIVETNVGKQFNFCSPETVREEVLLTLTPC
3D structure
PDB1gpl A pancreatic lipase with a phospholipase A1 activity: crystal structure of a chimeric pancreatic lipase-related protein 2 from guinea pig.
ChainA
Resolution2.01 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 CA A E187 R190 D192 D195 E189 R192 D194 D197
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

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Molecular Function
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Biological Process
External links
PDB RCSB:1gpl, PDBe:1gpl, PDBj:1gpl
PDBsum1gpl
PubMed8939760
UniProtP16233|LIPP_HUMAN Pancreatic triacylglycerol lipase (Gene Name=PNLIP);
P81139

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