Structure of PDB 1rp1 Chain A

Receptor sequence
>1rp1A (length=441) Species: 9615 (Canis lupus familiaris) [Search protein sequence]
KEVCYEQIGCFSDAEPWAGTAIRPLKVLPWSPERIGTRFLLYTNKNPNNF
QTLLPSDPSTIGASNFQTDKKTRFIIHGFIDKGEENWLLDMCKNMFKVEE
VNCICVDWKKGSQTSYTQAANNVRVVGAQVAQMLSMLSANYSYSPSQVQL
IGHSLGAHVAGEAGSRTPGLGRITGLDPVEASFQGTPEEVRLDPTDADFV
DVIHTDAAPLIPFLGFGTSQQMGHLDFFPNGGEEMPGCKKNALSQIVDLD
GIWEGTRDFVACNHLRSYKYYSESILNPDGFASYPCASYRAFESNKCFPC
PDQGCPQMGHYADKFAQKYFLNTGDSSNFARWRYGVSITLSGKRATGQAK
VALFGSKGNTHQFNIFKGILKPGSTHSNEFDAKLDVGTIEKVKFLWNNNN
PTFPKVGAAKITVQKGEEKTVHSFCSESTVREDVLLTLTPC
3D structure
PDB1rp1 Reactivation of the totally inactive pancreatic lipase RP1 by structure-predicted point mutations.
ChainA
Resolution2.1 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 D177 H264
Enzyme Commision number 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 E188 R191 D193 D196
Gene Ontology
Molecular Function
GO:0004806 triacylglycerol lipase activity
GO:0005509 calcium ion binding
GO:0016298 lipase activity
GO:0046872 metal ion binding
GO:0052689 carboxylic ester hydrolase activity
Biological Process
GO:0006629 lipid metabolic process
GO:0016042 lipid catabolic process
Cellular Component
GO:0005576 extracellular region

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Molecular Function
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Cellular Component
External links
PDB RCSB:1rp1, PDBe:1rp1, PDBj:1rp1
PDBsum1rp1
PubMed9726421
UniProtP06857|LIPR1_CANLF Inactive pancreatic lipase-related protein 1 (Gene Name=PNLIPRP1)

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