Structure of PDB 3rar Chain A

Receptor sequence
>3rarA (length=534) Species: 5481 (Diutina rugosa) [Search protein sequence]
APTATLANGDTITGLNAIINEAFLGIPFAEPPVGNLRFKDPVPYSGSLDG
QKFTSYGPSCMQQNPEGTYEENLPKAALDLVMQSKVFEAVSPSSEDCLTI
NVVRPPGTKAGANLPVMLWIFGGGFEVGGTSTFPPAQMITKSIAMGKPII
HVSVNYRVSSWGFLAGDEIKAEGSANAGLKDQRLGMQWVADNIAAFGGDP
TKVTIFGESAGSMSVMCHILWNDGDNTYKGKPLFRAGIMQSGAMVPSDAV
DGIYGNEIFDLLASNAGCGSASDKLACLRGVSSDTLEDATNNTPGFLAYS
SLRLSYLPRPDGVNITDDMYALVREGKYANIPVIIGDQNDEGTFFGTSSL
NVTTDAQAREYFKQSFVHASDAEIDTLMTAYPGDITQGSPFDTGILNALT
PQFKRISAVLGDLGFTLARRYFLNHYTGGTKYSFLSKQLSGLPVLGTFHS
NDIVFQDYLLGSGSLIYNNAFIAFATDLDPNTAGLLVKWPEYTSSSQSGN
NLMMINALGLYTGKDNFRTAGYDALFSNPPSFFV
3D structure
PDB3rar Insights into the molecular basis of chiral acid recognition by Candida rugosa lipase from an X-ray crystal structure of a bound phosphonate transition state analog
ChainA
Resolution2.19 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) G123 G124 S159 S209 A210 Y254 L304 Y306 E341 H449
Catalytic site (residue number reindexed from 1) G123 G124 S159 S209 A210 Y254 L304 Y306 E341 H449
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 IAN A G123 G124 S209 A210 M213 F296 L304 F345 H449 G123 G124 S209 A210 M213 F296 L304 F345 H449
Gene Ontology
Molecular Function
GO:0004806 triacylglycerol lipase activity
GO:0016787 hydrolase activity
Biological Process
GO:0016042 lipid catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3rar, PDBe:3rar, PDBj:3rar
PDBsum3rar
PubMed
UniProtP20261|LIP1_DIURU Lipase 1 (Gene Name=LIP1)

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