Structure of PDB 1cle Chain A

Receptor sequence
>1cleA (length=534) Species: 44322 (Limtongozyma cylindracea) [Search protein sequence]
APTAKLANGDTITGLNAIINEAFLGIPFAEPPVGNLRFKDPVPYSGSLNG
QKFTSYGPSCMQQNPEGTFEENLGKTALDLVMQSKVFQAVLPQSEDCLTI
NVVRPPGTKAGANLPVMLWIFGGGFEIGSPTIFPPAQMVTKSVLMGKPII
HVAVNYRVASWGFLAGDDIKAEGSGNAGLKDQRLGMQWVADNIAGFGGDP
SKVTIFGESAGSMSVLCHLIWNDGDNTYKGKPLFRAGIMQSGAMVPSDPV
DGTYGNEIYDLFVSSAGCGSASDKLACLRSASSDTLLDATNNTPGFLAYS
SLRLSYLPRPDGKNITDDMYKLVRDGKYASVPVIIGDQNDEGTVFGLSSL
NVTTNAQARAYFKQSFIHASDAEIDTLMAAYPQDITQGSPFDTGIFNAIT
PQFKRISAVLGDLAFIHARRYFLNHFQGGTKYSFLSKQLSGLPIMGTFHA
NDIVWQDYLLGSGSVIYNNAFIAFATDLDPNTAGLLVNWPKYTSSSQSGN
NLMMINALGLYTGKDNFRTAGYDALMTNPSSFFV
3D structure
PDB1cle Structure of uncomplexed and linoleate-bound Candida cylindracea cholesterol esterase.
ChainA
Resolution2.0 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 A159 S209 A210 Y254 L304 Y306 E341 H449
Catalytic site (residue number reindexed from 1) G123 G124 A159 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 CLL A G122 G124 I132 F133 E208 S209 M213 P246 F296 L302 R303 L304 S365 F366 L410 I453 Y458 G122 G124 I132 F133 E208 S209 M213 P246 F296 L302 R303 L304 S365 F366 L410 I453 Y458
Gene Ontology
Molecular Function
GO:0004806 triacylglycerol lipase activity
GO:0016787 hydrolase activity
Biological Process
GO:0008203 cholesterol metabolic process
GO:0016042 lipid catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1cle, PDBe:1cle, PDBj:1cle
PDBsum1cle
PubMed7788294
UniProtP32947|LIP3_DIURU Lipase 3 (Gene Name=LIP3)

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