Structure of PDB 4lip Chain E

Receptor sequence
>4lipE (length=319) Species: 292 (Burkholderia cepacia) [Search protein sequence]
DNYAATRYPIILVHGLTGTDKYAGVLEYWYGIQEDLQQRGATVYVANLSG
FQSDDGPNGRGEQLLAYVKTVLAATGATKVNLVGHSQGGLTSRYVAAVAP
DLVASVTTIGTPHRGSEFADFVQGVLAYDPTGLSSTVIAAFVNVFGILTS
SSNNTNQDALAALKTLTTAQAATYNQNYPSAGLGAPGSCQTGAPTETVGG
NTHLLYSWAGTAIQPTISVFGVTGATDTSTIPLVDPANALDPSTLALFGT
GTVMVNRGSGQNDGVVSKCSALYGQVLSTSYKWNHLDEINQLLGVRGANA
EDPVAVIRTHANRLKLAGV
3D structure
PDB4lip Structural basis of the chiral selectivity of Pseudomonas cepacia lipase
ChainE
Resolution1.75 Å
3D
structure
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Enzymatic activity
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 E D242 D288 Q292 V296 D241 D287 Q291 V295
BS02 CCP E G16 L17 S87 Q88 S117 H286 G15 L16 S86 Q87 S116 H285
Gene Ontology
Molecular Function
GO:0004806 triacylglycerol lipase activity
GO:0016787 hydrolase activity
GO:0046872 metal ion binding
Biological Process
GO:0016042 lipid catabolic process
Cellular Component
GO:0005576 extracellular region

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4lip, PDBe:4lip, PDBj:4lip
PDBsum4lip
PubMed9660188
UniProtP22088|LIP_BURCE Triacylglycerol lipase (Gene Name=lip)

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