Structure of PDB 2nw6 Chain A

Receptor sequence
>2nw6A (length=320) Species: 292 (Burkholderia cepacia) [Search protein sequence]
ADNYAATRYPIILVHGLTGTDKYAGVLEYWYGIQEDLQQRGATVYVANLS
GFQSDDGPNGRGEQLLAYVKTVLAATGATKVNLVGHSQGGLTSRYVAAVA
PDLVASVTTIGTPHRGSEFADFVQGVLAYDPTGLSSTVIAAFVNVFGILT
SSSNNTNQDALAALKTLTTAQAATYNQNYPSAGLGAPGSCQTGAPTETVG
GNTHLLYSWAGTAIQPTISVFGVTGATDTSTIPLVDPANALDPSTLALFG
TGTVMVNRGSGQNDGVVSKCSALYGQVLSTSYKWNHLDEINQLLGVRGAN
AEDPVAVIRTHANRLKLAGV
3D structure
PDB2nw6 Combined X-ray diffraction and QM/MM study of the Burkholderia cepacia lipase-catalyzed secondary alcohol esterification
ChainA
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) L17 S87 Q88 D242 D264 H286 D288 Q292 V296
Catalytic site (residue number reindexed from 1) L17 S87 Q88 D242 D264 H286 D288 Q292 V296
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 D242 D288 V296 D242 D288 V296
BS02 POT A G16 L17 S87 Q88 A120 H286 G16 L17 S87 Q88 A120 H286
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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Cellular Component
External links
PDB RCSB:2nw6, PDBe:2nw6, PDBj:2nw6
PDBsum2nw6
PubMed18386861
UniProtP22088|LIP_BURCE Triacylglycerol lipase (Gene Name=lip)

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