Structure of PDB 2es4 Chain A

Receptor sequence
>2es4A (length=316) Species: 337 (Burkholderia glumae) [Search protein sequence]
ADTYAATRYPVILVHGLAGTDKFANVVDYWYGIQSDLQSHGAKVYVANLS
GFQSDDGPNGRGEQLLAYVKQVLAATGATKVNLIGHSQGGLTSRYVAAVA
PQLVASVTTIGTPHRGSEFADFVQDVLKTDPTGLSSTVIAAFVNVFGTLV
SSSHNTDQDALAALRTLTTAQTATYNRNFPSAGLGAPGSCQTGAATETVG
GSQHLLYSWGGTAIQPTSTVTGATDTSTGTLDVANVTDPSTLALLATGAV
MINRASGQNDGLVSRCSSLFGQVISTSYHWNHLDEINQLLGVRGANAEDP
VAVIRTHVNRLKLQGV
3D structure
PDB2es4 Structure of a membrane-based steric chaperone in complex with its lipase substrate.
ChainA
Resolution1.85 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 D241 D263 H285 D287 Q291 V295
Catalytic site (residue number reindexed from 1) L17 S87 Q88 D238 D260 H282 D284 Q288 V292
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 D241 D287 Q291 V295 D238 D284 Q288 V292
Gene Ontology
Molecular Function
GO:0004806 triacylglycerol lipase activity
GO:0005515 protein binding
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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Biological Process
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Cellular Component
External links
PDB RCSB:2es4, PDBe:2es4, PDBj:2es4
PDBsum2es4
PubMed16518399
UniProtP0DUB8|LIP_BURPL Triacylglycerol lipase (Gene Name=lip)

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