Structure of PDB 1oil Chain A Binding Site BS01

Receptor Information

>1oil Chain A (length=320) Species: 292 (Burkholderia cepacia)

ADNYAATRYPIILVHGLTGTDKYAGVLEYWYGIQEDLQQRGATVYVANLS
GFQSDDGPNGRGEQLLAYVKTVLAATGATKVNLVGHSQGGLTSRYVAAVA
PDLVASVTTIGTPHRGSEFADFVQGVLAYDPTGLSSTVIAAFVNVFGILT
SSSNNTNQDALAALKTLTTAQAATYNQNYPSAGLGAPGSCQTGAPTETVG
GNTHLLYSWAGTAIQPTISVFGVTGATDTSTIPLVDPANALDPSTLALFG
TGTVMVNRGSGQNDGVVSKCSALYGQVLSTSYKWNHLDEINQLLGVRGAN
AEDPVAVIRTHANRLKLAGV

Ligand information

• Ligand ID: CA
• InChI: InChI=1S/Ca/q+2
• InChIKey: BHPQYMZQTOCNFJ-UHFFFAOYSA-N
• SMILES:
  CACTVS 3.341: [Ca++]
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Ca+2]
• Formula: Ca
• Name: CALCIUM ION
• DrugBank: DB14577
• PDB chain: 1oil Chain A Residue 401

Receptor-Ligand Complex Structure

Structure summary

• PDB: 1oil The crystal structure of a triacylglycerol lipase from Pseudomonas cepacia reveals a highly open conformation in the absence of a bound inhibitor.
• Resolution: 2.1 Å
• Binding residue (original residue number in PDB): D242 D288 Q292 V296
• Binding residue (residue number reindexed from 1): D242 D288 Q292 V296
• Annotation score: 1

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.

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

External links

• PDB: RCSB:1oil, PDBe:1oil, PDBj:1oil
• PDBsum: 1oil
• PubMed: 9032073
• UniProt: P22088|LIP_BURCE Triacylglycerol lipase (Gene Name=lip)