Structure of PDB 1t6m Chain B

Receptor sequence
>1t6mB (length=296) Species: 1428 (Bacillus thuringiensis) [Search protein sequence]
ASSVNELENWSKWMQPIPDNIPLARISIPGTHDSGTFKLQNPIKQVWGMT
QEYDFRYQMDHGARIFDIDGRLTDDNTIVLHHGPLYLYVTLHEFINEAKQ
FLKDNPSETIIMSLKKEYEDMKGAEGSFSSTFEKNYFVDPIFLKTEGNIK
LGDARGKIVLLKRYSGSNESGGYNNFYWPDNETFTTTVNQNVNVTVQDKY
KVNYDEKVKSIKDTMDETMNNSEDLNHLYINFTSLSSGGTAWNSPYYYAS
YINPEIANDIKQKNPTRVGWVIQDYINEKWSPLLYQEVIRANKSLI
3D structure
PDB1t6m X-ray Structure of the R69D Phosphatidylinositol-Specific Phospholipase C Enzyme: Insight into the Role of Calcium and Surrounding Amino Acids in Active Site Geometry and Catalysis.
ChainB
Resolution2.107 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H36 D37 D73 H86 D278
Catalytic site (residue number reindexed from 1) H32 D33 D69 H82 D274
Enzyme Commision number 4.6.1.13: phosphatidylinositol diacylglycerol-lyase.
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 B D37 D73 H86 D33 D69 H82
BS02 CA B D228 N230 D224 N226
Gene Ontology
Molecular Function
GO:0004436 phosphatidylinositol diacylglycerol-lyase activity
GO:0008081 phosphoric diester hydrolase activity
GO:0016829 lyase activity
Biological Process
GO:0006629 lipid metabolic process
GO:0016042 lipid catabolic process
Cellular Component
GO:0005576 extracellular region

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Cellular Component
External links
PDB RCSB:1t6m, PDBe:1t6m, PDBj:1t6m
PDBsum1t6m
PubMed16042375
UniProtP08954|PLC_BACTU 1-phosphatidylinositol phosphodiesterase

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