Structure of PDB 3ea2 Chain A

Receptor sequence
>3ea2A (length=296) Species: 1428 (Bacillus thuringiensis) [Search protein sequence]
ASSVNELENWSKWMQPIPDNIPLARISIPGTHDSGTFKLQNPIKQVWGMT
QEYDFRYQMDHGARIFDIRGRLTDDNTIVLHHGPLYLYVTLHEFINEAKQ
FLKDNPSETIIMSLKKEYEDMKGAEGSFSSTFEKNYFVDPIFLKTEGNIK
LGDARGKIVLLKRYSGSNESGGYNNFYWPDNETFTTTVNQNVNVTVQDKY
KVNYDEKVKSIKDTMDETMNNSEDLNHLYINFTSLSSGGTAWNSPYSYAS
SINPEIANDIKQKNPTRVGWVIQDYINEKWSPLLYQEVIRANKSLI
3D structure
PDB3ea2 Modulation of bacillus thuringiensis phosphatidylinositol-specific phospholipase C activity by mutations in the putative dimerization interface.
ChainA
Resolution1.95 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H32 D33 R69 H82 D274
Catalytic site (residue number reindexed from 1) H32 D33 R69 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 INS A H32 R69 R163 D198 Y200 H32 R69 R163 D198 Y200
BS02 ZN A D224 H227 D224 H227
BS03 ZN A H61 E278 H61 E278
BS04 ZN A D74 D75 D74 D75
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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Biological Process
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Cellular Component
External links
PDB RCSB:3ea2, PDBe:3ea2, PDBj:3ea2
PDBsum3ea2
PubMed19369255
UniProtP08954|PLC_BACTU 1-phosphatidylinositol phosphodiesterase

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