Structure of PDB 3ea3 Chain B

Receptor sequence
>3ea3B (length=296) Species: 1428 (Bacillus thuringiensis) [Search protein sequence]
ASSVNELENWSKWMQPIPDNIPLARISIPGTHDSGTFKLQNPIKQVWGMT
QEYDFRYQMDHGARIFDIRGRLTDDNTIVLHHGPLYLYVTLHEFINEAKQ
FLKDNPSETIIMSLKKEYEDMKGAEGSFSSTFEKNYFVDPIFLKTEGNIK
LGDARGKIVLLKRYSGSNESGGYNNFYWPDNETFTTTVNQNVNVTVQDKY
KVNYDEKVKSIKDTMDETMNNSEDLNHLYINFTSLSSGGTAWNSPSSSAS
SINPEIANDIKQKNPTRVGWVIQDYINEKWSPLLYQEVIRANKSLI
3D structure
PDB3ea3 Modulation of Bacillus thuringiensis Phosphatidylinositol-specific Phospholipase C Activity by Mutations in the Putative Dimerization Interface.
ChainB
Resolution1.78 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 MN B H32 D33 H82 H32 D33 H82
BS02 MN B N193 D224 H227 N193 D224 H227
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:3ea3, PDBe:3ea3, PDBj:3ea3
PDBsum3ea3
PubMed19369255
UniProtP08954|PLC_BACTU 1-phosphatidylinositol phosphodiesterase

[Back to BioLiP]