2OR2

Structure of the W47A/W242A Mutant of Bacterial Phosphatidylinositol-Specific Phospholipase C

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Functional Information from GO Data

ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
A0004436molecular_functionphosphatidylinositol diacylglycerol-lyase activity
A0008081molecular_functionphosphoric diester hydrolase activity
A0016042biological_processlipid catabolic process
B0005576cellular_componentextracellular region
B0004436molecular_functionphosphatidylinositol diacylglycerol-lyase activity
B0008081molecular_functionphosphoric diester hydrolase activity
B0016042biological_processlipid catabolic process
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Functional Information from PDB Data

site_idNumber of ResiduesDetails
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Functional Information from PDB atom coordinates for the "HETATM" binding sites

site_idNumber of ResiduesDetails
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Functional Information from PROSITE/UniProt

site_idNumber of ResiduesDetails
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Functional Information from SwissProt/UniProt

site_idNumber of ResiduesDetails
SWS_FT_FI11Proton donor. {ECO:0000255|PROSITE- ProRule:PRU00270}.
ChainResidueDetails
AHIS82

SWS_FT_FI21Proton acceptor. {ECO:0000255|PROSITE- ProRule:PRU00270}.
ChainResidueDetails
AHIS32

SWS_FT_FI31Proton donor. {ECO:0000255|PROSITE- ProRule:PRU00270}.
ChainResidueDetails
BHIS82

SWS_FT_FI41Proton acceptor. {ECO:0000255|PROSITE- ProRule:PRU00270}.
ChainResidueDetails
BHIS32

CSA15Annotated By Reference To The Literature 2plc
ChainResidueDetails
AASP274
AHIS32
AASP33
AARG69
AHIS82

CSA25Annotated By Reference To The Literature 2plc
ChainResidueDetails
BASP274
BHIS32
BASP33
BARG69
BHIS82

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Catalytic Information from CSA

site_idNumber of ResiduesDetails
CSA15Annotated By Reference To The Literature 2plc
ChainResidueDetails
AASP274
AHIS32
AASP33
AARG69
AHIS82

CSA25Annotated By Reference To The Literature 2plc
ChainResidueDetails
BASP274
BHIS32
BASP33
BARG69
BHIS82