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3EA2

Crystal Structure of the Myo-inositol bound Y247S/Y251S Mutant of Phosphatidylinositol-Specific Phospholipase C from Bacillus Thuringiensis

Functional Information from GO Data
ChainGOidnamespacecontents
A0004436molecular_functionphosphatidylinositol diacylglycerol-lyase activity
A0005576cellular_componentextracellular region
A0006629biological_processlipid metabolic process
A0008081molecular_functionphosphoric diester hydrolase activity
A0016042biological_processlipid catabolic process
A0016829molecular_functionlyase activity
B0004436molecular_functionphosphatidylinositol diacylglycerol-lyase activity
B0005576cellular_componentextracellular region
B0006629biological_processlipid metabolic process
B0008081molecular_functionphosphoric diester hydrolase activity
B0016042biological_processlipid catabolic process
B0016829molecular_functionlyase activity
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE INS A 801
ChainResidue
AHIS32
AHOH975
AHOH1015
AHOH1041
AARG69
ALYS115
AARG163
AASP198
ATYR200
AHOH912
AHOH916
AHOH943

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN A 901
ChainResidue
AASP224
AHIS227
AHOH915
AHOH920
AHOH1045
AHOH1070

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN A 902
ChainResidue
AHIS61
AGLU278
BASP75

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 903
ChainResidue
AGLU93
AHOH1061
AHOH1083
BHOH1091

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 905
ChainResidue
AASP74
AASP75
AHOH1011
AHOH1057
BASP54

site_idAC6
Number of Residues13
DetailsBINDING SITE FOR RESIDUE INS B 802
ChainResidue
BHIS32
BARG69
BLYS115
BARG163
BASP198
BTYR200
BHOH923
BHOH928
BHOH930
BHOH983
BHOH1093
BHOH1100
BHOH1116

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN B 904
ChainResidue
BTYR57
BHIS61
BGLU278

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN B 906
ChainResidue
BASP224
BHIS227
BHOH921
BHOH952
BHOH1042
BHOH1067

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00270
ChainResidueDetails
AHIS32
BHIS32

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU00270
ChainResidueDetails
AHIS82
BHIS82

Catalytic Information from CSA
site_idCSA1
Number of Residues5
DetailsAnnotated By Reference To The Literature 2plc
ChainResidueDetails
AASP274
AHIS32
AASP33
AARG69
AHIS82

site_idCSA2
Number of Residues5
DetailsAnnotated By Reference To The Literature 2plc
ChainResidueDetails
BASP274
BHIS32
BASP33
BARG69
BHIS82

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PDB entries from 2024-07-24

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