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4I90

Structure of the N254Y/H258Y mutant of the phosphatidylinositol-specific phospholipase C from S. aureus bound to choline

Functional Information from GO Data
ChainGOidnamespacecontents
A0006629biological_processlipid metabolic process
A0008081molecular_functionphosphoric diester hydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACT A 500
ChainResidue
ALYS113
AARG166
ATRP185
AHOH647
AHOH679
AHOH771

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACT A 501
ChainResidue
ALYS42
AHIS86
ALEU37
ALYS38
AASP39

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CHT A 502
ChainResidue
ATYR211
ATYR212
ATYR254
ATYR258

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CHT A 503
ChainResidue
ASER257
ATYR258
ATRP287
ATYR290
AHOH678

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 504
ChainResidue
ALYS114
ATHR125
APHE126

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00270
ChainResidueDetails
AHIS30

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU00270
ChainResidueDetails
AHIS80

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PDB entries from 2024-07-24

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