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4F2U

Structure of the N254Y/H258Y double mutant of the Phosphatidylinositol-Specific Phospholipase C from S.aureus

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 EPE A 401
ChainResidue
ATYR211
ATYR212
ASER247
AASN250
ATYR254
AHOH782

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EPE A 402
ChainResidue
ATRP287
ATYR290
AHOH610
AHOH717
AHOH726
ATYR253
ASER257
ATYR258

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 403
ChainResidue
ALEU37
ALYS38
AASP39
ALYS42
AHIS86
AHOH707

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues149
DetailsDomain: {"description":"PI-PLC X-box","evidences":[{"source":"PROSITE-ProRule","id":"PRU00270","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00270","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00270","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

245663

PDB entries from 2025-12-03

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