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4I9T

Structure of the H258Y mutant of the phosphatidylinositol-specific phospholipase C from Staphylococcus 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 Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 501
ChainResidue
ALEU37
ALYS38
AASP39
ALYS42
AHIS86

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE INS A 502
ChainResidue
AASP206
ATYR208
AHOH603
AHOH604
AHOH655
AHOH722
AHIS30
AARG67
ALYS113
AARG166

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE INS A 503
ChainResidue
AASP50
ALYS51
AGLY284
ATYR285
ATHR286
AHOH697
AHOH756

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PGE A 504
ChainResidue
ATYR253
ASER257
ATYR258
ATRP287
ATYR290

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PGE A 505
ChainResidue
ALYS47
AASP50
ATYR282
ATYR285

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

219140

PDB entries from 2024-05-01

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