4I9T

Structure of the H258Y mutant of the phosphatidylinositol-specific phospholipase C from Staphylococcus aureus

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0006629	biological_process	lipid metabolic process
A	0008081	molecular_function	phosphoric diester hydrolase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 501

Chain	Residue
A	LEU37
A	LYS38
A	ASP39
A	LYS42
A	HIS86

---

site_id	AC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE INS A 502

Chain	Residue
A	ASP206
A	TYR208
A	HOH603
A	HOH604
A	HOH655
A	HOH722
A	HIS30
A	ARG67
A	LYS113
A	ARG166

---

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE INS A 503

Chain	Residue
A	ASP50
A	LYS51
A	GLY284
A	TYR285
A	THR286
A	HOH697
A	HOH756

---

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PGE A 504

Chain	Residue
A	TYR253
A	SER257
A	TYR258
A	TRP287
A	TYR290

---

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PGE A 505

Chain	Residue
A	LYS47
A	ASP50
A	TYR282
A	TYR285

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	149
Details	Domain: {"description":"PI-PLC X-box","evidences":[{"source":"PROSITE-ProRule","id":"PRU00270","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00270","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	Active site: {"description":"Proton donor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00270","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---