4I9J

Structure of the N254Y/H258Y mutant of the phosphatidylinositol-specific phospholipase C from S. aureus bound to diC4PC

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 ACT A 501

Chain	Residue
A	LYS113
A	ARG166
A	TRP185
A	XP5503
A	HOH679

---

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE XP5 A 502

Chain	Residue
A	TRP287
A	TYR290
A	HOH812
A	SER257
A	TYR258
A	GLU262
A	LYS265

---

site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE XP5 A 503

Chain	Residue
A	THR36
A	LEU37
A	LYS38
A	ASP39
A	LYS42
A	HIS86
A	ACT501
A	HOH686

---

site_id	AC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE XP5 A 504

Chain	Residue
A	LEU37
A	LYS38
A	SER43
A	VAL44
A	LYS47
A	SER251
A	TYR282
A	TYR285
A	HOH618
A	HOH774

---

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

---