4YU7

Crystal structure of Piratoxin I (PrTX-I) complexed to caffeic acid

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004623	molecular_function	phospholipase A2 activity
A	0005509	molecular_function	calcium ion binding
A	0005543	molecular_function	phospholipid binding
A	0005576	cellular_component	extracellular region
A	0006644	biological_process	phospholipid metabolic process
A	0016042	biological_process	lipid catabolic process
A	0035821	biological_process	modulation of process of another organism
A	0042130	biological_process	negative regulation of T cell proliferation
A	0047498	molecular_function	calcium-dependent phospholipase A2 activity
A	0050482	biological_process	arachidonic acid secretion
A	0090729	molecular_function	toxin activity
B	0004623	molecular_function	phospholipase A2 activity
B	0005509	molecular_function	calcium ion binding
B	0005543	molecular_function	phospholipid binding
B	0005576	cellular_component	extracellular region
B	0006644	biological_process	phospholipid metabolic process
B	0016042	biological_process	lipid catabolic process
B	0035821	biological_process	modulation of process of another organism
B	0042130	biological_process	negative regulation of T cell proliferation
B	0047498	molecular_function	calcium-dependent phospholipase A2 activity
B	0050482	biological_process	arachidonic acid secretion
B	0090729	molecular_function	toxin activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	binding site for residue PE4 B 201

Chain	Residue
A	PRO113
B	GLY6
B	PRO17
B	TYR21

---

site_id	AC2
Number of Residues	6
Details	binding site for residue PE4 B 202

Chain	Residue
B	TRP68
B	PHE3
B	LYS7
B	LEU10
B	GLN11
B	TYR66

---

site_id	AC3
Number of Residues	7
Details	binding site for residue DHC B 203

Chain	Residue
A	LEU111
B	LYS15
B	ASN16
B	PRO80
B	HOH307
B	HOH314
B	HOH357

---

site_id	AC4
Number of Residues	5
Details	binding site for residue DHC B 204

Chain	Residue
B	LYS19
B	THR55
B	LYS105
B	ARG108
B	HOH307

---

site_id	AC5
Number of Residues	5
Details	binding site for residue PE4 A 201

Chain	Residue
A	LEU2
A	GLY6
A	PRO17
A	TYR21
A	HOH307

---

site_id	AC6
Number of Residues	6
Details	binding site for residue SO4 A 202

Chain	Residue
A	GLY32
A	ARG33
A	LYS52
A	HOH343
A	HOH346
A	HOH364

---

site_id	AC7
Number of Residues	10
Details	binding site for residue DHC A 203

Chain	Residue
A	THR72
A	ILE94
A	ARG97
A	GLU98
A	HOH303
A	HOH309
A	HOH359
B	LYS35
B	PRO36
B	ARG42

---

site_id	AC8
Number of Residues	8
Details	binding site for residue DHC A 204

Chain	Residue
A	LYS15
A	LYS19
A	LYS105
A	ARG108
A	HOH301
A	HOH370
B	THR55
B	GLY56

---

Functional Information from PROSITE/UniProt

site_id	PS00118
Number of Residues	8
Details	PA2_HIS Phospholipase A2 histidine active site. CCYvHKcC

Chain	Residue	Details
B	CYS43-CYS50

---

site_id	PS00119
Number of Residues	11
Details	PA2_ASP Phospholipase A2 aspartic acid active site. LCECDKAVaIC

Chain	Residue	Details
B	LEU85-CYS95

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	SITE: Important residue of the cationic membrane-docking site (MDoS) => ECO:0000250|UniProtKB:I6L8L6

Chain	Residue	Details
B	LYS105
B	ARG108
A	LYS105
A	ARG108

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	SITE: Hydrophobic membrane-disruption site (MDiS) => ECO:0000250|UniProtKB:I6L8L6

Chain	Residue	Details
B	LEU111
B	PHE114
A	LEU111
A	PHE114

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	SITE: Cationic membrane-docking site (MDoS) => ECO:0000250|UniProtKB:I6L8L6

Chain	Residue	Details
B	LYS112
B	LYS117
A	LYS112
A	LYS117

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