3QNL

Crystal structure of PrTX-I complexed to Rosmarinic 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	5
Details	BINDING SITE FOR RESIDUE IPA A 201

Chain	Residue
A	TYR22
A	CYS29
A	GLY30
A	IPA202
A	HOH381

---

site_id	AC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE IPA A 202

Chain	Residue
A	IPA201
A	HOH410

---

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE IPA A 203

Chain	Residue
A	HOH411
A	LYS115
A	ARG118

---

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE IPA A 204

Chain	Residue
A	ASN87
A	ASN88
A	GLU108
A	HOH394
B	IPA203

---

site_id	AC5
Number of Residues	14
Details	BINDING SITE FOR RESIDUE ROA A 205

Chain	Residue
A	PHE3
A	LYS7
A	LEU10
A	GLN11
A	GLY15
A	HOH395
A	HOH399
A	HOH426
A	HOH427
B	LYS7
B	LEU10
B	GLN11
B	TRP77
B	P33205

---

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE IPA B 201

Chain	Residue
B	CYS29
B	GLY30
B	P33205
B	HOH386

---

site_id	AC7
Number of Residues	1
Details	BINDING SITE FOR RESIDUE IPA B 202

Chain	Residue
B	ARG72

---

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE IPA B 203

Chain	Residue
A	IPA204
A	HOH379
B	LYS53
B	LYS57
B	HOH361
B	HOH381

---

site_id	AC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE IPA B 204

Chain	Residue
B	LYS36
B	PRO37
B	LYS38

---

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE P33 B 205

Chain	Residue
A	LEU10
A	PRO123
A	ROA205
B	LEU2
B	LEU121
B	IPA201

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	CYS44-CYS51

---

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

Chain	Residue	Details
A	LEU95-CYS105

---

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
A	LYS115
A	ARG118
B	LYS115
B	ARG118

---

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

Chain	Residue	Details
A	LEU121
A	PHE125
B	LEU121
B	PHE125

---

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

Chain	Residue	Details
A	LYS122
A	LYS129
B	LYS122
B	LYS129

---