2I0U

Crystal structures of phospholipases A2 from Vipera nikolskii venom revealing Triton X-100 bound in hydrophobic channel

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	0016787	molecular_function	hydrolase activity
A	0035821	biological_process	modulation of process of another organism
A	0046872	molecular_function	metal ion binding
A	0047498	molecular_function	calcium-dependent phospholipase A2 activity
A	0050482	biological_process	arachidonic acid secretion
A	0090729	molecular_function	toxin activity
E	0004623	molecular_function	phospholipase A2 activity
E	0005509	molecular_function	calcium ion binding
E	0005543	molecular_function	phospholipid binding
E	0005576	cellular_component	extracellular region
E	0006644	biological_process	phospholipid metabolic process
E	0016042	biological_process	lipid catabolic process
E	0016787	molecular_function	hydrolase activity
E	0035821	biological_process	modulation of process of another organism
E	0046872	molecular_function	metal ion binding
E	0047498	molecular_function	calcium-dependent phospholipase A2 activity
E	0050482	biological_process	arachidonic acid secretion
E	0090729	molecular_function	toxin activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA E 1003

Chain	Residue
A	ASN10
A	PHE17
E	ASN10
E	ALA16
E	PHE17

---

site_id	AC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CA E 1001

Chain	Residue
E	ARG43
E	ARG43

---

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 A 1206

Chain	Residue
A	ASN114
A	ASN116
A	HOH2147
A	HOH2156
A	ARG56
A	GLY59

---

site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 E 1207

Chain	Residue
E	ARG56
E	GLY59
E	ASN114
E	ASN116
E	HOH1226
E	HOH1249
E	HOH1288

---

site_id	AC5
Number of Residues	12
Details	BINDING SITE FOR RESIDUE TRT E 1123

Chain	Residue
A	PHE17
A	TFA1200
E	PHE5
E	VAL19
E	TRP20
E	TYR22
E	TYR28
E	GLY30
E	TRP31
E	HIS48
E	HOH1306
E	HOH1316

---

site_id	AC6
Number of Residues	9
Details	BINDING SITE FOR RESIDUE TRT A 2123

Chain	Residue
A	LEU2
A	PHE5
A	TYR22
A	TYR28
A	GLY30
A	GLY32
A	ASP49
A	TFA1200
E	PHE17

---

site_id	AC7
Number of Residues	9
Details	BINDING SITE FOR RESIDUE TFA A 1200

Chain	Residue
A	PHE17
A	TRP20
A	TRT2123
A	HOH2126
A	HOH2127
A	HOH2175
E	PHE17
E	TRP20
E	TRT1123

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
E	CYS44-CYS51

---

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

Chain	Residue	Details
E	ILE95-CYS105

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: ACT_SITE => ECO:0000250

Chain	Residue	Details
E	HIS48
E	ASP99
A	HIS48
A	ASP99

---

site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
E	TYR28
E	GLY30
E	GLY32
E	ASP49
A	TYR28
A	GLY30
A	GLY32
A	ASP49

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1n29

Chain	Residue	Details
E	HIS48
E	GLY30
E	ASP99

---

site_id	CSA2
Number of Residues	3
Details	Annotated By Reference To The Literature 1n29

Chain	Residue	Details
A	HIS48
A	GLY30
A	ASP99

---