Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3UX7

Crystal structure of a dimeric myotoxic component of the Vipera ammodytes meridionalis venom reveals determinants of myotoxicity and membrane damaging activity

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	0042130	biological_process	negative regulation of T cell proliferation
A	0046872	molecular_function	metal ion binding
A	0047498	molecular_function	calcium-dependent phospholipase A2 activity
A	0050482	biological_process	arachidonic acid secretion
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	0042130	biological_process	negative regulation of T cell proliferation
B	0046872	molecular_function	metal ion binding
B	0047498	molecular_function	calcium-dependent phospholipase A2 activity
B	0050482	biological_process	arachidonic acid secretion
C	0004623	molecular_function	phospholipase A2 activity
C	0005509	molecular_function	calcium ion binding
C	0005543	molecular_function	phospholipid binding
C	0005576	cellular_component	extracellular region
C	0006644	biological_process	phospholipid metabolic process
C	0016042	biological_process	lipid catabolic process
C	0042130	biological_process	negative regulation of T cell proliferation
C	0046872	molecular_function	metal ion binding
C	0047498	molecular_function	calcium-dependent phospholipase A2 activity
C	0050482	biological_process	arachidonic acid secretion
D	0004623	molecular_function	phospholipase A2 activity
D	0005509	molecular_function	calcium ion binding
D	0005543	molecular_function	phospholipid binding
D	0005576	cellular_component	extracellular region
D	0006644	biological_process	phospholipid metabolic process
D	0016042	biological_process	lipid catabolic process
D	0042130	biological_process	negative regulation of T cell proliferation
D	0046872	molecular_function	metal ion binding
D	0047498	molecular_function	calcium-dependent phospholipase A2 activity
D	0050482	biological_process	arachidonic acid secretion
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	0042130	biological_process	negative regulation of T cell proliferation
E	0046872	molecular_function	metal ion binding
E	0047498	molecular_function	calcium-dependent phospholipase A2 activity
E	0050482	biological_process	arachidonic acid secretion
F	0004623	molecular_function	phospholipase A2 activity
F	0005509	molecular_function	calcium ion binding
F	0005543	molecular_function	phospholipid binding
F	0005576	cellular_component	extracellular region
F	0006644	biological_process	phospholipid metabolic process
F	0016042	biological_process	lipid catabolic process
F	0042130	biological_process	negative regulation of T cell proliferation
F	0046872	molecular_function	metal ion binding
F	0047498	molecular_function	calcium-dependent phospholipase A2 activity
F	0050482	biological_process	arachidonic acid secretion
G	0004623	molecular_function	phospholipase A2 activity
G	0005509	molecular_function	calcium ion binding
G	0005543	molecular_function	phospholipid binding
G	0005576	cellular_component	extracellular region
G	0006644	biological_process	phospholipid metabolic process
G	0016042	biological_process	lipid catabolic process
G	0042130	biological_process	negative regulation of T cell proliferation
G	0046872	molecular_function	metal ion binding
G	0047498	molecular_function	calcium-dependent phospholipase A2 activity
G	0050482	biological_process	arachidonic acid secretion
H	0004623	molecular_function	phospholipase A2 activity
H	0005509	molecular_function	calcium ion binding
H	0005543	molecular_function	phospholipid binding
H	0005576	cellular_component	extracellular region
H	0006644	biological_process	phospholipid metabolic process
H	0016042	biological_process	lipid catabolic process
H	0042130	biological_process	negative regulation of T cell proliferation
H	0046872	molecular_function	metal ion binding
H	0047498	molecular_function	calcium-dependent phospholipase A2 activity
H	0050482	biological_process	arachidonic acid secretion

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 123

Chain	Residue
A	ALA39
A	ARG42
E	LYS105
E	LYS108

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 A 124

Chain	Residue
A	TYR21
A	CYS28
A	GLY29

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 A 125

Chain	Residue
A	THR19
A	SER20
A	HOH127
E	ALA91
A	LYS15
A	ASN16

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 A 126

Chain	Residue
A	CYS75
A	GLU87
E	LYS7

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 B 123

Chain	Residue
B	LYS121
B	HOH128
H	ARG112

site_id	AC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 B 124

Chain	Residue
B	ARG42
H	LYS105

site_id	AC7
Number of Residues	1
Details	BINDING SITE FOR RESIDUE SO4 C 123

Chain	Residue
C	LEU18

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 C 124

Chain	Residue
C	LYS35
F	LYS97
G	LYS114

site_id	AC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 D 123

Chain	Residue
D	LYS15
D	ASN16
D	THR19
D	SER20
D	HOH131
F	ALA91

site_id	BC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 D 124

Chain	Residue
D	ALA39
D	ARG42
F	LYS108

site_id	BC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 E 123

Chain	Residue
A	LYS105
A	LYS108
A	HOH134
E	ALA39
E	ARG42
E	HOH134

site_id	BC3
Number of Residues	1
Details	BINDING SITE FOR RESIDUE SO4 F 123

Chain	Residue
F	SER119

site_id	BC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 F 124

Chain	Residue
D	LYS7
D	GLN10
F	CYS75
F	GLU87
F	LYS90

site_id	BC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 F 125

Chain	Residue
D	LYS105
F	ARG42

site_id	BC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 G 123

Chain	Residue
C	LYS108
G	ALA39
G	ARG42

site_id	BC7
Number of Residues	1
Details	BINDING SITE FOR RESIDUE SO4 G 124

Chain	Residue
G	HOH130

site_id	BC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 G 125

Chain	Residue
C	ALA91
G	ASN16
G	THR19
G	SER20

site_id	BC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 H 123

Chain	Residue
H	GLY29
H	LEU30
H	HOH129

site_id	CC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 H 124

Chain	Residue
H	LYS37
H	TYR107
H	TYR110

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	CYS43-CYS50

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

Chain	Residue	Details
A	ILE85-CYS95

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)