Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1BJJ

AGKISTRODOTOXIN, A PHOSPHOLIPASE A2-TYPE PRESYNAPTIC NEUROTOXIN FROM AGKISTRODON HALYS PALLAS

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	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	arachidonate 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	0016787	molecular_function	hydrolase activity
B	0035821	biological_process	modulation of process of another organism
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	arachidonate secretion
B	0090729	molecular_function	toxin activity
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	0016787	molecular_function	hydrolase activity
C	0035821	biological_process	modulation of process of another organism
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	arachidonate secretion
C	0090729	molecular_function	toxin activity
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	0016787	molecular_function	hydrolase activity
D	0035821	biological_process	modulation of process of another organism
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	arachidonate secretion
D	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	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	arachidonate secretion
E	0090729	molecular_function	toxin activity
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	0016787	molecular_function	hydrolase activity
F	0035821	biological_process	modulation of process of another organism
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	arachidonate secretion
F	0090729	molecular_function	toxin activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 134

Chain	Residue
A	ASP71
A	ILE72
A	GLU92
E	ASP71
E	ILE72
E	GLU92

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA F 134

Chain	Residue
F	ASP71
F	ILE72
F	GLU92
B	ASP71
B	ILE72
B	GLU92

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA C 134

Chain	Residue
C	ASP71
C	ILE72
C	GLU92
D	ASP71
D	ILE72
D	GLU92

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA A 11

Chain	Residue
A	TYR28
A	GLY30
A	GLY32
A	ASP49

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA B 134

Chain	Residue
B	TYR28
B	GLY30
B	GLY32
B	ASP49

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA D 134

Chain	Residue
D	TYR28
D	GLY30
D	GLY32
D	GLY33
D	ASP49

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA E 134

Chain	Residue
E	TYR28
E	GLY30
E	GLY32
E	ASP49

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA F 135

Chain	Residue
F	TYR28
F	GLY30
F	GLY32
F	ASP49

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	CYS44-CYS51

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

Chain	Residue	Details
A	ILE95-CYS105

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	ACT_SITE: ACT_SITE => ECO:0000305\|PubMed:9733637

Chain	Residue	Details
A	HIS48
E	ASP99
F	HIS48
F	ASP99
A	ASP99
B	HIS48
B	ASP99
C	HIS48
C	ASP99
D	HIS48
D	ASP99
E	HIS48

site_id	SWS_FT_FI2
Number of Residues	24
Details	BINDING: BINDING => ECO:0000269\|PubMed:10666574, ECO:0007744\|PDB:1BJJ

Chain	Residue	Details
A	TYR28
C	GLY30
C	GLY32
C	ASP49
D	TYR28
D	GLY30
D	GLY32
D	ASP49
E	TYR28
E	GLY30
E	GLY32
A	GLY30
E	ASP49
F	TYR28
F	GLY30
F	GLY32
F	ASP49
A	GLY32
A	ASP49
B	TYR28
B	GLY30
B	GLY32
B	ASP49
C	TYR28

Catalytic Information from CSA

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

Chain	Residue	Details
A	HIS48
A	GLY30
A	ASP99

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

Chain	Residue	Details
B	HIS48
B	GLY30
B	ASP99

site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1n29

Chain	Residue	Details
C	HIS48
C	GLY30
C	ASP99

site_id	CSA4
Number of Residues	3
Details	Annotated By Reference To The Literature 1n29

Chain	Residue	Details
D	HIS48
D	GLY30
D	ASP99

site_id	CSA5
Number of Residues	3
Details	Annotated By Reference To The Literature 1n29

Chain	Residue	Details
E	HIS48
E	GLY30
E	ASP99

site_id	CSA6
Number of Residues	3
Details	Annotated By Reference To The Literature 1n29

Chain	Residue	Details
F	HIS48
F	GLY30
F	ASP99

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)