4HG9

Crystal structure of AhV_bPA, a basic PLA2 from Agkistrodon halys pallas venom

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
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	0046872	molecular_function	metal ion binding
B	0047498	molecular_function	calcium-dependent phospholipase A2 activity
B	0050482	biological_process	arachidonic acid 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	0046872	molecular_function	metal ion binding
C	0047498	molecular_function	calcium-dependent phospholipase A2 activity
C	0050482	biological_process	arachidonic acid 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	0046872	molecular_function	metal ion binding
D	0047498	molecular_function	calcium-dependent phospholipase A2 activity
D	0050482	biological_process	arachidonic acid secretion
D	0090729	molecular_function	toxin activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA A 201

Chain	Residue
A	TYR28
A	GLY30
A	GLY32
A	ASP49

---

site_id	AC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE CIT A 202

Chain	Residue
C	HIS1
C	LEU3
C	LYS7
C	ASP72
A	ARG6
A	LYS7
A	LYS10
A	HOH307
A	HOH360

---

site_id	AC3
Number of Residues	10
Details	BINDING SITE FOR RESIDUE CIT A 203

Chain	Residue
A	HIS1
A	LEU3
A	LYS7
A	ASP72
A	HOH307
A	HOH336
A	HOH378
C	ARG6
C	LYS7
C	LYS10

---

site_id	AC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE G3P A 204

Chain	Residue
A	PHE5
A	GLY30

---

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA B 201

Chain	Residue
B	TYR28
B	GLY30
B	GLY32
B	ASP49

---

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL B 202

Chain	Residue
B	ARG6
B	PRO18
B	TYR22
B	ALA23
B	HOH347

---

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA C 201

Chain	Residue
C	TYR28
C	GLY30
C	GLY32
C	ASP49

---

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE G3P C 202

Chain	Residue
C	LEU2
C	PHE5
C	GLY30
C	HIS48

---

site_id	AC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL C 203

Chain	Residue
C	PRO37
C	ASP39
C	ARG43

---

site_id	BC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL C 204

Chain	Residue
C	ALA101
C	CYS105
C	HOH306
C	HOH332
C	HOH348
C	HOH358
C	HOH364

---

site_id	BC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA D 201

Chain	Residue
D	TYR28
D	GLY30
D	GLY32
D	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. VCECDKAAaIC

Chain	Residue	Details
A	VAL95-CYS105

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	ACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:P06859

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

---

site_id	SWS_FT_FI2
Number of Residues	16
Details	BINDING: BINDING => ECO:0000269|PubMed:9761847, ECO:0007744|PDB:1JIA

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

---