3CBI

Crystal structure of the ternary complex of phospholipase A2 with ajmaline and anisic acid at 3.1 A resolution

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	0006629	biological_process	lipid metabolic process
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	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	0006629	biological_process	lipid metabolic process
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	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	0006629	biological_process	lipid metabolic process
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	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	0006629	biological_process	lipid metabolic process
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	0050482	biological_process	arachidonate secretion
D	0090729	molecular_function	toxin activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE AJM C 201

Chain	Residue
C	TRP31
C	GLY32
C	GLY33
C	ASP49

---

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE AJM B 202

Chain	Residue
B	GLY30
B	TRP31
B	ASP49

---

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE AJM A 203

Chain	Residue
A	GLY33
A	ASP49
A	TRP31
A	GLY32

---

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE AJM D 204

Chain	Residue
D	TRP31
D	GLY33
D	ASP49

---

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ANN C 347

Chain	Residue
C	PHE5
C	ILE19
C	TYR22
C	SER23
C	GLY30
C	LYS69

---

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ANN B 348

Chain	Residue
B	LEU2
B	SER23
B	LYS69
C	LYS116

---

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ANN A 349

Chain	Residue
A	PHE5
A	TYR22
A	GLY30
A	CYS45
A	HIS48
A	LYS69

---

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ANN D 350

Chain	Residue
B	GLU11
D	PHE5
D	TYR22
D	SER23
D	GLY30
D	LYS69

---

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. ICECDKAAaIC

Chain	Residue	Details
A	ILE95-CYS105

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	Active site: {"evidences":[{"source":"UniProtKB","id":"P14418","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAY-2004","submissionDatabase":"PDB data bank","title":"Crystal structure of a complex formed between group II phospholipase A2 and aspirin at 1.86 A resolution.","authors":["Singh N.","Jabeen T.","Sharma S.","Bhushan A.","Singh T.P."]}},{"source":"PDB","id":"1TGM","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

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

---