1PP2

THE REFINED CRYSTAL STRUCTURE OF DIMERIC PHOSPHOLIPASE A2 AT 2.5 ANGSTROMS. ACCESS TO A SHIELDED CATALYTIC CENTER

Functional Information from GO Data

Chain	GOid	namespace	contents
L	0004623	molecular_function	phospholipase A2 activity
L	0005509	molecular_function	calcium ion binding
L	0005543	molecular_function	phospholipid binding
L	0005576	cellular_component	extracellular region
L	0006629	biological_process	lipid metabolic process
L	0006644	biological_process	phospholipid metabolic process
L	0016042	biological_process	lipid catabolic process
L	0016787	molecular_function	hydrolase activity
L	0035821	biological_process	modulation of process of another organism
L	0042130	biological_process	negative regulation of T cell proliferation
L	0046872	molecular_function	metal ion binding
L	0047498	molecular_function	calcium-dependent phospholipase A2 activity
L	0050482	biological_process	arachidonate secretion
L	0090729	molecular_function	toxin activity
R	0004623	molecular_function	phospholipase A2 activity
R	0005509	molecular_function	calcium ion binding
R	0005543	molecular_function	phospholipid binding
R	0005576	cellular_component	extracellular region
R	0006629	biological_process	lipid metabolic process
R	0006644	biological_process	phospholipid metabolic process
R	0016042	biological_process	lipid catabolic process
R	0016787	molecular_function	hydrolase activity
R	0035821	biological_process	modulation of process of another organism
R	0042130	biological_process	negative regulation of T cell proliferation
R	0046872	molecular_function	metal ion binding
R	0047498	molecular_function	calcium-dependent phospholipase A2 activity
R	0050482	biological_process	arachidonate secretion
R	0090729	molecular_function	toxin activity

Functional Information from PDB Data

site_id	ANL
Number of Residues	4
Details	RESIDUES FORMING THE ACTIVATION NETWORK

Chain	Residue
L	SER1
L	GLN4
L	VAL71
L	TYR73

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site_id	ANR
Number of Residues	4
Details	RESIDUES FORMING THE ACTIVATION NETWORK

Chain	Residue
R	SER1
R	GLN4
R	VAL71
R	TYR73

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site_id	CAL
Number of Residues	4
Details	RESIDUES FORMING THE CA2+ BINDING SITE DEDUCED FROM BOVINE STRUCTURE

Chain	Residue
L	TYR28
L	GLY30
L	GLY32
L	ASP49

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site_id	CAR
Number of Residues	4
Details	RESIDUES FORMING THE CA2+ BINDING SITE DEDUCED FROM BOVINE STRUCTURE

Chain	Residue
R	GLY30
R	GLY32
R	ASP49
R	TYR28

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site_id	CNL
Number of Residues	4
Details	RESIDUES FORMING THE CATALYTIC NETWORK

Chain	Residue
L	HIS48
L	TYR52
L	TYR73
L	ASP99

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site_id	CNR
Number of Residues	4
Details	RESIDUES FORMING THE CATALYTIC NETWORK

Chain	Residue
R	HIS48
R	TYR52
R	TYR73
R	ASP99

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Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
R	CYS44-CYS51

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

Chain	Residue	Details
R	ILE95-CYS105

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"evidences":[{"source":"PubMed","id":"4019493","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"O42191","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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Catalytic Information from CSA

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

Chain	Residue	Details
R	HIS48
R	GLY30
R	ASP99

---

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

Chain	Residue	Details
L	HIS48
L	GLY30
L	ASP99

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