Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1CJY

HUMAN CYTOSOLIC PHOSPHOLIPASE A2

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000139	cellular_component	Golgi membrane
A	0001516	biological_process	prostaglandin biosynthetic process
A	0002827	biological_process	positive regulation of T-helper 1 type immune response
A	0004620	molecular_function	phospholipase activity
A	0004622	molecular_function	phosphatidylcholine lysophospholipase activity
A	0004623	molecular_function	phospholipase A2 activity
A	0005509	molecular_function	calcium ion binding
A	0005544	molecular_function	calcium-dependent phospholipid binding
A	0005634	cellular_component	nucleus
A	0005635	cellular_component	nuclear envelope
A	0005737	cellular_component	cytoplasm
A	0005743	cellular_component	mitochondrial inner membrane
A	0005783	cellular_component	endoplasmic reticulum
A	0005789	cellular_component	endoplasmic reticulum membrane
A	0005794	cellular_component	Golgi apparatus
A	0005829	cellular_component	cytosol
A	0006071	biological_process	glycerol metabolic process
A	0006629	biological_process	lipid metabolic process
A	0006631	biological_process	fatty acid metabolic process
A	0006633	biological_process	fatty acid biosynthetic process
A	0006640	biological_process	monoacylglycerol biosynthetic process
A	0006650	biological_process	glycerophospholipid metabolic process
A	0006663	biological_process	platelet activating factor biosynthetic process
A	0006690	biological_process	icosanoid metabolic process
A	0006693	biological_process	prostaglandin metabolic process
A	0008289	molecular_function	lipid binding
A	0008374	molecular_function	O-acyltransferase activity
A	0009395	biological_process	phospholipid catabolic process
A	0010314	molecular_function	phosphatidylinositol-5-phosphate binding
A	0010572	biological_process	positive regulation of platelet activation
A	0016042	biological_process	lipid catabolic process
A	0016787	molecular_function	hydrolase activity
A	0019369	biological_process	arachidonate metabolic process
A	0019370	biological_process	leukotriene biosynthetic process
A	0032266	molecular_function	phosphatidylinositol-3-phosphate binding
A	0034478	biological_process	phosphatidylglycerol catabolic process
A	0034638	biological_process	phosphatidylcholine catabolic process
A	0036151	biological_process	phosphatidylcholine acyl-chain remodeling
A	0043032	biological_process	positive regulation of macrophage activation
A	0046475	biological_process	glycerophospholipid catabolic process
A	0046872	molecular_function	metal ion binding
A	0047498	molecular_function	calcium-dependent phospholipase A2 activity
A	0047499	molecular_function	calcium-independent phospholipase A2 activity
A	0050482	biological_process	arachidonate secretion
A	0052689	molecular_function	carboxylic ester hydrolase activity
A	0070273	molecular_function	phosphatidylinositol-4-phosphate binding
A	1902387	molecular_function	ceramide 1-phosphate binding
B	0000139	cellular_component	Golgi membrane
B	0001516	biological_process	prostaglandin biosynthetic process
B	0002827	biological_process	positive regulation of T-helper 1 type immune response
B	0004620	molecular_function	phospholipase activity
B	0004622	molecular_function	phosphatidylcholine lysophospholipase activity
B	0004623	molecular_function	phospholipase A2 activity
B	0005509	molecular_function	calcium ion binding
B	0005544	molecular_function	calcium-dependent phospholipid binding
B	0005634	cellular_component	nucleus
B	0005635	cellular_component	nuclear envelope
B	0005737	cellular_component	cytoplasm
B	0005743	cellular_component	mitochondrial inner membrane
B	0005783	cellular_component	endoplasmic reticulum
B	0005789	cellular_component	endoplasmic reticulum membrane
B	0005794	cellular_component	Golgi apparatus
B	0005829	cellular_component	cytosol
B	0006071	biological_process	glycerol metabolic process
B	0006629	biological_process	lipid metabolic process
B	0006631	biological_process	fatty acid metabolic process
B	0006633	biological_process	fatty acid biosynthetic process
B	0006640	biological_process	monoacylglycerol biosynthetic process
B	0006650	biological_process	glycerophospholipid metabolic process
B	0006663	biological_process	platelet activating factor biosynthetic process
B	0006690	biological_process	icosanoid metabolic process
B	0006693	biological_process	prostaglandin metabolic process
B	0008289	molecular_function	lipid binding
B	0008374	molecular_function	O-acyltransferase activity
B	0009395	biological_process	phospholipid catabolic process
B	0010314	molecular_function	phosphatidylinositol-5-phosphate binding
B	0010572	biological_process	positive regulation of platelet activation
B	0016042	biological_process	lipid catabolic process
B	0016787	molecular_function	hydrolase activity
B	0019369	biological_process	arachidonate metabolic process
B	0019370	biological_process	leukotriene biosynthetic process
B	0032266	molecular_function	phosphatidylinositol-3-phosphate binding
B	0034478	biological_process	phosphatidylglycerol catabolic process
B	0034638	biological_process	phosphatidylcholine catabolic process
B	0036151	biological_process	phosphatidylcholine acyl-chain remodeling
B	0043032	biological_process	positive regulation of macrophage activation
B	0046475	biological_process	glycerophospholipid catabolic process
B	0046872	molecular_function	metal ion binding
B	0047498	molecular_function	calcium-dependent phospholipase A2 activity
B	0047499	molecular_function	calcium-independent phospholipase A2 activity
B	0050482	biological_process	arachidonate secretion
B	0052689	molecular_function	carboxylic ester hydrolase activity
B	0070273	molecular_function	phosphatidylinositol-4-phosphate binding
B	1902387	molecular_function	ceramide 1-phosphate binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 950

Chain	Residue
A	ASP40
A	THR41
A	ASP43
A	ASN65
A	MES3000
A	HOH3026

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA A 951

Chain	Residue
A	ALA94
A	ASN95
A	ASP40
A	ASP43
A	ASP93

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA B 1950

Chain	Residue
B	HOH53
B	ASP1040
B	THR1041
B	ASP1043
B	ASN1065
B	MES4000

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA B 1951

Chain	Residue
B	HOH54
B	ASP1040
B	ASP1043
B	ASP1093
B	ALA1094
B	ASN1095

site_id	AC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE MES A 3000

Chain	Residue
A	ASP40
A	ASP43
A	ASN64
A	ASN65
A	ALA94
A	TYR96
A	CA950
A	HOH3026
B	LYS1281

site_id	AC6
Number of Residues	11
Details	BINDING SITE FOR RESIDUE MES B 4000

Chain	Residue
A	LYS281
B	HOH53
B	ASP1040
B	ASP1043
B	HIS1062
B	ASN1064
B	ASN1065
B	ALA1094
B	ASN1095
B	TYR1096
B	CA1950

Functional Information from PROSITE/UniProt

site_id	PS00136
Number of Residues	11
Details	SUBTILASE_ASP Serine proteases, subtilase family, aspartic acid active site. IHVVDSGLtf.N

Chain	Residue	Details
A	ILE545-ASN555

site_id	PS00387
Number of Residues	7
Details	PPASE Inorganic pyrophosphatase signature. DDDELDA

Chain	Residue	Details
A	ASP517-ALA523

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"10319815","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8083230","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8619991","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8702602","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	2
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"10319815","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8702602","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	14
Details	Binding site: {}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	6
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	a catalytic site defined by CSA, PubMed 10319815, 8619991, 8702602, 11080675

Chain	Residue	Details
A	SER228
A	GLY198
A	GLY197
A	ASP549

site_id	CSA2
Number of Residues	4
Details	a catalytic site defined by CSA, PubMed 10319815, 8619991, 8702602, 11080675

Chain	Residue	Details
B	GLY1197
B	GLY1198
B	SER1228
B	ASP1549

site_id	MCSA1
Number of Residues	5
Details	M-CSA 529

Chain	Residue	Details
A	GLY197	electrostatic stabiliser
A	GLY198	electrostatic stabiliser
A	ARG200	electrostatic stabiliser
A	SER228	covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor
A	ASP549	proton acceptor, proton donor

site_id	MCSA2
Number of Residues	5
Details	M-CSA 529

Chain	Residue	Details
B	GLY1197	electrostatic stabiliser
B	GLY1198	electrostatic stabiliser
B	ARG1200	electrostatic stabiliser
B	SER1228	covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor
B	ASP1549	proton acceptor, proton donor

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