Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1HN4

PROPHOSPHOLIPASE A2 DIMER COMPLEXED WITH MJ33, SULFATE, AND CALCIUM

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0002446	biological_process	neutrophil mediated immunity
A	0004623	molecular_function	phospholipase A2 activity
A	0005102	molecular_function	signaling receptor binding
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	0006633	biological_process	fatty acid biosynthetic process
A	0006644	biological_process	phospholipid metabolic process
A	0008284	biological_process	positive regulation of cell population proliferation
A	0009986	cellular_component	cell surface
A	0010524	biological_process	positive regulation of calcium ion transport into cytosol
A	0016042	biological_process	lipid catabolic process
A	0016787	molecular_function	hydrolase activity
A	0019370	biological_process	leukotriene biosynthetic process
A	0030593	biological_process	neutrophil chemotaxis
A	0032052	molecular_function	bile acid binding
A	0032652	biological_process	regulation of interleukin-1 production
A	0032757	biological_process	positive regulation of interleukin-8 production
A	0032869	biological_process	cellular response to insulin stimulus
A	0035556	biological_process	intracellular signal transduction
A	0043406	biological_process	positive regulation of MAP kinase activity
A	0045944	biological_process	positive regulation of transcription by RNA polymerase II
A	0046324	biological_process	regulation of glucose import
A	0046470	biological_process	phosphatidylcholine metabolic process
A	0046471	biological_process	phosphatidylglycerol metabolic process
A	0046872	molecular_function	metal ion binding
A	0047498	molecular_function	calcium-dependent phospholipase A2 activity
A	0048146	biological_process	positive regulation of fibroblast proliferation
A	0050482	biological_process	arachidonic acid secretion
A	0050778	biological_process	positive regulation of immune response
A	0051092	biological_process	positive regulation of NF-kappaB transcription factor activity
A	1904635	biological_process	positive regulation of podocyte apoptotic process
B	0002446	biological_process	neutrophil mediated immunity
B	0004623	molecular_function	phospholipase A2 activity
B	0005102	molecular_function	signaling receptor binding
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	0006633	biological_process	fatty acid biosynthetic process
B	0006644	biological_process	phospholipid metabolic process
B	0008284	biological_process	positive regulation of cell population proliferation
B	0009986	cellular_component	cell surface
B	0010524	biological_process	positive regulation of calcium ion transport into cytosol
B	0016042	biological_process	lipid catabolic process
B	0016787	molecular_function	hydrolase activity
B	0019370	biological_process	leukotriene biosynthetic process
B	0030593	biological_process	neutrophil chemotaxis
B	0032052	molecular_function	bile acid binding
B	0032652	biological_process	regulation of interleukin-1 production
B	0032757	biological_process	positive regulation of interleukin-8 production
B	0032869	biological_process	cellular response to insulin stimulus
B	0035556	biological_process	intracellular signal transduction
B	0043406	biological_process	positive regulation of MAP kinase activity
B	0045944	biological_process	positive regulation of transcription by RNA polymerase II
B	0046324	biological_process	regulation of glucose import
B	0046470	biological_process	phosphatidylcholine metabolic process
B	0046471	biological_process	phosphatidylglycerol metabolic process
B	0046872	molecular_function	metal ion binding
B	0047498	molecular_function	calcium-dependent phospholipase A2 activity
B	0048146	biological_process	positive regulation of fibroblast proliferation
B	0050482	biological_process	arachidonic acid secretion
B	0050778	biological_process	positive regulation of immune response
B	0051092	biological_process	positive regulation of NF-kappaB transcription factor activity
B	1904635	biological_process	positive regulation of podocyte apoptotic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 290

Chain	Residue
A	TYR28
A	GLY30
A	GLY32
A	ASP49
A	MJI397
A	HOH408

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA B 291

Chain	Residue
B	ASP49
B	HOH525
B	TYR28
B	GLY30
B	GLY32

site_id	AC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SO4 A 392

Chain	Residue
A	ARG6
A	HIS17
A	PRO18
A	LEU19
A	MET20
A	HOH399
A	HOH430
B	SER-3
B	SER-2

site_id	AC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SO4 B 393

Chain	Residue
A	SER-2
A	SER-3
B	ARG6
B	HIS17
B	LEU19
B	MET20
B	HOH405
B	HOH409

site_id	AC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 B 394

Chain	Residue
A	ARG6
A	LYS10
A	HOH430
A	HOH451
B	ARG-1
B	HOH403
B	HOH445

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 B 395

Chain	Residue
A	HOH558
B	ARG6
B	LYS10
B	HOH440
B	HOH483

site_id	AC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 A 396

Chain	Residue
A	ASN85
A	LYS87

site_id	AC8
Number of Residues	14
Details	BINDING SITE FOR RESIDUE MJI A 397

Chain	Residue
A	SER-2
A	LEU2
A	PHE5
A	PHE22
A	TYR28
A	CYS29
A	GLY30
A	CYS45
A	HIS48
A	ASP49
A	TYR52
A	PHE106
A	CA290
B	SER-2

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	CYS44-CYS51

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

Chain	Residue	Details
A	ILE95-CYS105

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: ACT_SITE => ECO:0000269\|PubMed:6876174

Chain	Residue	Details
A	HIS48
A	ASP99
B	HIS48
B	ASP99

site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:P00593

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

site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: Pyrrolidone carboxylic acid => ECO:0000269\|PubMed:5528841

Chain	Residue	Details
A	GLN-7
B	GLN-7

site_id	SWS_FT_FI4
Number of Residues	2
Details	LIPID: N6-palmitoyl lysine => ECO:0000269\|PubMed:2498336

Chain	Residue	Details
A	LYS56
B	LYS56

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	MCSA1
Number of Residues	8
Details	M-CSA 83

Chain	Residue	Details
A	TYR28	metal ligand
A	GLY30	metal ligand
A	GLY32	metal ligand
A	HIS48	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	ASP49	metal ligand
A	TYR52	electrostatic stabiliser, hydrogen bond donor
A	TYR73	electrostatic stabiliser, hydrogen bond donor
A	ASP99	electrostatic stabiliser, hydrogen bond acceptor

site_id	MCSA2
Number of Residues	8
Details	M-CSA 83

Chain	Residue	Details
B	TYR28	metal ligand
B	GLY30	metal ligand
B	GLY32	metal ligand
B	HIS48	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	ASP49	metal ligand
B	TYR52	electrostatic stabiliser, hydrogen bond donor
B	TYR73	electrostatic stabiliser, hydrogen bond donor
B	ASP99	electrostatic stabiliser, hydrogen bond acceptor

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)