Structure of PDB 5wzo Chain A

Receptor sequence

>5wzoA (length=123) Species: 9606 (Homo sapiens)

NLVQFGVMIEKMTGKSALQYNDYGCYCGIGGSHWPVDQTDWCCHAHDCCY
GRLEKLGCEPKLEKYLFSVSERGIFCAGRTTCQRLTCECDKRAALCFRRN
LGTYNRKYAHYPNKLCTGPTPPC

3D structure

• PDB: 5wzo Structural basis for functional selectivity and ligand recognition revealed by crystal structures of human secreted phospholipase A2 group IIE
• Chain: A
• Resolution: 1.9 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): Y26 G28 G30 H46 D47 Y50 Y65 D90
• Catalytic site (residue number reindexed from 1): Y26 G28 G30 H46 D47 Y50 Y65 D90
• Enzyme Commision number: 3.1.1.4: phospholipase A2.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	CA	A	Y26 G28 G30 D47	Y26 G28 G30 D47
BS02	CA	A	D22 Y23 G24 Y111	D22 Y23 G24 Y111

Gene Ontology

Molecular Function

• GO:0004623 phospholipase A2 activity
• GO:0005509 calcium ion binding
• GO:0005515 protein binding
• GO:0005543 phospholipid binding
• GO:0016787 hydrolase activity
• GO:0046872 metal ion binding
• GO:0047498 calcium-dependent phospholipase A2 activity

Biological Process

• GO:0006629 lipid metabolic process
• GO:0006644 phospholipid metabolic process
• GO:0006954 inflammatory response
• GO:0016042 lipid catabolic process
• GO:0034374 low-density lipoprotein particle remodeling
• GO:0042130 negative regulation of T cell proliferation
• GO:0046470 phosphatidylcholine metabolic process
• GO:0046471 phosphatidylglycerol metabolic process
• GO:0050482 arachidonate secretion

Cellular Component

• GO:0005576 extracellular region
• GO:0005737 cytoplasm

External links

• PDB: RCSB:5wzo, PDBe:5wzo, PDBj:5wzo
• PDBsum: 5wzo
• PubMed: 28883454
• UniProt: Q9NZK7|PA2GE_HUMAN Group IIE secretory phospholipase A2 (Gene Name=PLA2G2E)