Structure of PDB 5y5e Chain A

Receptor sequence

>5y5eA (length=121) Species: 9606 (Homo sapiens)

VQFGVMIEKMTGKSALQYGDYGCYCGIGGSHWPVDQTDWCCHAHDCCYGR
LEKLGCEPKLEKYLFSVSERGIFCAGRTTCQRLTCECDKRAALCFRRNLG
TYNRKYAHYPNKLCTGPTPPC

3D structure

• PDB: 5y5e Structural basis for functional selectivity and ligand recognition revealed by crystal structures of human secreted phospholipase A2group IIE
• Chain: A
• Resolution: 1.8 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): Y24 G26 G28 H44 D45 Y48 Y63 D88
• 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	7W3	A	F5 G6 A17 G21 Y26 C27 G28 I29 C43 H46 D47	F3 G4 A15 G19 Y24 C25 G26 I27 C41 H44 D45
BS02	CA	A	Y26 G28 G30 D47	Y24 G26 G28 D45

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:5y5e, PDBe:5y5e, PDBj:5y5e
• PDBsum: 5y5e
• PubMed: 28883454
• UniProt: Q9NZK7|PA2GE_HUMAN Group IIE secretory phospholipase A2 (Gene Name=PLA2G2E)