Structure of PDB 4yv5 Chain A

Receptor sequence

>4yv5A (length=122) Species: 98334 (Bothrops moojeni)

SLFELGKMILQETGKNPAKSYGVYGCNCGVGGRGKPKDATDRCCYVHKCC
YKKLTGCDPKKDRYSYSWKDKTIVCGENNSCLKELCECDKAVAICLRENL
DTYNKKYRYNYLKPFCKKADPC

3D structure

• PDB: 4yv5 Structural and functional evidence for membrane docking and disruption sites on phospholipase A2-like proteins revealed by complexation with the inhibitor suramin.
• Chain: A
• Resolution: 1.9 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): N28 G30 G32 H48 K49 Y52 Y73 D99
• Catalytic site (residue number reindexed from 1): N27 G29 G31 H47 K48 Y51 Y64 D89

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	SVR	A	K7 L10 N17	K7 L10 N16	MOAD: Kd=0.6uM PDBbind-CN: -logKd/Ki=6.22,Kd=0.6uM
BS02	SVR	A	N114 K115 K116 Y119 Y121 L122 F126	N104 K105 K106 Y109 Y111 L112 F115	MOAD: Kd=0.6uM PDBbind-CN: -logKd/Ki=6.22,Kd=0.6uM

Gene Ontology

Molecular Function

• GO:0004623 phospholipase A2 activity
• GO:0005509 calcium ion binding
• GO:0005543 phospholipid binding
• GO:0047498 calcium-dependent phospholipase A2 activity
• GO:0090729 toxin activity

Biological Process

• GO:0006644 phospholipid metabolic process
• GO:0016042 lipid catabolic process
• GO:0031640 killing of cells of another organism
• GO:0035821 modulation of process of another organism
• GO:0042130 negative regulation of T cell proliferation
• GO:0042742 defense response to bacterium
• GO:0050482 arachidonate secretion
• GO:0050832 defense response to fungus

Cellular Component

• GO:0005576 extracellular region

External links

• PDB: RCSB:4yv5, PDBe:4yv5, PDBj:4yv5
• PDBsum: 4yv5
• PubMed: 26457430
• UniProt: Q9I834|PA2H2_BOTMO Basic phospholipase A2 homolog myotoxin II