Structure of PDB 1jq9 Chain A

Receptor sequence

>1jq9A (length=121) Species: 97228 (Daboia russelii pulchella)

SLLEFGKMILEETGKLAIPSYSSYGCYCGWGGKGTPKDATDRCCFVHDCC
YGNLPDCNPKSDRYKYKRVNGAIVCEKGTSCENRICECDKAAAICFRQNL
NTYSKKYMLYPDFLCKGELKC

3D structure

• PDB: 1jq9 Crystal Structure of a Complex Formed between a Snake Venom Phospholipase A2 and a Potent Peptide Inhibitor Phe-Leu-Ser-Tyr-Lys at 1.8 A Resolution
• Chain: A
• Resolution: 1.8 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): Y28 G30 G32 H48 D49 Y52 Y73 D99
• Catalytic site (residue number reindexed from 1): Y27 G29 G31 H47 D48 Y51 Y64 D89
• 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	peptide	A	L2 L3 F5 G6 K7 I9 A18 I19 Y28 C29 G30 W31 H48 D49	L2 L3 F5 G6 K7 I9 A17 I18 Y27 C28 G29 W30 H47 D48

Gene Ontology

Molecular Function

• GO:0004623 phospholipase A2 activity
• GO:0005509 calcium ion binding
• GO:0005543 phospholipid binding
• GO:0016787 hydrolase activity
• GO:0046872 metal ion 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:0035821 modulation of process of another organism
• GO:0042130 negative regulation of T cell proliferation
• GO:0050482 arachidonate secretion

Cellular Component

• GO:0005576 extracellular region

External links

• PDB: RCSB:1jq9, PDBe:1jq9, PDBj:1jq9
• PDBsum: 1jq9
• PubMed: 12186870
• UniProt: P59071|PA2B8_DABRR Basic phospholipase A2 VRV-PL-VIIIa