Structure of PDB 2do2 Chain A

Receptor sequence

>2do2A (length=121) Species: 97228 (Daboia russelii pulchella)

SLLEFGKMILEETGKLAIPSYSSYGCYCGGCGSGTPKDATDRCCFVHCCC
YGNLPDCNPKSDRYKYKRVNGAIVCEKGTSCENRICECDKAAAICFRQNL
NTYSKKYMLYPDFLCKGELKC

3D structure

• PDB: 2do2 Design of specific inhibitors of phospholipase A2: Crystal structure of the complex formed between a group II Cys 49 phospholipase A2 and a designed pentapeptide Ala-Leu-Ala-Ser-Lys at 2.6A resolution
• Chain: A
• Resolution: 2.6 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): Y28 G30 C32 H48 C49 Y52 Y73 D99
• Catalytic site (residue number reindexed from 1): Y27 G29 C31 H47 C48 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 L17 I19 S23 G30	L2 L3 L16 I18 S22 G29

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:2do2, PDBe:2do2, PDBj:2do2
• PDBsum: 2do2
• UniProt: P59071|PA2B8_DABRR Basic phospholipase A2 VRV-PL-VIIIa