Structure of PDB 3jq5 Chain A

Receptor sequence
>3jq5A (length=119) Species: 195058 (Naja sagittifera) [Search protein sequence]
NLYQFKNMIQCTVPSRSWADFADYGCYCGKGGSGTPVDDLDRCCQTHDNC
YNEAENISGCRPYFKTYSYECTQGTLTCKGDNNACAASVCDCDRLAAICF
AGAPYNDANYNIDLKARCN
3D structure
PDB3jq5 Phospholipase A2 Prevents the Aggregation of Amyloid Beta Peptides: Crystal Structure of the Complex of Phospholipase A2 with Octapeptide Fragment of Amyloid Beta Peptide, Asp-Ala-Glu-Phe-Arg-His-Asp-Ser at 2 A Resolution
ChainA
Resolution2.03 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y28 G30 G32 H48 D49 Y52 Y68 D94
Catalytic site (residue number reindexed from 1) Y27 G29 G31 H47 D48 Y51 Y67 D93
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 K6 W19 F22 A23 Y28 C29 G30 C45 H48 D49 Y64 F101 L2 K6 W18 F21 A22 Y27 C28 G29 C44 H47 D48 Y63 F100
BS02 CA A Y28 G30 K31 G32 D49 Y27 G29 K30 G31 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
Biological Process
GO:0006644 phospholipid metabolic process
GO:0016042 lipid catabolic process
GO:0050482 arachidonate secretion
Cellular Component
GO:0005576 extracellular region

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Cellular Component
External links
PDB RCSB:3jq5, PDBe:3jq5, PDBj:3jq5
PDBsum3jq5
PubMed
UniProtP60045|PA2A3_NAJSG Acidic phospholipase A2 3 (Fragment)

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