Structure of PDB 1oxr Chain A

Receptor sequence
>1oxrA (length=119) Species: 195058 (Naja sagittifera) [Search protein sequence]
NLYQFKNMIQCTVPSRSWQDFADYGCYCGKGGSGTPVDDLDRCCQVHDNC
YNEAENISGCRPYFKTYSYECTQGTLTCKGDNNACAASVCDCDRLAAICF
AGAPYNDANYNIDLKARCN
3D structure
PDB1oxr Aspirin induces its anti-inflammatory effects through its specific binding to phospholipase A2: crystal structure of the complex formed between phospholipase A2 and aspirin at 1.9 angstroms resolution.
ChainA
Resolution1.93 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 AIN A L2 G30 Y64 L2 G29 Y63 MOAD: Kd=0.000000064M
PDBbind-CN: -logKd/Ki=5.19,Kd=6.4uM
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:1oxr, PDBe:1oxr, PDBj:1oxr
PDBsum1oxr
PubMed15823962
UniProtP60045|PA2A3_NAJSG Acidic phospholipase A2 3 (Fragment)

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