Structure of PDB 2rd4 Chain B

Receptor sequence
>2rd4B (length=119) Species: 195058 (Naja sagittifera) [Search protein sequence]
NRWQFKNMISCTVPSRSWWDFADYGCYCGRGGSGTPVDDLDRCCQVHDNC
YNEAEKISGCNPRFRTYSYECTAGTLTCTGRNNACAASVCDCDRLAAICF
AGAPYNDNNYNIDLQARCN
3D structure
PDB2rd4 Design of specific inhibitors of Phospholipase A2: Crystal structure of the complex of phospholipase A2 with pentapeptide Leu-Val-Phe-Phe-Ala at 2.9 A resolution
ChainB
Resolution2.97 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 B R2 F5 K6 I9 W19 R31 C45 H48 D49 R64 R2 F5 K6 I9 W18 R30 C44 H47 D48 R63
BS02 CA B D24 N112 D23 N111
BS03 CA B Y28 G30 R31 G32 D49 Y27 G29 R30 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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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:2rd4, PDBe:2rd4, PDBj:2rd4
PDBsum2rd4
PubMed
UniProtP60044|PA2A2_NAJSG Acidic phospholipase A2 2 (Fragment)

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