Structure of PDB 1fe5 Chain A

Receptor sequence
>1fe5A (length=118) Species: 132961 (Bungarus caeruleus) [Search protein sequence]
NLIQFKNMIQCAGTRPWTAYVNYGCYCGKGGSGTPVDELDRCCYTHDNCY
NEAEKIPGCNPNIKTYSYTCTEPNLTCTDTADTCARFLCNCDRTAAICFA
SAPYNSNNVMISSSTNCQ
3D structure
PDB1fe5 Sequence and crystal structure determination of a basic phospholipase A2 from common krait (Bungarus caeruleus) at 2.4 A resolution: identification and characterization of its pharmacological sites.
ChainA
Resolution2.45 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) Y26 G28 G30 H46 D47 Y50 Y66 D92
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 CA A Y28 G30 G32 D49 Y26 G28 G30 D47
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: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:1fe5, PDBe:1fe5, PDBj:1fe5
PDBsum1fe5
PubMed11286555
UniProtQ9DF52|PA2B_BUNCE Basic phospholipase A2 KPA2

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