Structure of PDB 1m8t Chain E

Receptor sequence
>1m8tE (length=119) Species: 8665 (Ophiophagus hannah) [Search protein sequence]
HLVQFNGMIRCTIPGSIPWWDYSDYGCYCGSGGSGTPVDELDRCCQVHDN
CYTQAQQLTECSPYSKRYSYDCSEGTLTCKADNDECAAFVCDCDRVAAIC
FAGAPYNKENINIDTTTRC
3D structure
PDB1m8t Structure of a king cobra phospholipase A2 determined from a hemihedrally twinned crystal.
ChainE
Resolution2.1 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 Y73 D99
Catalytic site (residue number reindexed from 1) Y28 G30 G32 H48 D49 Y52 Y68 D94
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 E Y28 G30 G32 D49 Y28 G30 G32 D49
Gene Ontology
Molecular Function
GO:0004623 phospholipase A2 activity
GO:0005102 signaling receptor binding
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:0006633 fatty acid biosynthetic process
GO:0006644 phospholipid metabolic process
GO:0016042 lipid catabolic process
GO:0035821 modulation of process of another organism
GO:0048146 positive regulation of fibroblast proliferation
GO:0050482 arachidonate secretion
Cellular Component
GO:0005576 extracellular region

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Cellular Component
External links
PDB RCSB:1m8t, PDBe:1m8t, PDBj:1m8t
PDBsum1m8t
PubMed12925787
UniProtQ9DF33|PA2A2_OPHHA Acidic phospholipase A2 2

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