Structure of PDB 3r0l Chain D

Receptor sequence
>3r0lD (length=122) Species: 8732 (Crotalus durissus terrificus) [Search protein sequence]
HLLQFNKMIKFETRKNAVPFYAFYGCYCGWGGQGRPKDATDRCCFVHDCC
YGKLAKCNTKWDIYRYSLKSGYITCGKGTWCEEQICECDRVAAECLRRSL
STYKNGYMFYPDSRCRGPSETC
3D structure
PDB3r0l Crystal Structure of Crotoxin Reveals Key Residues Involved in the Stability and Toxicity of This Potent Heterodimeric Beta-Neurotoxin
ChainD
Resolution1.35 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y27 G29 G31 H47 D48 Y51 Y64 D89
Catalytic site (residue number reindexed from 1) Y27 G29 G31 H47 D48 Y51 Y64 D89
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 MN D D62 E82 D62 E82
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
GO:0099106 ion channel regulator activity
Biological Process
GO:0006644 phospholipid metabolic process
GO:0016042 lipid catabolic process
GO:0035821 modulation of process of another organism
GO:0042130 negative regulation of T cell proliferation
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:3r0l, PDBe:3r0l, PDBj:3r0l
PDBsum3r0l
PubMed21787789
UniProtP0CG56|PA2BB_CRODU Phospholipase A2 crotoxin basic subunit CBb

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