Structure of PDB 1qll Chain B

Receptor sequence
>1qllB (length=121) Species: 113192 (Bothrops pirajai) [Search protein sequence]
SLFELGKMILQETGKNPAKSYGAYGCNCGVLGRGKPKDATDRCCYVHKCC
YKKLTGCNPKKDRYSYSWKDKTIVCGENNPCLKELCECDKAVAICLRENL
GTYNKKYRYHLKPFCKKADKC
3D structure
PDB1qll Structural Basis for Low Catalytic Activity in Lys49 Phospholipases A2-A Hypothesis: The Crystal Structure of Piratoxin II Complexed to Fatty Acid
ChainB
Resolution2.04 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) N27 G29 L31 H47 K48 Y51 Y64 D89
Catalytic site (residue number reindexed from 1) N27 G29 L31 H47 K48 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 TDA B L2 G6 Y21 C28 G29 H47 L2 G6 Y21 C28 G29 H47
Gene Ontology
Molecular Function
GO:0004623 phospholipase A2 activity
GO:0005509 calcium ion binding
GO:0005543 phospholipid 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: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:1qll, PDBe:1qll, PDBj:1qll
PDBsum1qll
PubMed11141053
UniProtP82287|PA2H2_BOTPI Basic phospholipase A2 homolog piratoxin-2

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