Structure of PDB 1z76 Chain A

Receptor sequence
>1z76A (length=122) Species: 8726 (Bothrops jararacussu) [Search protein sequence]
SLWQFGKMINYVMGESGVLQYLSYGCYCGLGGQGQPTDATDRCCFVHDCC
YGKVTGCDPKIDSYTYSKKNGDVVCGGDDPCKKQICECDRVATTCFRDNK
DTYDIKYWFYGAKNCQEKSEPC
3D structure
PDB1z76 Structure of BthA-I complexed with p-bromophenacyl bromide: possible correlations with lack of pharmacological activity.
ChainA
Resolution1.85 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) 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 PBP A G30 C45 H48 G29 C44 H47
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:0008217 regulation of blood pressure
GO:0016042 lipid catabolic process
GO:0035821 modulation of process of another organism
GO:0042742 defense response to bacterium
GO:0050482 arachidonate secretion
Cellular Component
GO:0005576 extracellular region

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Cellular Component
External links
PDB RCSB:1z76, PDBe:1z76, PDBj:1z76
PDBsum1z76
PubMed16301802
UniProtQ8AXY1|PA2A_BOTJR Acidic phospholipase A2 BthA-1

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