| 1xxs » Myotoxin II | |
|---|---|
| Depth | 4.5 ± 1.2 Å |
| Tilt Angle | 76 ± 10° |
| ΔGtransfer | -5.3 kcal/mol |
| Links to 1xxs | PDB Sum, PDB, SCOP, MSD, OCA, MMDB |
| Topology | out |
| Resolution | 1.8 Å |
| Other PDB entries of this protein | none |
| Number of subunits | 1 |
| 1 reference |
|---|
| Watanabe L, Soares AM, Ward RJ, Fontes MR, Arni RK. 2005. Structural insights for fatty acid binding in a Lys49-phospholipase A2: crystal structure of myotoxin II from Bothrops moojeni complexed with stearic acid. Biochimie. 87: 161-7. PubMed |
| Comments on 1xxs » Myotoxin II |
|---|
| Displays myotoxin and edema-inducing activities. Lacks PA2 enzymatic activity as well as of hemorrhagic, anticoagulant and coagulant activities. Homodimer in aqueous solution. Does not bind calcium as one of the calcium binding ligands is lost (Asp->Lys in position 48). Two stearic acid molecules were located in the substrate-binding cleft of each monomer in positions, which favor the interaction of their carboxyl groups with active site residues. The way of binding of stearic acids to this Lys49-PLA(2)s is analogous to phospholipids and transition state analogues to catalytically active PLA(2)s. Two additional stearic acid molecules were located at the dimer interface region, defining a hitherto unidentified acyl-binding site on the protein surface. The strictly conserved Lys122 for Lys49-PLA(2)s may play a fundamental role for stabilization of ligand-protein complex (Watanabe et al. 2005). |