- Protein Classification
- Protein Links
| 1poa » Snake phospholipase A2, group I | |
|---|---|
| Depth | 4.8 ± 1.0 Å |
| Tilt Angle | 89 ± 7° |
| ΔGtransfer | -10.7 kcal/mol |
| Links to 1poa | PDB Sum, PDB, SCOP, MSD, OCA, MMDB |
| Topology | out |
| Resolution | 1.5 Å |
| Other PDB entries of this protein | 1pob |
| Number of subunits | 1 |
| Experimental Verification for 1poa » Snake phospholipase A2, group I |
|---|
| Residues penetrating the bilayer core are W19, W61 and F64 (Y3 and W18 are mostly outsite the calculated boundaries). This is consistent with the important role of W19, W61, and F64 (Sumandea et al. 1999) or W61, F64 and Y110 (Stahelin and Cho 2001) in protein-membrane asociation. Y110 is in the interfacial region (just beyond the hydrophobic core) in the calculated orientation of the phospholipase. Maximal membrane binding affinity is -11.4 kcal/mol (Stahelin and Cho 2001). |
| 2 references |
|---|
| Stahelin, R.V., and Cho, W. 2001. Differential roles of ionic, aliphatic, and aromatic residues in membrane-protein interactions: a surface plasmon resonance study on phospholipases A2. Biochemistry. 40:4672-4678. PubMed |
| Sumandea M, Das S, Sumandea C, Cho W. 1999. Roles of aromatic residues in high interfacial activity of Naja naja atra phospholipase A2. Biochemistry. 38:16290-7. PubMed |
