- Protein Classification
- Protein Links
| 7ahl » Alpha-hemolysin | |
|---|---|
| Hydrophobic Thickness | 23.5 ± 0.9 Å |
| Tilt Angle | 0 ± 1° |
| ΔGtransfer | -49.3 kcal/mol |
| Links to 7ahl | PDB Sum, PDB, SCOP, MSD, OCA, MMDB |
| Topology | subunit A (N-terminus out) |
| Resolution | 1.89 Å |
| Other PDB entries of this protein | 3anz, 3m2l, 3m3r, 3m4d, 3m4e |
| Number of TM Secondary Structures | 14 |
| 7 transmembrane subunits |
|---|
| A - Tilt: 33° - Segments: 1(119-126), 2(132-140) |
| B - Tilt: 34° - Segments: 1(119-126), 2(132-140) |
| C - Tilt: 34° - Segments: 1(119-126), 2(132-140) |
| D - Tilt: 34° - Segments: 1(119-126), 2(132-140) |
| E - Tilt: 35° - Segments: 1(119-126), 2(132-140) |
| F - Tilt: 34° - Segments: 1(119-126), 2(132-140) |
| G - Tilt: 34° - Segments: 1(119-126), 2(132-140) |
| Experimental Verification for 7ahl » Alpha-hemolysin |
|---|
| Several Trp residues of alpha-hemolysin (7ahl) are situated in the lipid head group area according to our results, which is consistent with their accessibility to water-soluble iodide and doxyl probes (Raja et al. 1999) and with locations of lipid head groups determined crystallographically (Galdiero and Gouaux 2004). |
| 2 references |
|---|
| Galdiero S, Gouaux E. 2004. Protein Sci. 13:1503-1511. PubMed |
| Raja SM, Rawat SS, Chattopadhyay A, and Lala AK (1999) Localization and environment of tryptophans in soluble and membrane-bound states of a pore-forming toxin from Staphylococcus aureus. Biophys. J. 76: 1469-1479. PubMed |
