- Protein Classification
- Protein Links
 | intermembrane space side |
| cytoplasmic side |
| 1zza » Stannin | |
|---|---|
| Hydrophobic Thickness | 30.0 ± 2.0 Å |
| Tilt Angle | 13 ± 2° |
| ΔGtransfer | -25.2 kcal/mol |
| Links to 1zza | PDB Sum, PDB, SCOP, MSD, OCA, MMDB |
| Topology | subunit A (N-terminus intermembrane space) |
| Resolution | NMR |
| Other PDB entries of this protein | none |
| Number of TM Secondary Structures | 1 |
| 1 transmembrane subunit |
|---|
| A - Tilt: 13° - Segments: 1(10-28) |
| 2 references |
|---|
| Buck-Koehntop BA, Mascioni A, Buffy JJ, Veglia G. 2005. Structure, dynamics, and membrane topology of stannin: a mediator of neuronal cell apoptosis induced by trimethyltin chloride. J Mol Biol. 354:652-665. PubMed |
| Davidson CE, Reese BE, Billingsley ML, Yun JK. 2004. Stannin, a protein that localizes to the mitochondria and sensitizes NIH-3T3 cells to trimethyltin and dimethyltin toxicity. Mol Pharmacol. 66: 855-863. PubMed |
| Comments on 1zza » Stannin |
|---|
| This is structure in SDS micelles. Calculated orientation and hydrophobic thickness of this protein are unreliable, because the experimental structure was determined by combining distance constraints obtained for individual alpha-helices in micelles with orientational constraints obtained in the lipid bilayer (Buck-Koehntop et al. 2005). The transmembrane topology is tentative (Davidson et al. 2004). |
