![]() | extracellular side |
| cytoplasmic side |
| 1dm5 » Annexin XII | |
|---|---|
| Depth | 2.7 ± 1.0 Å |
| Tilt Angle | 90 ± 7° |
| ΔGtransfer | -10.2 kcal/mol |
| Links to 1dm5 | PDB Sum, PDB, SCOP, MSD, OCA, MMDB |
| Topology | cytoplasmic |
| Resolution | 1.9 Å |
| Other PDB entries of this protein | 1aei |
| Number of subunits | 3 |
| Experimental Verification for 1dm5 » Annexin XII |
|---|
| Residues E142, S144 and G145 of annexin B12 are positioned just beyond the calculated hydrophobic boundary (subunit C of the trimer) and their side-chains are directed toward the membrane, which is consistent with spin-labeling studies (Isas et al. 2004). |
| 1 reference |
|---|
| Isas, J.M., Langen, R., Hubbell, W.L., and Haigler, H.T. 2004. Structure and dynamics of a helical hairpin that mediates calcium-dependent membrane binding of annexin B12. J. Biol. Chem. 279:32492-32498. PubMed |
| Comments on 1dm5 » Annexin XII |
|---|
| This protein undergoes major conformational changes upon association with membranes. |