- Protein Classification
- Protein Links
 | extracellular side |
| cytoplasmic side |
| 1d7p » C2 domain of coagulation factor VIII | |
|---|---|
| Depth | 4.8 ± 2.0 Å |
| Tilt Angle | 28 ± 10° |
| ΔGtransfer | -8.8 kcal/mol |
| Links to 1d7p | PDB Sum, PDB, SCOP, MSD, OCA, MMDB |
| Topology | extracellular |
| Resolution | 1.5 Å |
| Other PDB entries of this protein | 1iqd, 2r7e, 3cdz, 3hnb, 3hny, 3hob |
| Number of subunits | 1 |
| Experimental Verification for 1d7p » C2 domain of coagulation factor VIII |
|---|
| Residues M2199, F2200, L2251 and L2252 are involved in hydrophobic interactions with the membrane (Gilbert et al. 2002) in agreement with the set of calculated membrane core embedded residues M2199, F2200, L2251 and L2252. Maximal membrane binding affinity is -11.2 kcal/mol (Gilbert et al. 2002). |
| 1 reference |
|---|
| Gilbert, G.E., Kaufman, R.J., Arena, A.A., Miao, H., and Pipe, S.W. 2002. Four hydrophobic amino acids of the factor VIII C2 domain are constituents of both the membrane-binding and von Willebrand factor-binding motifs. J. Biol. Chem. 277:6374-6381. PubMed |
| Comments on 1d7p » C2 domain of coagulation factor VIII |
|---|
| Factor VIII, along with calcium and phospholipid, acts as a cofactor for factor IXa when it converts factor X to the activated form, factor Xa. C2 domain is responsible for phospholipid-binding. |
