The C-terminal Region of Disintegrin Modulate its 3D Conformation and Cooperate with RGD Loop in Regulating Recognitions of Integrins. Determined by solution NMR. Released 22 May 2013.
Explore 2M75 in 3D Show helices and sheets RCSB PDB PDBe
2M75 contains 1 α-helix and 6 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 14-15 | 2 | 1 |
| β-strand | 20-21 | 2 | 1 |
| β-strand | 33-34 | 2 | 2 |
| β-strand | 37-38 | 2 | 2 |
| β-strand | 41-46 | 6 | 3 |
| α-helix | 53-54 | 2 | |
| β-strand | 55-58 | 4 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Zinc metalloproteinase/disintegrin | A | protein | 76 | Calloselasma rhodostoma | P30403 (AlphaFold model) |
>2M75_1 Zinc metalloproteinase/disintegrin (chains A) EFHHHHHHGKECDCSSPENPCCDAATCKLRPGAQCGEGLCCEQCKFSRAGKICRIARGDW NDDRCTGQSADCPRYH
The C-terminal Region of Disintegrin Modulate its 3D Conformation and Cooperate with RGD Loop in Regulating Recognitions of Integrins. Chuang, W., Chang, Y., Shiu, J. et al. To be published.
Other PDB entries of the same protein (UniProt P30403 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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