Solution structure of rhodostomin. Determined by solution NMR. Released 8 May 2007.
Explore 2PJF in 3D Show helices and sheets RCSB PDB PDBe
2PJF 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 |
|---|---|---|---|---|---|
| Rhodostoxin-disintegrin rhodostomin | A | protein | 68 | Calloselasma rhodostoma | P30403 (AlphaFold model) |
>2PJF_1 Rhodostoxin-disintegrin rhodostomin (chains A) GKECDCSSPENPCCDAATCKLRPGAQCGEGLCCEQCKFSRAGKICRIPRGDMPDDRCTGQ SADCPRYH
Effect of D to E mutation of the RGD motif in rhodostomin on its activity, structure, and dynamics: Importance of the interactions between the D residue and integrin. Chen, C.Y., Shiu, J.H., Hsieh, Y.H. et al. Proteins (2009). DOI 10.1002/prot.22387 · PubMed
Other PDB entries of the same protein (UniProt P30403 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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