X-ray Crystal Structure of Chemically Synthesized Crambin. Determined by X-ray diffraction at 1.75 Å resolution. Released 16 Jan 2007.
Explore 2FD7 in 3D Show helices and sheets RCSB PDB PDBe
2FD7 contains 3 α-helices and 2 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 | 2-3 | 2 | 1 |
| α-helix | 7-17 | 11 | |
| α-helix | 23-30 | 8 | |
| β-strand | 33-34 | 2 | 1 |
| α-helix | 42-44 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Crambin | A | protein | 46 | P01542 (AlphaFold model) |
>2FD7_1 Crambin (chains A) TTCCPSIVARSNFNVCRLPGTPEALCATYTGCIIIPGATCPGDYAN
Role of a salt bridge in the model protein crambin explored by chemical protein synthesis: X-ray structure of a unique protein analogue, [V15A]crambin-alpha-carboxamide. Bang, D., Tereshko, V., Kossiakoff, A.A. et al. Mol Biosyst (2009) 5:750-756. DOI 10.1039/b903610e · PubMed
Other PDB entries of the same protein (UniProt P01542 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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