Correlated disorder of the pure PRO22(SLASH)LEU25 form of crambin at 150K refined to 1.05 Å resolution. Determined by X-ray diffraction at 1.05 Å resolution. Released 31 Aug 1994.
Explore 1CNR in 3D Show helices and sheets RCSB PDB PDBe
1CNR 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 | Crambe hispanica subsp. abyssinica | P01542 (AlphaFold model) |
>1CNR_1 CRAMBIN (chains A) TTCCPSIVARSNFNVCRLPGTPEALCATYTGCIIIPGATCPGDYAN
| ID | Name | Formula | Copies |
|---|---|---|---|
| EOH | Ethanol | C2 H6 O | 1 |
Correlated disorder of the pure Pro22/Leu25 form of crambin at 150 K refined to 1.05-A resolution. Yamano, A., Teeter, M.M. J Biol Chem (1994) 269:13956-13965. 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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