The crystal structure of poplar apoplastocyanin at 1.8-Å resolution. The geometry of the copper-binding site is created by the polypeptide. Determined by X-ray diffraction at 1.8 Å resolution. Released 2 Feb 1984.
Explore 2PCY in 3D Show helices and sheets RCSB PDB PDBe
2PCY contains 2 α-helices and 10 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 | 2-5 | 4 | 1 |
| β-strand | 14-15 | 2 | 1 |
| β-strand | 18-21 | 4 | 2 |
| β-strand | 26-31 | 6 | 1 |
| β-strand | 37 | 1 | 3 |
| β-strand | 40-41 | 2 | 2 |
| α-helix | 52-55 | 4 | |
| β-strand | 63 | 1 | 3 |
| β-strand | 69-73 | 5 | 1 |
| β-strand | 78-83 | 6 | 2 |
| α-helix | 85-87 | 3 | |
| β-strand | 93-98 | 6 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Plastocyanin | A | protein | 99 | Populus nigra | P00299 (AlphaFold model) |
>2PCY_1 PLASTOCYANIN (chains A) IDVLLGADDGSLAFVPSEFSISPGEKIVFKNNAGFPHNIVFDEDSIPSGVDASKISMSEE DLLNAKGETFEVALSNKGEYSFYCSPHQGAGMVGKVTVN
The crystal structure of poplar apoplastocyanin at 1.8-A resolution. The geometry of the copper-binding site is created by the polypeptide. Garrett, T.P., Clingeleffer, D.J., Guss, J.M. et al. J Biol Chem (1984) 259:2822-2825. PubMed
Other PDB entries of the same protein (UniProt P00299 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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