Cu(II)-bound structure of the engineered cyt cb562 variant, CH3Y. Determined by X-ray diffraction at 1.1 Å resolution. Released 24 Apr 2019.
Explore 6DYF in 3D Show helices and sheets RCSB PDB PDBe
6DYF contains 12 α-helices and 0 β-strands across 2 chains. 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 |
|---|---|---|---|
| α-helix | 3-19 | 17 | |
| α-helix | 23-40 | 18 | |
| α-helix | 44-45 | 2 | |
| α-helix | 46-48 | 3 | |
| α-helix | 56-80 | 25 | |
| α-helix | 84-92 | 9 | |
| α-helix | 95-105 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-19 | 17 | |
| α-helix | 23-40 | 18 | |
| α-helix | 46-48 | 3 | |
| α-helix | 56-80 | 25 | |
| α-helix | 84-105 | 22 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Soluble cytochrome b562 | A, B | protein | 106 | Escherichia coli | P0ABE7 (AlphaFold model) |
>6DYF_1 Soluble cytochrome b562 (chains A, B) ADLEDNMETLNDNLKVIEKADNAAQVKDALTKMRAAALDAQKATPPKLEDKSPDSPEMWD FRHGFDHLVYHIDDALKLANEGKVKEAQAAAEQLKCHCNACHQKYR
Water and common crystallization additives (PEG, CL) are not listed.
An efficient, step-economical strategy for the design of functional metalloproteins. Rittle, J., Field, M.J., Green, M.T. et al. Nat Chem (2019) 11:434-441. DOI 10.1038/s41557-019-0218-9 · PubMed
Other PDB entries of the same protein (UniProt P0ABE7 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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