Co-bound crystal structure of the engineered cyt cb562 variant, DiCyt2. Determined by X-ray diffraction at 1.27 Å resolution. Released 27 Apr 2022.
Explore 7MK4 in 3D Show helices and sheets RCSB PDB PDBe
7MK4 contains 13 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 | 23-41 | 19 | |
| α-helix | 44-45 | 2 | |
| α-helix | 46-48 | 3 | |
| α-helix | 56-80 | 25 | |
| α-helix | 84-93 | 10 | |
| α-helix | 95-105 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-19 | 17 | |
| α-helix | 24-40 | 17 | |
| α-helix | 46-48 | 3 | |
| α-helix | 56-80 | 25 | |
| α-helix | 84-93 | 10 | |
| α-helix | 95-105 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Soluble cytochrome b562 | A, B | protein | 106 | Escherichia coli | P0ABE7 (AlphaFold model) |
>7MK4_1 Soluble cytochrome b562 (chains A, B) ADLEDNMETLNDNLKVIEKADNAAQVKDALTKMRAAALDAQKATPPKLEDKSPDSPEMWH FRHGFDHLVGHIDDALKLANEGKVKEAQAAAEQLKCHCNHCHQHYR
Overcoming universal restrictions on metal selectivity by protein design. Choi, T.S., Tezcan, F.A. Nature (2022) 603:522-527. DOI 10.1038/s41586-022-04469-8 · 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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