Zn- and Bi-bound structure of the H77C variant of TriCyt2. Determined by X-ray diffraction at 1.57 Å resolution. Released 22 Oct 2025.
Explore 9PPR in 3D Show helices and sheets RCSB PDB PDBe
9PPR contains 15 α-helices and 0 β-strands across 3 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 | 3-18 | 16 | |
| α-helix | 23-40 | 18 | |
| α-helix | 46-48 | 3 | |
| α-helix | 56-80 | 25 | |
| α-helix | 84-105 | 22 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-19 | 17 | |
| α-helix | 23-41 | 19 | |
| α-helix | 46-48 | 3 | |
| α-helix | 56-80 | 25 | |
| α-helix | 84-105 | 22 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-18 | 16 | |
| α-helix | 23-41 | 19 | |
| 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, C | protein | 106 | Escherichia coli BL21(DE3) | P0ABE7 (AlphaFold model) |
>9PPR_1 Soluble cytochrome b562 (chains A, B, C) ADWEDNMETLNDNLKVIEKADNAAQVKDALTKMRAAALDAKKATPPKLEDKSPASPEMID FRVGFDILLWQIHDALCLANEGKVKEAQAAAEQLKTTVNAHWQKYR
Water and common crystallization additives (CL, NA) are not listed.
Design of a protein scaffold with a selective, Bi-containing heterodinuclear metal coordination motif. Eng, V.H., Gascon, M., Kakkis, A. et al. J Inorg Biochem (2025) 274:113104-113104. DOI 10.1016/j.jinorgbio.2025.113104 · 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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