Improvement of the 2.5 Å resolution model of cytochrome B562 by redetermining the primary structure and using molecular graphics. Determined by X-ray diffraction at 1.4 Å resolution. Released 15 Jan 1991.
Explore 256B in 3D Show helices and sheets RCSB PDB PDBe
256B 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 | 46-48 | 3 | |
| α-helix | 56-80 | 25 | |
| α-helix | 84-91 | 8 | |
| α-helix | 93-105 | 13 |
| 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 | 84-92 | 9 | |
| α-helix | 94-105 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Cytochrome B562 | A, B | protein | 106 | Escherichia coli | P0ABE7 (AlphaFold model) |
>256B_1 CYTOCHROME B562 (chains A, B) ADLEDNMETLNDNLKVIEKADNAAQVKDALTKMRAAALDAQKATPPKLEDKSPDSPEMKD FRHGFDILVGQIDDALKLANEGKVKEAQAAAEQLKTTRNAYHQKYR
| ID | Name | Formula | Copies |
|---|---|---|---|
| HEM | Protoporphyrin IX containing FE | C34 H32 Fe N4 O4 | 2 |
Water and common crystallization additives (SO4) are not listed.
Improvement of the 2.5 A resolution model of cytochrome b562 by redetermining the primary structure and using molecular graphics. Lederer, F., Glatigny, A., Bethge, P.H. et al. J Mol Biol (1981) 148:427-448. DOI 10.1016/0022-2836(81)90185-6 · 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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