K13R mutant of horse cytochrome c and yeast cytochrome c peroxidase complex. Determined by X-ray diffraction at 2.11 Å resolution. Released 24 Sept 2014.
Explore 4NFG in 3D Show helices and sheets RCSB PDB PDBe
4NFG contains 30 α-helices and 13 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 |
|---|---|---|---|
| β-strand | 7 | 1 | 1 |
| α-helix | 10-11 | 2 | |
| α-helix | 16-32 | 17 | |
| α-helix | 36-39 | 4 | |
| α-helix | 43-54 | 12 | |
| β-strand | 58 | 1 | 2 |
| β-strand | 63 | 1 | 2 |
| α-helix | 70-72 | 3 | |
| α-helix | 74-77 | 4 | |
| α-helix | 80-82 | 3 | |
| α-helix | 86-98 | 13 | |
| α-helix | 104-118 | 15 | |
| β-strand | 126 | 1 | 3 |
| α-helix | 135-137 | 3 | |
| α-helix | 138-140 | 3 | |
| α-helix | 145-146 | 2 | |
| α-helix | 151-159 | 9 | |
| α-helix | 165-172 | 8 | |
| α-helix | 173-176 | 4 | |
| β-strand | 179-180 | 2 | 4 |
| α-helix | 182-185 | 4 | |
| β-strand | 189-190 | 2 | 4 |
| α-helix | 201-208 | 8 | |
| α-helix | 210-211 | 2 | |
| β-strand | 212-215 | 4 | 5 |
| β-strand | 221-224 | 4 | 5 |
| β-strand | 230-231 | 2 | 5 |
| α-helix | 233-240 | 8 | |
| α-helix | 242-253 | 12 | |
| α-helix | 255-271 | 17 | |
| β-strand | 275 | 1 | 1 |
| α-helix | 276-277 | 2 | |
| α-helix | 281-283 | 3 | |
| β-strand | 284 | 1 | 3 |
| α-helix | 286-288 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-13 | 11 | |
| α-helix | 24-26 | 3 | |
| β-strand | 39 | 1 | 6 |
| α-helix | 50-53 | 4 | |
| β-strand | 58 | 1 | 6 |
| α-helix | 61-69 | 9 | |
| α-helix | 71-74 | 4 | |
| α-helix | 88-101 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Cytochrome c peroxidase, mitochondrial | A | protein | 294 | Saccharomyces cerevisiae | P00431 (AlphaFold model) |
| Cytochrome c | B | protein | 104 | Equus caballus | P00004 (AlphaFold model) |
>4NFG_1 Cytochrome c peroxidase, mitochondrial (chains A) MKTLVHVASVEKGRSYEDFQKVYNAIALKLREDDEYDNYIGYGPVLVRLAWHTSGTWDKH DNTGGSYGGTYRFKKEFNDPSNAGLQNGFKFLEPIHKEFPWISSGDLFSLGGVTAVQEMQ GPKIPWRAGRVDTPEDTTPDNGRLPDADKDADYVRTFFQRLNMNDREVVALMGAHALGKT HLKNSGYEGPWGAANNVFTNEFYLNLLNEDWKLEKNDANNEQWDSKSGYMMLPTDYSLIQ DPKYLSIVKEYANDQDKFFKDFSKAFEKLLENGITFPKDAPSPFIFKTLEEQGL
>4NFG_2 Cytochrome c (chains B) GDVEKGKKIFVQRCAQCHTVEKGGKNKTGPNLNGLFGRKTGQAPGFTYTDANKNKGITWK EETLMEYLENPKKYIPGTKMIFAGIKKKTEREDLIAYLKKATNE
Water and common crystallization additives (UNX) are not listed.
Engineering specificity in a dynamic protein complex with a single conserved mutation. Bashir, Q., Meulenbroek, E.M., Pannu, N.S. et al. FEBS J (2014) 281:4892-4905. DOI 10.1111/febs.13028 · PubMed
Other PDB entries of the same protein (UniProt P00431 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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