Crystal structure of a complex between electron transfer partners, cytochrome C peroxidase and cytochrome C. Determined by X-ray diffraction at 2.8 Å resolution. Released 15 Jul 1993.
Explore 2PCB in 3D Show helices and sheets RCSB PDB PDBe
2PCB contains 49 α-helices and 24 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 |
|---|---|---|---|
| β-strand | 6-7 | 2 | 1 |
| 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 | 74-78 | 5 | |
| 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 | |
| β-strand | 212-215 | 4 | 5 |
| β-strand | 221-224 | 4 | 5 |
| β-strand | 230-231 | 2 | 5 |
| α-helix | 233-237 | 5 | |
| α-helix | 242-253 | 12 | |
| α-helix | 255-271 | 17 | |
| β-strand | 274-275 | 2 | 1 |
| α-helix | 281-283 | 3 | |
| β-strand | 284 | 1 | 3 |
| α-helix | 286-288 | 3 | |
| α-helix | 289-291 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 4-13 | 10 | |
| α-helix | 24-26 | 3 | |
| β-strand | 36 | 1 | 6 |
| α-helix | 50-53 | 4 | |
| β-strand | 59 | 1 | 6 |
| α-helix | 61-67 | 7 | |
| α-helix | 71-74 | 4 | |
| α-helix | 89-101 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 2-4 | 3 | |
| β-strand | 7 | 1 | 7 |
| α-helix | 16-32 | 17 | |
| α-helix | 36-39 | 4 | |
| α-helix | 43-54 | 12 | |
| β-strand | 58 | 1 | 8 |
| β-strand | 63 | 1 | 8 |
| α-helix | 70-72 | 3 | |
| α-helix | 74-77 | 4 | |
| α-helix | 80-82 | 3 | |
| α-helix | 86-97 | 12 | |
| α-helix | 104-118 | 15 | |
| β-strand | 126 | 1 | 9 |
| α-helix | 138-140 | 3 | |
| α-helix | 151-159 | 9 | |
| α-helix | 165-171 | 7 | |
| α-helix | 172-176 | 5 | |
| β-strand | 180 | 1 | 10 |
| α-helix | 182-185 | 4 | |
| β-strand | 189 | 1 | 10 |
| α-helix | 201-208 | 8 | |
| β-strand | 211-215 | 5 | 11 |
| β-strand | 221-225 | 5 | 11 |
| β-strand | 230-231 | 2 | 11 |
| α-helix | 233-240 | 8 | |
| α-helix | 242-253 | 12 | |
| α-helix | 255-271 | 17 | |
| β-strand | 275 | 1 | 7 |
| α-helix | 281-283 | 3 | |
| β-strand | 284 | 1 | 9 |
| α-helix | 285 | 1 | |
| α-helix | 289-292 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Cytochrome C peroxidase (CCP) | A, C | protein | 296 | Saccharomyces cerevisiae | P00431 (AlphaFold model) |
| Cytochrome C | B | protein | 104 | Equus caballus | P00004 (AlphaFold model) |
>2PCB_1 CYTOCHROME C PEROXIDASE (CCP) (chains A, C) MITTPLVHVASVEKGRSYEDFQKVYNAIALKLREDDEYDNYIGYGPVLVRLAWHISGTWD KHDNTGGSYGGTYRFKKEFNDPSNAGLQNGFKFLEPIHKEFPWISSGDLFSLGGVTAVQE MQGPKIPWRCGRVDTPEDTTPDNGRLPDADKDAGYVRTFFQRLNMNDREVVALMGAHALG KTHLKNSGYEGPWGAANNVFTNEFYLNLLNEDWKLEKNDANNEQWDSKSGYMMLPTDYSL IQDPKYLSIVKEYANDQDKFFKDFSKAFEKLLENGITFPKDAPSPFIFKTLEEQGL
>2PCB_2 CYTOCHROME C (chains B) GDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAPGFTYTDANKNKGITWK EETLMEYLENPKKYIPGTKMIFAGIKKKTEREDLIAYLKKATNE
| ID | Name | Formula | Copies |
|---|---|---|---|
| HEM | Protoporphyrin IX containing FE | C34 H32 Fe N4 O4 | 3 |
Crystal structure of a complex between electron transfer partners, cytochrome c peroxidase and cytochrome c. Pelletier, H., Kraut, J. Science (1992) 258:1748-1755. 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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