Structure of human ferredoxin 2 (Fdx2)in complex with 2Fe2S cluster. Determined by X-ray diffraction at 1.7 Å resolution. Released 1 Feb 2012.
Explore 2Y5C in 3D Show helices and sheets RCSB PDB PDBe
2Y5C contains 16 α-helices and 14 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 | 5-11 | 7 | 1 |
| β-strand | 17-23 | 7 | 1 |
| β-strand | 27 | 1 | 2 |
| α-helix | 28-34 | 7 | |
| β-strand | 53-56 | 4 | 1 |
| α-helix | 57 | 1 | |
| α-helix | 58-61 | 4 | |
| α-helix | 65-68 | 4 | |
| α-helix | 69-76 | 8 | |
| β-strand | 85-87 | 3 | 1 |
| α-helix | 88-90 | 3 | |
| β-strand | 92 | 1 | 2 |
| α-helix | 95-97 | 3 | |
| β-strand | 101-103 | 3 | 1 |
| α-helix | 104-105 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 5-11 | 7 | 3 |
| β-strand | 17-23 | 7 | 3 |
| β-strand | 27 | 1 | 4 |
| α-helix | 28-35 | 8 | |
| β-strand | 53-56 | 4 | 3 |
| α-helix | 57 | 1 | |
| α-helix | 58-61 | 4 | |
| α-helix | 65-68 | 4 | |
| α-helix | 69-76 | 8 | |
| β-strand | 85-87 | 3 | 3 |
| α-helix | 88-90 | 3 | |
| β-strand | 92 | 1 | 4 |
| α-helix | 95-97 | 3 | |
| β-strand | 101-103 | 3 | 3 |
| α-helix | 104-105 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Adrenodoxin-like protein, mitochondrial | A, B | protein | 109 | HOMO SAPIENS | Q6P4F2 (AlphaFold model) |
>2Y5C_1 ADRENODOXIN-LIKE PROTEIN, MITOCHONDRIAL (chains A, B) MASDVVNVVFVDRSGQRIPVSGRVGDNVLHLAQRHGVDLEGACEASLACSTCHVYVSEDH LDLLPPPEEREDDMLDMAPLLQENSRLGCQIVLTPELEGAEFTLPKITR
| ID | Name | Formula | Copies |
|---|---|---|---|
| FES | FE2/S2 (inorganic) cluster | Fe2 S2 | 2 |
Water and common crystallization additives (SO4) are not listed.
Structure and Functional Studies on Human Mitochondrial Ferredoxins. Webert, H., Hobler, A., Sheftel, A.D. et al. To be published.
Other PDB entries of the same protein (UniProt Q6P4F2 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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