The bovine mitochondrial ADP-ATP carrier. Determined by X-ray diffraction at 2.8 Å resolution. Released 20 Oct 2005.
Explore 2C3E in 3D Show helices and sheets RCSB PDB PDBe
2C3E contains 14 α-helices and 0 β-strands across 1 chain. 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 | 8-37 | 30 | |
| α-helix | 38-40 | 3 | |
| α-helix | 53-64 | 12 | |
| α-helix | 66-70 | 5 | |
| α-helix | 73-98 | 26 | |
| α-helix | 108-141 | 34 | |
| α-helix | 156-172 | 17 | |
| α-helix | 176-200 | 25 | |
| α-helix | 210-226 | 17 | |
| α-helix | 228-238 | 11 | |
| α-helix | 253-259 | 7 | |
| α-helix | 260-264 | 5 | |
| α-helix | 268-270 | 3 | |
| α-helix | 275-290 | 16 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Adp/atp translocase 1 | A | protein | 297 | BOS TAURUS | P02722 (AlphaFold model) |
>2C3E_1 ADP/ATP TRANSLOCASE 1 (chains A) SDQALSFLKDFLAGGVAAAISKTAVAPIERVKLLLQVQHASKQISAEKQYKGIIDCVVRI PKEQGFLSFWRGNLANVIRYFPTQALNFAFKDKYKQIFLGGVDRHKQFWRYFAGNLASGG AAGATSLCFVYPLDFARTRLAADVGKGAAQREFTGLGNCITKIFKSDGLRGLYQGFNVSV QGIIIYRAAYFGVYDTAKGMLPDPKNVHIIVSWMIAQTVTAVAGLVSYPFDTVRRRMMMQ SGRKGADIMYTGTVDCWRKIAKDEGPKAFFKGAWSNVLRGMGGAFVLVLYDEIKKFV
Structural Basis for Lipid-Mediated Interactions between Mitochondrial Adp/ATP Carrier Monomers. Nury, H., Dahout-Gonzalez, C., Trezeguet, V. et al. FEBS Lett (2005) 579:6031. DOI 10.1016/J.FEBSLET.2005.09.061 · PubMed
Other PDB entries of the same protein (UniProt P02722 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 2C3E directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.