Crystal structure of ColE7 translocation domain. Determined by X-ray diffraction at 1.7 Å resolution. Released 14 Mar 2006.
Explore 2AXC in 3D Show helices and sheets RCSB PDB PDBe
2AXC contains 13 α-helices and 20 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 | 80-82 | 3 | |
| β-strand | 83 | 1 | 1 |
| α-helix | 84 | 1 | |
| β-strand | 89-91 | 3 | 2 |
| β-strand | 94 | 1 | 3 |
| β-strand | 97 | 1 | 3 |
| β-strand | 98-102 | 5 | 4 |
| α-helix | 105-108 | 4 | |
| α-helix | 109-116 | 8 | |
| β-strand | 127-134 | 8 | 5 |
| α-helix | 136-142 | 7 | |
| β-strand | 149-155 | 7 | 2 |
| α-helix | 156-158 | 3 | |
| α-helix | 164-166 | 3 | |
| β-strand | 173-176 | 4 | 6 |
| β-strand | 179-185 | 7 | 5 |
| β-strand | 188-195 | 8 | 5 |
| β-strand | 199-202 | 4 | 6 |
| β-strand | 203-205 | 3 | 2 |
| β-strand | 207-208 | 2 | 4 |
| β-strand | 214-219 | 6 | 4 |
| β-strand | 222-229 | 8 | 4 |
| β-strand | 236 | 1 | 1 |
| α-helix | 238-240 | 3 | |
| β-strand | 243-245 | 3 | 5 |
| α-helix | 246-247 | 2 | |
| β-strand | 252-253 | 2 | 5 |
| β-strand | 262-268 | 7 | 2 |
| α-helix | 269-270 | 2 | |
| α-helix | 271-273 | 3 | |
| α-helix | 275-277 | 3 | |
| β-strand | 278-284 | 7 | 2 |
| α-helix | 288-307 | 20 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Colicin E7 | A | protein | 264 | Escherichia coli str. K12 substr. | Q47112 (AlphaFold model) |
>2AXC_1 Colicin E7 (chains A) MRGSRSGHGNGGGNSNSGGGSNSSVAAPMAFGFPALAAPGAGTLGISVSGEALSAAIADI FAALKGPFKFSAWGIALYGILPSEIAKDDPNMMSKIVTSLPAETVTNVQVSTLPLDQATV SVTKRVTDVVKDTRQHIAVVAGVPMSVPVVNAKPTRTPGVFHASFPGVPSLTVSTVKGLP VSTTLPRGITEDKGRTAVPAGFTFGGGSHEAVIRFPKESGQKPVYVSVTDVLTPAQVKQR QDEEKRLQQEWNDAHPVEVAERRS
High-resolution crystal structure of a truncated ColE7 translocation domain: implications for colicin transport across membranes. Cheng, Y.S., Shi, Z., Doudeva, L.G. et al. J Mol Biol (2006) 356:22-31. DOI 10.1016/j.jmb.2005.11.056 · PubMed
Other PDB entries of the same protein (UniProt Q47112 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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