Structure, interaction, and real-time monitoring of the enzymatic reaction of wild type APOBEC3G. Determined by solution NMR. Released 3 Feb 2009.
Explore 2KBO in 3D Show helices and sheets RCSB PDB PDBe
2KBO contains 8 α-helices and 5 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 | 9-14 | 6 | |
| β-strand | 31-38 | 8 | 1 |
| β-strand | 41-42 | 2 | 1 |
| α-helix | 68-79 | 12 | |
| β-strand | 86-92 | 7 | 1 |
| α-helix | 99-106 | 8 | |
| α-helix | 107-111 | 5 | |
| β-strand | 115-121 | 7 | 1 |
| α-helix | 130-132 | 3 | |
| α-helix | 133-141 | 9 | |
| β-strand | 143-147 | 5 | 1 |
| α-helix | 150-160 | 11 | |
| α-helix | 174-189 | 16 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| DNA dC->dU-editing enzyme APOBEC-3G | A | protein | 194 | Homo sapiens | Q9HC16 (AlphaFold model) |
>2KBO_1 DNA dC->dU-editing enzyme APOBEC-3G (chains A) HMLRHSMDPPTFTFNFNNEPWVRGRHETYLCYEVERMHNDTWVLLNQRRGFLCNQAPHKH GFLEGRHAELCFLDVIPFWKLDLDQDYRVTCFTSWSPCFSCAQEMAKFISKNKHVSLCIF TARIYDDQGRCQEGLRTLAEAGAKISIMTYSEFKHCWDTFVDHQGCPFQPWDGLDEHSQD LSGRLRAILQNQEN
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 1 |
Structure, interaction and real-time monitoring of the enzymatic reaction of wild-type APOBEC3G. Furukawa, A., Nagata, T., Matsugami, A. et al. EMBO J (2009) 28:440-451. DOI 10.1038/emboj.2008.290 · PubMed
Other PDB entries of the same protein (UniProt Q9HC16 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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