Crystal structure of rA3G-ssDNA-AA. Determined by X-ray diffraction at 1.93 Å resolution. Released 6 Nov 2024.
Explore 8TVC in 3D Show helices and sheets RCSB PDB PDBe
8TVC contains 21 α-helices and 17 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 | 5-8 | 4 | |
| α-helix | 11 | 1 | |
| β-strand | 12 | 1 | 1 |
| α-helix | 13 | 1 | |
| α-helix | 14-21 | 8 | |
| β-strand | 32-40 | 9 | 2 |
| β-strand | 50-57 | 8 | 2 |
| α-helix | 62-64 | 3 | |
| α-helix | 66-79 | 14 | |
| β-strand | 86-94 | 9 | 2 |
| α-helix | 95-97 | 3 | |
| α-helix | 98-109 | 12 | |
| β-strand | 114-122 | 9 | 2 |
| α-helix | 129-140 | 12 | |
| β-strand | 148-151 | 4 | 2 |
| α-helix | 154-164 | 11 | |
| β-strand | 165 | 1 | 1 |
| α-helix | 170-172 | 3 | |
| α-helix | 178-193 | 16 | |
| β-strand | 197 | 1 | 3 |
| α-helix | 199-206 | 8 | |
| α-helix | 210-211 | 2 | |
| β-strand | 219-228 | 10 | 4 |
| β-strand | 231-234 | 4 | 4 |
| β-strand | 240-243 | 4 | 4 |
| β-strand | 245 | 1 | 5 |
| β-strand | 256 | 1 | 5 |
| α-helix | 258-268 | 11 | |
| β-strand | 276-284 | 9 | 4 |
| α-helix | 288-300 | 13 | |
| β-strand | 304-312 | 9 | 4 |
| α-helix | 320-329 | 10 | |
| β-strand | 333-336 | 4 | 4 |
| α-helix | 339-349 | 11 | |
| β-strand | 350 | 1 | 3 |
| α-helix | 355-357 | 3 | |
| α-helix | 359-360 | 2 | |
| α-helix | 363-378 | 16 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| DNA dC->dU-editing enzyme APOBEC-3G | A | protein | 386 | Macaca mulatta | Q7YR23 (AlphaFold model) |
| DNA 21-mer | B | DNA | 21 | synthetic construct |
>8TVC_1 DNA dC->dU-editing enzyme APOBEC-3G (chains A) GPGGSGGMKPQIRNMVEPMDPRTFVSNFNNRPILSGLDTVWLCCEVKTKDPSGPPLDAKI FQGKVYPKAKYHPEMRFLRWFHKWRQLHHDQEYKVTWYVSWSPCTRCANSVATFLAKDPK VTLTIFVARLYYFWKPDYQQALRILAEAGATMKIMNYNEFQDCWNKFVDGRGKPFKPWNN LPKHYTLLQATLGELLRHLMDPGTFTSNFNNKPWVSGQHETYLCYKVERLHNDTWVPLNQ HRGFLRNQAPNIHGFPKGRHAALCFLDLIPFWKLDGQQYRVTCFTSWSPCFSCAQEMAKF ISNNEHVSLCIFAARIYDDQGRYQEGLRTLHRDGAKIAMMNYSEFEYCWDTFVDRQGRPF QPWDGLDEHSQALSGRLRAILQNILQ
>8TVC_2 DNA 21-mer (chains B) TTTCCCGTGTCTGTCAATCTG
Molecular mechanism for regulating APOBEC3G DNA editing function by the non-catalytic domain. Yang, H., Pacheco, J., Kim, K. et al. Nat Commun (2024) 15:8773-8773. DOI 10.1038/s41467-024-52671-1 · PubMed
Other PDB entries of the same protein (UniProt Q7YR23 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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