Crystal structure of human 5' exonuclease Appollo H61Y variant. Determined by X-ray diffraction at 3.1 Å resolution. Released 20 Jan 2021.
Explore 7B2X in 3D Show helices and sheets RCSB PDB PDBe
7B2X contains 13 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 |
|---|---|---|---|
| β-strand | 4-6 | 3 | 1 |
| β-strand | 11-13 | 3 | 1 |
| β-strand | 26-28 | 3 | 1 |
| α-helix | 34-36 | 3 | |
| β-strand | 48-50 | 3 | 1 |
| α-helix | 52-62 | 11 | |
| α-helix | 66-68 | 3 | |
| β-strand | 69-71 | 3 | 1 |
| β-strand | 77-81 | 5 | 2 |
| β-strand | 89-96 | 8 | 2 |
| β-strand | 104-110 | 7 | 2 |
| β-strand | 113-117 | 5 | 2 |
| α-helix | 125-129 | 5 | |
| β-strand | 141-144 | 4 | 2 |
| α-helix | 147-149 | 3 | |
| α-helix | 158-171 | 14 | |
| β-strand | 176-181 | 6 | 3 |
| α-helix | 187-197 | 11 | |
| β-strand | 201-202 | 2 | 3 |
| α-helix | 205-214 | 10 | |
| β-strand | 220-221 | 2 | 3 |
| α-helix | 224-226 | 3 | |
| β-strand | 229-233 | 5 | 3 |
| α-helix | 234-236 | 3 | |
| α-helix | 239-246 | 8 | |
| β-strand | 251-257 | 7 | 3 |
| β-strand | 268-272 | 5 | 3 |
| α-helix | 279-289 | 11 | |
| β-strand | 294-296 | 3 | 2 |
| α-helix | 321-327 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| 5' exonuclease Apollo | A | protein | 339 | Homo sapiens | Q9H816 (AlphaFold model) |
>7B2X_1 5' exonuclease Apollo (chains A) SMGYGNGVLIPHTPIAVDFWSLRRAGTARLFFLSHMHSDHTVGLSSTWARPLYCSPITAH LLHRYLQVSKQWIQALEVGESHVLPLDEIGQETMTVTLLDANHCPGSVMFLFEGYFGTIL YTGDFRYTPSMLKEPALTLGKQIHTLYLDNTNCNPALVLPSRQEAAHQIVQLIRKHPQHN IKIGLYSLGKESLLEQLALEFQTWVVLSPRRLELVQLLGLADVFTVEEKAGRIHAVDHME ICHSNMLRWNQTHPTIAILPTSRKIHSSHPDIHVIPYSDHSSYSELRAFVAALKPCQVVP IVSRRPCGGFQDSLSPRISVPLIPDSVQQYMSSSSRKPS
| ID | Name | Formula | Copies |
|---|---|---|---|
| NI | Nickel (II) ion | Ni | 1 |
A phosphate binding pocket is a key determinant of exo- versus endo-nucleolytic activity in the SNM1 nuclease family. Baddock, H.T., Newman, J.A., Yosaatmadja, Y. et al. Nucleic Acids Res (2021) 49:9294-9309. DOI 10.1093/nar/gkab692 · PubMed
Other PDB entries of the same protein (UniProt Q9H816 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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