Crystal structure of a eukaryotic polyphosphate polymerase in complex with a phosphate polymer. Determined by X-ray diffraction at 2.64 Å resolution. Released 5 May 2009.
Explore 3G3Q in 3D Show helices and sheets RCSB PDB PDBe
3G3Q contains 30 α-helices and 22 β-strands across 2 chains. 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 | 194-203 | 10 | 1 |
| α-helix | 205-218 | 14 | |
| α-helix | 220 | 1 | |
| β-strand | 221 | 1 | 1 |
| α-helix | 222 | 1 | |
| α-helix | 229-230 | 2 | |
| α-helix | 232-235 | 4 | |
| β-strand | 236-243 | 8 | 1 |
| α-helix | 248-255 | 8 | |
| β-strand | 261-268 | 8 | 1 |
| β-strand | 275-282 | 8 | 1 |
| α-helix | 286-288 | 3 | |
| β-strand | 293-300 | 8 | 1 |
| α-helix | 301-303 | 3 | |
| α-helix | 304-309 | 6 | |
| α-helix | 314-322 | 9 | |
| α-helix | 329-348 | 20 | |
| β-strand | 352-364 | 13 | 1 |
| β-strand | 372-384 | 13 | 1 |
| α-helix | 414-416 | 3 | |
| β-strand | 417-419 | 3 | 1 |
| β-strand | 423-432 | 10 | 1 |
| α-helix | 439-445 | 7 | |
| β-strand | 451-452 | 2 | 1 |
| α-helix | 458-466 | 9 | |
| α-helix | 468-470 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Vacuolar transporter chaperone 4 | A, B | protein | 295 | Saccharomyces cerevisiae | P47075 (AlphaFold model) |
>3G3Q_1 Vacuolar transporter chaperone 4 (chains A, B) GAMGKQQNFVRQTTKYWVHPDNITELKLIILKHLPVLVFNTNKEFEREDSAITSIYFDNE NLDLYYGRLRKDEGAEAHRLRWYGGMSTDTIFVERKTHREDWTGEKSVKARFALKERHVN DFLKGKYTVDQVFAKMRKEGKKPMNEIENLEALASEIQYVMLKKKLRPVVRSFYNRTAFQ LPGDARVRISLDTELTMVREDNFDGVDRTHKNWRRTDIGVDWPFKQLDDKDICRFPYAVL EVKLQTQLGQEPPEWVRELVGSHLVEPVPKFSKFIHGVATLLNDKVDSIPFWLPQ
| ID | Name | Formula | Copies |
|---|---|---|---|
| PO4 | Phosphate ion | O4 P | 29 |
Water and common crystallization additives (SO4) are not listed.
Catalytic core of a membrane-associated eukaryotic polyphosphate polymerase. Hothorn, M., Neumann, H., Lenherr, E.D. et al. Science (2009) 324:513-516. DOI 10.1126/science.1168120 · PubMed
Other PDB entries of the same protein (UniProt P47075 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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