Crystal structure of a eukaryotic polyphosphate polymerase in complex with AppNHp-Mn2+. Determined by X-ray diffraction at 2.0 Å resolution. Released 5 May 2009.
Explore 3G3R in 3D Show helices and sheets RCSB PDB PDBe
3G3R contains 25 α-helices and 23 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 | 196-203 | 8 | 1 |
| α-helix | 208-216 | 9 | |
| α-helix | 220 | 1 | |
| β-strand | 221-223 | 3 | 1 |
| α-helix | 232-235 | 4 | |
| β-strand | 236-243 | 8 | 1 |
| α-helix | 248-255 | 8 | |
| β-strand | 261-268 | 8 | 1 |
| β-strand | 275-286 | 12 | 1 |
| β-strand | 289-300 | 12 | 1 |
| α-helix | 301-303 | 3 | |
| α-helix | 304-308 | 5 | |
| α-helix | 314-324 | 11 | |
| α-helix | 329-348 | 20 | |
| β-strand | 352-366 | 15 | 1 |
| β-strand | 369-384 | 16 | 1 |
| α-helix | 414-416 | 3 | |
| β-strand | 417-419 | 3 | 1 |
| β-strand | 423-430 | 8 | 1 |
| α-helix | 435-438 | 4 | |
| α-helix | 439-446 | 8 | |
| β-strand | 451-452 | 2 | 1 |
| α-helix | 458-466 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 194-203 | 10 | 2 |
| α-helix | 205-207 | 3 | |
| α-helix | 208-215 | 8 | |
| α-helix | 220 | 1 | |
| β-strand | 221 | 1 | 2 |
| β-strand | 222-224 | 3 | 1 |
| β-strand | 236-243 | 8 | 2 |
| α-helix | 248-255 | 8 | |
| β-strand | 261-268 | 8 | 2 |
| β-strand | 275-282 | 8 | 2 |
| α-helix | 286-288 | 3 | |
| β-strand | 293-300 | 8 | 2 |
| α-helix | 301-303 | 3 | |
| α-helix | 304-309 | 6 | |
| α-helix | 314-317 | 4 | |
| α-helix | 319-323 | 5 | |
| α-helix | 329-348 | 20 | |
| β-strand | 352-366 | 15 | 2 |
| β-strand | 369-384 | 16 | 2 |
| α-helix | 414-416 | 3 | |
| β-strand | 417-419 | 3 | 2 |
| β-strand | 423-432 | 10 | 2 |
| α-helix | 439-445 | 7 | |
| β-strand | 451-452 | 2 | 2 |
| α-helix | 458-466 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Vacuolar transporter chaperone 4 | A, B | protein | 295 | Saccharomyces cerevisiae | P47075 (AlphaFold model) |
>3G3R_1 Vacuolar transporter chaperone 4 (chains A, B) GAMGKQQNFVRQTTKYWVHPDNITELKLIILKHLPVLVFNTNKEFEREDSAITSIYFDNE NLDLYYGRLRKDEGAEAHRLRWYGGMSTDTIFVERKTHREDWTGEKSVKARFALKERHVN DFLKGKYTVDQVFAKMRKEGKKPMNEIENLEALASEIQYVMLKKKLRPVVRSFYNRTAFQ LPGDARVRISLDTELTMVREDNFDGVDRTHKNWRRTDIGVDWPFKQLDDKDICRFPYAVL EVKLQTQLGQEPPEWVRELVGSHLVEPVPKFSKFIHGVATLLNDKVDSIPFWLPQ
| ID | Name | Formula | Copies |
|---|---|---|---|
| MN | Manganese (II) ion | Mn | 2 |
| ANP | Phosphoaminophosphonic acid-adenylate ester | C10 H17 N6 O12 P3 | 2 |
Water and common crystallization additives (NA, 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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