Structure of the C-terminal domain of the Menangle virus phosphoprotein (residues 329 -388), fused to MBP. Space group P212121. Determined by X-ray diffraction at 1.55 Å resolution. Released 6 Oct 2021.
Explore 7KD5 in 3D Show helices and sheets RCSB PDB PDBe
7KD5 contains 29 α-helices and 24 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 | 7-10 | 4 | 1 |
| α-helix | 17-31 | 15 | |
| β-strand | 35-38 | 4 | 1 |
| α-helix | 43-51 | 9 | |
| β-strand | 59-63 | 5 | 1 |
| α-helix | 64-66 | 3 | |
| α-helix | 67-72 | 6 | |
| β-strand | 76 | 1 | 2 |
| α-helix | 77-79 | 3 | |
| α-helix | 83-86 | 4 | |
| β-strand | 89 | 1 | 3 |
| α-helix | 91-96 | 6 | |
| β-strand | 98-99 | 2 | 4 |
| β-strand | 102-103 | 2 | 4 |
| β-strand | 106-111 | 6 | 1 |
| β-strand | 114-118 | 5 | 5 |
| β-strand | 128 | 1 | 6 |
| α-helix | 129-131 | 3 | |
| α-helix | 132-140 | 9 | |
| β-strand | 145-147 | 3 | 5 |
| α-helix | 154-156 | 3 | |
| α-helix | 158-163 | 6 | |
| β-strand | 167-172 | 6 | 7 |
| β-strand | 175-182 | 8 | 7 |
| α-helix | 186-200 | 15 | |
| α-helix | 210-218 | 9 | |
| β-strand | 222-227 | 6 | 5 |
| α-helix | 229-231 | 3 | |
| α-helix | 232-237 | 6 | |
| β-strand | 242-245 | 4 | 5 |
| α-helix | 246-248 | 3 | |
| β-strand | 249 | 1 | 6 |
| β-strand | 250 | 1 | 8 |
| β-strand | 253 | 1 | 8 |
| α-helix | 257 | 1 | |
| β-strand | 258-259 | 2 | 9 |
| β-strand | 260-266 | 7 | 1 |
| β-strand | 267 | 1 | 2 |
| α-helix | 273-279 | 7 | |
| α-helix | 280-284 | 5 | |
| α-helix | 287-296 | 10 | |
| β-strand | 301-302 | 2 | 1 |
| β-strand | 304 | 1 | 3 |
| α-helix | 305-311 | 7 | |
| α-helix | 315-326 | 12 | |
| β-strand | 328-329 | 2 | 9 |
| α-helix | 330-331 | 2 | |
| α-helix | 336-351 | 16 | |
| α-helix | 357-368 | 12 | |
| α-helix | 1331-1334 | 4 | |
| α-helix | 1335-1352 | 18 | |
| α-helix | 1356-1366 | 11 | |
| α-helix | 1372-1383 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Maltodextrin-binding protein and Phosphoprotein fusion protein | A | protein | 431 | Serratia sp. (strain FS14), Menangle virus | A0ACD6BAW2 |
>7KD5_1 Maltodextrin-binding protein and Phosphoprotein fusion protein (chains A) MKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDI IFWAHDRFGGYAQSGLLAEITPAAAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNK DLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDIK DVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSK VNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPL GAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDA ALAAAQTNAAAKSSAASPAALSGYKMTLLALIKESIPNQAKRQKFEMQVGGIRNEQDFKN LRREIIRSAAQ
| ID | Name | Formula | Copies |
|---|---|---|---|
| PIN | Piperazine-n,n'-BIS(2-ethanesulfonic acid) | C8 H18 N2 O6 S2 | 3 |
| PRO | Proline | C5 H9 N O2 | 1 |
Water and common crystallization additives (EDO) are not listed.
Structural Analysis of the Menangle Virus P Protein Reveals a Soft Boundary between Ordered and Disordered Regions. Webby, M.N., Herr, N., Bulloch, E.M.M. et al. Viruses (2021) 13. DOI 10.3390/v13091737 · PubMed
Other PDB entries of the same protein (UniProt A0ACD6BAW2), best resolution first:
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