MBP bound to distal DARPin (AHIR dodecamer scaffold system). Determined by electron microscopy at 3.4 Å resolution. Released 25 Feb 2026.
Explore 28QM in 3D Show helices and sheets RCSB PDB PDBe
28QM contains 31 α-helices and 27 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 | 8-11 | 4 | 1 |
| α-helix | 18-31 | 14 | |
| β-strand | 36-39 | 4 | 1 |
| α-helix | 44-52 | 9 | |
| β-strand | 60-64 | 5 | 1 |
| α-helix | 65-73 | 9 | |
| β-strand | 77 | 1 | 2 |
| α-helix | 84-87 | 4 | |
| β-strand | 90 | 1 | 3 |
| α-helix | 92-95 | 4 | |
| β-strand | 99-100 | 2 | 4 |
| β-strand | 103-104 | 2 | 4 |
| β-strand | 106-112 | 7 | 1 |
| β-strand | 115-119 | 5 | 5 |
| β-strand | 129 | 1 | 6 |
| α-helix | 132-141 | 10 | |
| β-strand | 146 | 1 | 7 |
| α-helix | 155-164 | 10 | |
| β-strand | 168 | 1 | 8 |
| β-strand | 171 | 1 | 9 |
| β-strand | 178 | 1 | 9 |
| β-strand | 183 | 1 | 8 |
| α-helix | 187-201 | 15 | |
| α-helix | 211-219 | 9 | |
| β-strand | 223 | 1 | 7 |
| β-strand | 225-228 | 4 | 5 |
| α-helix | 230-232 | 3 | |
| α-helix | 233-239 | 7 | |
| β-strand | 243-246 | 4 | 5 |
| α-helix | 247-249 | 3 | |
| β-strand | 250 | 1 | 6 |
| β-strand | 251 | 1 | 10 |
| β-strand | 254 | 1 | 10 |
| β-strand | 259-260 | 2 | 11 |
| β-strand | 261-267 | 7 | 1 |
| β-strand | 268 | 1 | 2 |
| α-helix | 274-279 | 6 | |
| α-helix | 280-285 | 6 | |
| α-helix | 288-297 | 10 | |
| β-strand | 302-303 | 2 | 1 |
| β-strand | 305 | 1 | 3 |
| α-helix | 306-312 | 7 | |
| α-helix | 316-327 | 12 | |
| β-strand | 329-330 | 2 | 11 |
| α-helix | 331-332 | 2 | |
| α-helix | 337-353 | 17 | |
| α-helix | 358-369 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 14-24 | 11 | |
| α-helix | 27-33 | 7 | |
| α-helix | 50-57 | 8 | |
| α-helix | 60-68 | 9 | |
| α-helix | 83-90 | 8 | |
| α-helix | 93-101 | 9 | |
| α-helix | 116-123 | 8 | |
| α-helix | 126-134 | 9 | |
| α-helix | 149-155 | 7 | |
| α-helix | 159-164 | 6 | |
| α-helix | 165-169 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Maltose-binding periplasmic protein,PigG | A | protein | 373 | Homo sapiens | A0ACD6BAW2 |
| DARPin | B | protein | 159 | synthetic construct |
>28QM_1 Maltose-binding periplasmic protein,PigG (chains A) KIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDII FWAHDRFGGYAQSGLLAEITPAAAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKD LLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDIKD VGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSAV NYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLG AVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDAA LAAAQTNGSHHAH
>28QM_2 DARPin (chains B) DLGRKLLEAARAGQDDEVRILMANGADVNAADNTGTTPLHLAAYSGHLEIVEVLLKHGAD VDASDVFGYTPLHLAAYWGHLEIVEVLLKNGADVNAMDSDGMTPLHLAAKWGYLEIVEVL LKHGADVNAQDKFGKTPKDLARDNGNQWIYELLEAAGRA
| ID | Name | Formula | Copies |
|---|---|---|---|
| EOH | Ethanol | C2 H6 O | 1 |
An engineered symmetrical scaffold system enables high resolution imaging of small cargo proteins by cryo-electron microscopy. Ferreira, D.S.M., Noble, M., Rowland, R.J. et al. To be published.
Other PDB entries of the same protein (UniProt A0ACD6BAW2), best resolution first:
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