28QM: MBP

MBP bound to distal DARPin (AHIR dodecamer scaffold system). Determined by electron microscopy at 3.4 Å resolution. Released 25 Feb 2026.

Method
Electron microscopy
Resolution
3.4 Å
Organisms
Homo sapiens, synthetic construct
Chains
2
Atoms
4,034
Mol. weight
57.9 kDa
Ligands
EOH
Released
25 Feb 2026

Explore 28QM in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 20 helices, 27 β-strands

ElementResiduesLengthSheet
β-strand8-1141
α-helix18-3114
β-strand36-3941
α-helix44-529
β-strand60-6451
α-helix65-739
β-strand7712
α-helix84-874
β-strand9013
α-helix92-954
β-strand99-10024
β-strand103-10424
β-strand106-11271
β-strand115-11955
β-strand12916
α-helix132-14110
β-strand14617
α-helix155-16410
β-strand16818
β-strand17119
β-strand17819
β-strand18318
α-helix187-20115
α-helix211-2199
β-strand22317
β-strand225-22845
α-helix230-2323
α-helix233-2397
β-strand243-24645
α-helix247-2493
β-strand25016
β-strand251110
β-strand254110
β-strand259-260211
β-strand261-26771
β-strand26812
α-helix274-2796
α-helix280-2856
α-helix288-29710
β-strand302-30321
β-strand30513
α-helix306-3127
α-helix316-32712
β-strand329-330211
α-helix331-3322
α-helix337-35317
α-helix358-36912
Chain B: 11 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix14-2411
α-helix27-337
α-helix50-578
α-helix60-689
α-helix83-908
α-helix93-1019
α-helix116-1238
α-helix126-1349
α-helix149-1557
α-helix159-1646
α-helix165-1695

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Maltose-binding periplasmic protein,PigGAprotein373Homo sapiensA0ACD6BAW2
DARPinBprotein159synthetic construct
Sequence of entity 1 (A), FASTA
>28QM_1 Maltose-binding periplasmic protein,PigG (chains A)
KIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDII
FWAHDRFGGYAQSGLLAEITPAAAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKD
LLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDIKD
VGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSAV
NYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLG
AVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDAA
LAAAQTNGSHHAH
Sequence of entity 2 (B), FASTA
>28QM_2 DARPin (chains B)
DLGRKLLEAARAGQDDEVRILMANGADVNAADNTGTTPLHLAAYSGHLEIVEVLLKHGAD
VDASDVFGYTPLHLAAYWGHLEIVEVLLKNGADVNAMDSDGMTPLHLAAKWGYLEIVEVL
LKHGADVNAQDKFGKTPKDLARDNGNQWIYELLEAAGRA

Ligands and cofactors

IDNameFormulaCopies
EOHEthanolC2 H6 O1

Primary citation

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:

Browse structure collections

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