3Q28: PDB entry 3Q28

Cyrstal structure of human alpha-synuclein (58-79) fused to maltose binding protein (MBP). Determined by X-ray diffraction at 1.6 Å resolution. Released 1 Jun 2011.

Method
X-ray diffraction
Resolution
1.6 Å
Organisms
Escherichia coli, Homo sapiens
Chains
1
Atoms
3,405
Mol. weight
43.63 kDa
Released
1 Jun 2011

Explore 3Q28 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3Q28 contains 27 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.

Chain A: 27 helices, 24 β-strands

ElementResiduesLengthSheet
α-helix41
β-strand8-1141
α-helix18-3215
β-strand36-3941
α-helix44-529
β-strand60-6451
α-helix65-673
α-helix68-736
β-strand7712
α-helix78-803
α-helix84-874
β-strand9013
α-helix92-976
β-strand99-10024
β-strand103-10424
β-strand107-11261
β-strand115-11955
β-strand12916
α-helix133-1419
β-strand146-14835
α-helix155-1573
α-helix159-1646
β-strand168-17367
β-strand176-18387
α-helix187-20115
α-helix211-22010
β-strand223-22865
α-helix230-2323
α-helix233-2386
β-strand243-24645
α-helix247-2493
β-strand25016
β-strand25118
β-strand25418
α-helix255-2562
α-helix2581
β-strand259-26029
β-strand261-26771
β-strand26812
α-helix274-2807
α-helix281-2855
α-helix288-29710
β-strand302-30321
β-strand30513
α-helix306-3127
α-helix316-32712
β-strand329-33029
α-helix331-3322
α-helix337-35317
α-helix358-36912
α-helix380-3823

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Maltose-binding periplasmic protein/alpha-synuclein chimeric proteinAprotein393Escherichia coli, Homo sapiensP0AEX9 (AlphaFold model), P37840 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>3Q28_1 Maltose-binding periplasmic protein/alpha-synuclein chimeric protein (chains A)
MKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDI
IFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNK
DLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDIK
DVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSK
VNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPL
GAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDE
ALKDAQTNSSSKTKEQVTNVGGAVVTGVTAVAQ

Primary citation

Structures of segments of alpha-synuclein fused to maltose-binding protein suggest intermediate states during amyloid formation. Zhao, M., Cascio, D., Sawaya, M.R. et al. Protein Sci (2011) 20:996-1004. DOI 10.1002/pro.630 · PubMed

Other PDB entries of the same protein (UniProt P0AEX9 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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