5LLK: Human alpha-dystroglycan

Crystal structure of human alpha-dystroglycan. Determined by X-ray diffraction at 1.8 Å resolution. Released 12 Jul 2017.

Method
X-ray diffraction
Resolution
1.8 Å
Organism
Homo sapiens
Chains
1
Atoms
1,839
Mol. weight
28.68 kDa
Released
12 Jul 2017

Explore 5LLK in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5LLK contains 13 α-helices and 12 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: 13 helices, 12 β-strands

ElementResiduesLengthSheet
β-strand70-7341
β-strand78-8142
α-helix84-874
β-strand93-9861
α-helix104-1052
β-strand108-11142
β-strand116-11942
α-helix123-1253
β-strand127-138121
β-strand144-157141
α-helix1581
α-helix159-1613
α-helix182-1832
α-helix186-1872
β-strand188-19583
α-helix199-2013
α-helix204-21815
α-helix222-2243
β-strand225-22953
β-strand242-24543
β-strand256-26493
α-helix272-2732
α-helix275-2839
α-helix285-2906
β-strand294-30293

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
DystroglycanAprotein266Homo sapiensQ14118 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>5LLK_1 Dystroglycan (chains A)
GSSVLSDLHEAVPTVVGIPDGTAVVGRSFRVTIPTDLIASSGDIIKVSAAGKEALPSWLH
WDSQSHTLEGLPLDTDKGVHYISVSATRLGANGSHIPQTSSVFSIEVYPEDHSELQSVHT
ASPDPGEVVSSACAADEPVTVLTVILDADLTKMTPKQRIDLLHRMRSFSEVELHNMKLVP
VVNNRLFDMSAFMAGPGNAKKVVENGALLSWKLGCSLNQNSVPDIHGVEAPAREGAMSAQ
LGYPVVGWHIANKKPPLPKRVRRQIH

Primary citation

Structural flexibility of human alpha-dystroglycan. Covaceuszach, S., Bozzi, M., Bigotti, M.G. et al. FEBS Open Bio (2017) 7:1064-1077. DOI 10.1002/2211-5463.12259 · PubMed

Other PDB entries of the same protein (UniProt Q14118 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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