2MH9: Bloom syndrome protein

Resonance assignment of RQC domain of human Bloom syndrome protein. Determined by solution NMR. Released 29 Oct 2014.

Method
Solution NMR
Organism
Homo sapiens
Chains
1
Atoms
1,002
Mol. weight
16.12 kDa
Released
29 Oct 2014

Explore 2MH9 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2MH9 contains 5 α-helices and 7 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: 5 helices, 7 β-strands

ElementResiduesLengthSheet
β-strand211
β-strand511
β-strand9-1022
α-helix13-2412
α-helix30-323
β-strand4413
α-helix45-539
α-helix73-8614
β-strand90-9673
β-strand100-10673
α-helix111-1166
β-strand122-12322

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Bloom syndrome proteinAprotein144Homo sapiensP54132 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2MH9_1 Bloom syndrome protein (chains A)
CKTKDYKTRDVTDDVKSIVRFVQEHSSSQGMRNIKHVGPSGRFTMNMLVDIFLGSKSAKI
QSGIFGKGSAYSRHNAERLFKKLILDKILDEDLYINANDQAIAYVMLGNKAQTVLNGNLK
VDFMETENSSSVKKQKALVAKVSQ

Primary citation

Solution structure of the RecQ C-terminal domain of human Bloom syndrome protein. Park, C.J., Ko, J., Ryu, K.S. et al. J Biomol NMR (2014) 58:141-147. DOI 10.1007/s10858-014-9812-8 · PubMed

Other PDB entries of the same protein (UniProt P54132 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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