5MK5: DHBN domain of human BLM helicase

Structures of DHBN domain of human BLM helicase. Determined by X-ray diffraction at 2.16 Å resolution. Released 1 Mar 2017.

Method
X-ray diffraction
Resolution
2.16 Å
Organism
Homo sapiens
Chains
4
Atoms
1,830
Mol. weight
28.22 kDa
Released
1 Mar 2017

Explore 5MK5 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5MK5 contains 12 α-helices and 0 β-strands across 4 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: 3 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix365-38420
α-helix388-3914
α-helix397-41115
Chain B: 3 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix363-38422
α-helix388-3914
α-helix397-41115
Chain C: 3 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix363-38321
α-helix388-3914
α-helix397-41115
Chain D: 3 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix366-38520
α-helix388-3914
α-helix397-41014

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Bloom syndrome proteinA, B, C, Dprotein54Homo sapiensP54132 (AlphaFold model)
Sequence of entity 1 (A, B, C, D), FASTA
>5MK5_1 Bloom syndrome protein (chains A, B, C, D)
MDARQISLQQQLIHVMEHICKLIDTIPDDKLKLLDCGNELLQQRNIRRKLLTEV

Primary citation

A helical bundle in the N-terminal domain of the BLM helicase mediates dimer and potentially hexamer formation. Shi, J., Chen, W.F., Zhang, B. et al. J Biol Chem (2017) 292:5909-5920. DOI 10.1074/jbc.M116.761510 · PubMed

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

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