7ZQY: Chaetomium thermophilum Rad50 Zn hook

Chaetomium thermophilum Rad50 Zn hook. Determined by X-ray diffraction at 2.51 Å resolution. Released 28 Dec 2022.

Method
X-ray diffraction
Resolution
2.51 Å
Organism
Thermochaetoides thermophila
Chains
4
Atoms
5,801
Mol. weight
83.67 kDa
Ligands
ZN
Released
28 Dec 2022

Explore 7ZQY in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7ZQY contains 28 α-helices and 8 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: 7 helices, 2 β-strands

ElementResiduesLengthSheet
α-helix603-63836
α-helix644-6463
α-helix647-6493
α-helix650-68839
β-strand69011
β-strand69711
α-helix702-71514
α-helix719-74022
α-helix742-77231
Chain B: 7 helices, 2 β-strands
ElementResiduesLengthSheet
α-helix601-63838
α-helix644-6463
α-helix647-6493
α-helix650-68839
β-strand690-69122
β-strand696-69722
α-helix702-71413
α-helix718-74023
α-helix742-77534
Chain C: 7 helices, 2 β-strands
ElementResiduesLengthSheet
α-helix601-63838
α-helix644-6463
α-helix647-6493
α-helix650-68839
β-strand69013
β-strand69713
α-helix702-71312
α-helix719-74022
α-helix742-77231
Chain D: 7 helices, 2 β-strands
ElementResiduesLengthSheet
α-helix601-63838
α-helix644-6463
α-helix647-6493
α-helix650-68839
β-strand69014
β-strand69714
α-helix702-71514
α-helix719-74022
α-helix742-77433

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
DH domain-containing proteinA, B, C, Dprotein177Thermochaetoides thermophilaG0SHW7 (AlphaFold model)
Sequence of entity 1 (A, B, C, D), FASTA
>7ZQY_1 DH domain-containing protein (chains A, B, C, D)
QQELKQAEYQLSNARNLHNKLTNEMEACMRAVQTAMKEARDLDSAPPVDEYITMLETDEK
ELAEVETALKLYDELKKHYSTIKDRALRFNKCYICDRDFTNQEAAKTRLLEKVAKRLGDE
EKKELLEDQAAFMKSLDILRAVRVKYDTYQRLSSELPQLSREIDSETNRREDLVRRL

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn2

Primary citation

Cryo-EM structure of the Mre11-Rad50-Nbs1 complex reveals the molecular mechanism of scaffolding functions. Rotheneder, M., Stakyte, K., van de Logt, E. et al. Mol Cell (2023) 83:167-185.e9. DOI 10.1016/j.molcel.2022.12.003 · PubMed

Other PDB entries of the same protein (UniProt G0SHW7 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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