5GOX: Eukaryotic Rad50 Functions as A Rod-shaped Dimer

Eukaryotic Rad50 Functions as A Rod-shaped Dimer. Determined by X-ray diffraction at 2.4 Å resolution. Released 1 Feb 2017.

Method: X-ray diffraction
Resolution: 2.4 Å
Organism: Homo sapiens
Chains: 2
Atoms: 2,980
Mol. weight: 44.09 kDa
Ligands: ZN
Released: 1 Feb 2017

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

Secondary structure: helices and β-sheets

5GOX contains 15 α-helices and 4 β-strands across 2 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

Element	Residues	Length	Sheet
α-helix	586-632	47
α-helix	638-673	36
β-strand	680	1	1
β-strand	687	1	1
α-helix	691-704	14
α-helix	708-731	24
α-helix	733-741	9
α-helix	742-746	5
α-helix	747-764	18

Chain B: 8 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	586-632	47
α-helix	638-673	36
β-strand	680	1	2
β-strand	687	1	2
α-helix	691-704	14
α-helix	708-732	25
α-helix	733-735	3
α-helix	736-741	6
α-helix	742-746	5
α-helix	747-764	18

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
DNA repair protein RAD50	A, B	protein	186	Homo sapiens	Q92878 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>5GOX_1 DNA repair protein RAD50 (chains A, B)
GSHMKEINQTRDRLAKLNKELASSEQNKNHINNELKRKEEQLSSYEDKLFDVCGSQDFES
DLDRLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEVISD
LQSKLRLAPDKLKSTESELKKKEKRRDEMLGLVPMRQSIIDLKEKEIPELRNKLQNVNRD
IQRLKN

Ligands and cofactors

ID	Name	Formula	Copies
ZN	Zinc ion	Zn	1

Water and common crystallization additives (GOL) are not listed.

Primary citation

Eukaryotic Rad50 functions as a rod-shaped dimer. Park, Y.B., Hohl, M., Padjasek, M. et al. Nat Struct Mol Biol (2017) 24:248-257. DOI 10.1038/nsmb.3369 · PubMed

Other PDB entries of the same protein (UniProt Q92878 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9Q9K 2.59 Å, Cryo-EM structure of human Mre11-Rad50 (MR) complex bound to DNA and telomeric factor…
9Q9J 2.71 Å, Cryo-EM structure of human Mre11-Rad50-Nbs1 (MRN) complex bound to DNA and telomeric…
9Q9I 2.79 Å, Cryo-EM structure of human Mre11-Rad50-Nbs1 complex bound to DNA
9Q9M 2.81 Å, Cryo-EM structure of human Mre11-Rad50-Nbs1 (MRN) complex bound to DNA and telomeric…
9Q9H 3.11 Å, Cryo-EM structure of human Mre11-Rad50 complex bound to DNA

Browse structure collections

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