6HM5: TOPBP1 BRCT0,1,2

Crystal structure of TOPBP1 BRCT0,1,2 in complex with a RAD9 phosphopeptide. Determined by X-ray diffraction at 2.33 Å resolution. Released 17 Oct 2018.

Method
X-ray diffraction
Resolution
2.33 Å
Organisms
Gallus gallus, Homo sapiens
Chains
2
Atoms
2,114
Mol. weight
34.37 kDa
Released
17 Oct 2018

Explore 6HM5 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6HM5 contains 13 α-helices and 16 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: 13 helices, 15 β-strands

ElementResiduesLengthSheet
β-strand11-1441
α-helix21-277
β-strand39-4241
α-helix44-485
β-strand57-5931
α-helix66-749
β-strand77-7931
α-helix81-877
β-strand10111
β-strand110-11452
α-helix118-13013
β-strand134-13522
β-strand139-14023
β-strand145-14842
α-helix154-1618
β-strand166-16722
α-helix169-18113
α-helix186-1883
α-helix191-1944
β-strand19512
α-helix196-1972
β-strand203-20754
α-helix211-22313
β-strand227-22824
β-strand239-24244
β-strand259-26134
α-helix263-27210
α-helix278-2814
Chain B: 0 helices, 1 β-strand
ElementResiduesLengthSheet
β-strand382-38433

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
DNA topoisomerase II binding protein 1Aprotein290Gallus gallusA0A1D5P3M9
Cell cycle checkpoint control protein RAD9ABprotein11Homo sapiensQ99638 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>6HM5_1 DNA topoisomerase II binding protein 1 (chains A)
RMKGSKEVFLVKFVKSSGSSEYFLKALESIKEFQSEEHLQILEEEAALNIKENDKSLYIC
DPFTGVVFNHLKKLGCRIVGPQVVLYCMQSQRCVPRAEYPVYNMTMADVTISCTTLDKDV
REEVHKYVQMMGGRVYRDLNMSVTHLIAGEVGSKKYLVAASLKKPVLLPSWVKTLWDKSQ
QRMMRYTDVNMEDYACPVFLGCTICVTGLSSSDRKEVQRLTAEHGGQYSGQLKMNECTHL
IVQEPKGQKYECAKKWNVHCVPVQWFSDSIEKGFCQDETMYKIESGSKLS
Sequence of entity 2 (B), FASTA
>6HM5_2 Cell cycle checkpoint control protein RAD9A (chains B)
SPVLAEDSEGE

Primary citation

BRCT domains of the DNA damage checkpoint proteins TOPBP1/Rad4 display distinct specificities for phosphopeptide ligands. Day, M., Rappas, M., Ptasinska, K. et al. Elife (2018) 7. DOI 10.7554/eLife.39979 · PubMed

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