5T2F: FHA1 domain of Rad53

Structure of the FHA1 domain of Rad53 bound to the BRCT domain of Dbf4. Determined by X-ray diffraction at 2.66 Å resolution. Released 15 Mar 2017.

Method
X-ray diffraction
Resolution
2.66 Å
Organisms
Saccharomyces cerevisiae, Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Chains
4
Atoms
7,719
Mol. weight
124.59 kDa
Released
15 Mar 2017

Explore 5T2F in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5T2F contains 40 α-helices and 63 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: 10 helices, 16 β-strands

ElementResiduesLengthSheet
α-helix106-12217
β-strand125-12841
α-helix142-15716
α-helix1601
β-strand161-16331
β-strand172-17541
α-helix179-1846
α-helix190-1967
β-strand200-20341
α-helix204-2129
β-strand239-24682
β-strand254-25852
α-helix260-2656
β-strand270-27783
β-strand284-28523
β-strand297-30263
α-helix303-3053
β-strand307-31153
β-strand318-31922
β-strand322-32322
α-helix324-3252
β-strand32613
β-strand330-33123
β-strand336-34052
β-strand349-35572
α-helix357-3604
Chain B: 11 helices, 15 β-strands
ElementResiduesLengthSheet
α-helix106-12318
β-strand125-12844
α-helix138-15720
β-strand161-16334
β-strand172-17434
α-helix182-1843
α-helix190-1967
β-strand200-20234
α-helix204-21310
α-helix2381
β-strand239-24685
β-strand254-25855
α-helix260-2656
β-strand272-27766
β-strand284-28526
β-strand297-30156
α-helix303-3053
β-strand307-31156
β-strand318-31925
β-strand322-32325
α-helix324-3252
β-strand330-33126
α-helix332-3332
β-strand336-34055
β-strand349-35575
α-helix357-3637
Chain C: 9 helices, 16 β-strands
ElementResiduesLengthSheet
α-helix106-12217
β-strand125-12847
α-helix138-15720
β-strand161-16337
β-strand172-17547
α-helix182-1843
α-helix190-1967
β-strand200-20347
α-helix204-21310
β-strand239-24688
β-strand254-25858
α-helix260-2656
β-strand270-27789
β-strand284-28529
β-strand297-30269
α-helix303-3053
β-strand306-31169
β-strand318-31928
β-strand322-32328
α-helix324-3252
β-strand32619
β-strand329-33139
β-strand336-34058
β-strand349-35578
α-helix357-3648
Chain D: 10 helices, 16 β-strands
ElementResiduesLengthSheet
α-helix106-12217
β-strand125-128410
α-helix140-15718
β-strand161-163310
β-strand172-175410
α-helix179-1813
α-helix190-1967
β-strand200-203410
α-helix204-2129
β-strand239-246811
β-strand254-258511
α-helix260-2656
β-strand272-277612
β-strand284-285212
β-strand297-301512
α-helix303-3053
β-strand307-311512
β-strand317-319311
β-strand322-323211
α-helix324-3252
β-strand326112
β-strand330-331212
β-strand337-340411
α-helix345-3473
β-strand349-355711
α-helix357-3648

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
DDK kinase regulatory subunit DBF4,Serine/threonine-protein kinase RAD53 chimeric proteinA, B, C, Dprotein269Saccharomyces cerevisiae, Saccharomyces cerevisiae (strain ATCC 204508 / S288c)P22216 (AlphaFold model), P32325 (AlphaFold model)
Sequence of entity 1 (A, B, C, D), FASTA
>5T2F_1 DDK kinase regulatory subunit DBF4,Serine/threonine-protein kinase RAD53 chimeric protein (chains A, B, C, D)
SHMTPKELLEWQTNWKKIMKRDSRIYFDITDDVEMNTYNKSKMDKRRDLLKRGFLTLGAQ
ITQFFDTTVTIVITRRSVENIYLLKDTDILSRAKKNYMKVWSYEKAARFLKNLDVDLDHV
DSGASGGSKFSQEQIGENIVCRVICTTGQIPIRDLSADISQVLKEKRSIKKVWTFGRNPA
CDYHLGNISRLSNKHFQILLGEDGNLLLNDISTNGTWLNGQKVEKNSNQLLSQGDEITVG
VGVESDILSLVIFINDKFKQCLEQNKVDR

Primary citation

'AND' logic gates at work: Crystal structure of Rad53 bound to Dbf4 and Cdc7. Almawi, A.W., Matthews, L.A., Myrox, P. et al. Sci Rep (2016) 6:34237-34237. DOI 10.1038/srep34237 · PubMed

Other PDB entries of the same protein (UniProt P22216 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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