3T7K: Regulator of Ty1 transposition protein 107

Complex structure of Rtt107p and phosphorylated histone H2A. Determined by X-ray diffraction at 2.03 Å resolution. Released 15 Feb 2012.

Method
X-ray diffraction
Resolution
2.03 Å
Organism
Saccharomyces cerevisiae
Chains
4
Atoms
3,972
Mol. weight
60.63 kDa
Released
15 Feb 2012

Explore 3T7K in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3T7K contains 28 α-helices and 24 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.

Chains A and B: 13 helices, 11 β-strands

ElementResiduesLengthSheet
α-helix822-8276
β-strand837-84151
α-helix851-8599
β-strand862-86431
α-helix870-8723
β-strand876-87831
β-strand88512
α-helix886-8916
β-strand899-90131
α-helix904-91310
β-strand93111
α-helix9321
α-helix937-9426
α-helix949-9524
β-strand957-96153
α-helix968-97710
β-strand982-98653
α-helix993-9953
α-helix996-9983
β-strand1012-101543
α-helix1019-103214
β-strand1038-104143
α-helix1043-10519
β-strand1063-106753
Chains C and D: 1 helix, 1 β-strand
ElementResiduesLengthSheet
α-helix129-1302
β-strand13112

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Regulator of Ty1 transposition protein 107A, Bprotein256Saccharomyces cerevisiaeP38850 (AlphaFold model)
Histone H2A.1C, Dprotein8Saccharomyces cerevisiaeP04911 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>3T7K_1 Regulator of Ty1 transposition protein 107 (chains A, B)
GSPHMTKAEKILARFNELPNYDLKAVCTGCFHDGFNEVDIEILNQLGIKIFDNIKETDKL
NCIFAPKILRTEKFLKSLSFEPLKFALKPEFIIDLLKQIHSKKDKLSQININLFDYEING
INESIISKTKLPTKVFERANIRCINLVNDIPGGVDTIGSVLKAHGIEKINVLRSKKCTFE
DIIPNDVSKQENGGIFKYVLIVTKASQVKKFTKLINDRDKNETILIVEWNWCVESIFHLN
VDFTSKKNVLYQKKNN
Sequence of entity 2 (C, D), FASTA
>3T7K_2 Histone H2A.1 (chains C, D)
ATKASQEL

Primary citation

Structure of C-terminal Tandem BRCT Repeats of Rtt107 Protein Reveals Critical Role in Interaction with Phosphorylated Histone H2A during DNA Damage Repair. Li, X., Liu, K., Li, F. et al. J Biol Chem (2012) 287:9137-9146. DOI 10.1074/jbc.M111.311860 · PubMed

Other PDB entries of the same protein (UniProt P38850 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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