Complex structure of Rtt107p and phosphorylated histone H2A. Determined by X-ray diffraction at 2.03 Å resolution. Released 15 Feb 2012.
Explore 3T7K in 3D Show helices and sheets RCSB PDB PDBe
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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 822-827 | 6 | |
| β-strand | 837-841 | 5 | 1 |
| α-helix | 851-859 | 9 | |
| β-strand | 862-864 | 3 | 1 |
| α-helix | 870-872 | 3 | |
| β-strand | 876-878 | 3 | 1 |
| β-strand | 885 | 1 | 2 |
| α-helix | 886-891 | 6 | |
| β-strand | 899-901 | 3 | 1 |
| α-helix | 904-913 | 10 | |
| β-strand | 931 | 1 | 1 |
| α-helix | 932 | 1 | |
| α-helix | 937-942 | 6 | |
| α-helix | 949-952 | 4 | |
| β-strand | 957-961 | 5 | 3 |
| α-helix | 968-977 | 10 | |
| β-strand | 982-986 | 5 | 3 |
| α-helix | 993-995 | 3 | |
| α-helix | 996-998 | 3 | |
| β-strand | 1012-1015 | 4 | 3 |
| α-helix | 1019-1032 | 14 | |
| β-strand | 1038-1041 | 4 | 3 |
| α-helix | 1043-1051 | 9 | |
| β-strand | 1063-1067 | 5 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 129-130 | 2 | |
| β-strand | 131 | 1 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Regulator of Ty1 transposition protein 107 | A, B | protein | 256 | Saccharomyces cerevisiae | P38850 (AlphaFold model) |
| Histone H2A.1 | C, D | protein | 8 | Saccharomyces cerevisiae | P04911 (AlphaFold model) |
>3T7K_1 Regulator of Ty1 transposition protein 107 (chains A, B) GSPHMTKAEKILARFNELPNYDLKAVCTGCFHDGFNEVDIEILNQLGIKIFDNIKETDKL NCIFAPKILRTEKFLKSLSFEPLKFALKPEFIIDLLKQIHSKKDKLSQININLFDYEING INESIISKTKLPTKVFERANIRCINLVNDIPGGVDTIGSVLKAHGIEKINVLRSKKCTFE DIIPNDVSKQENGGIFKYVLIVTKASQVKKFTKLINDRDKNETILIVEWNWCVESIFHLN VDFTSKKNVLYQKKNN
>3T7K_2 Histone H2A.1 (chains C, D) ATKASQEL
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:
MolViewer shows 3T7K directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.