The crystal structure of MDC1 BRCT T2067D in complex with a minimal recognition tetrapeptide with an amidated C-terminus. Determined by X-ray diffraction at 1.33 Å resolution. Released 2 Mar 2010.
Explore 3K05 in 3D Show helices and sheets RCSB PDB PDBe
3K05 contains 30 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 |
|---|---|---|---|
| β-strand | 1894-1897 | 4 | 1 |
| α-helix | 1903-1911 | 9 | |
| β-strand | 1915-1916 | 2 | 1 |
| α-helix | 1920-1922 | 3 | |
| β-strand | 1925-1927 | 3 | 1 |
| β-strand | 1934 | 1 | 2 |
| α-helix | 1935-1943 | 9 | |
| β-strand | 1947-1948 | 2 | 1 |
| α-helix | 1950-1959 | 10 | |
| α-helix | 1962-1964 | 3 | |
| α-helix | 1966-1968 | 3 | |
| β-strand | 1969 | 1 | 1 |
| α-helix | 1973-1979 | 7 | |
| α-helix | 1983-1992 | 10 | |
| β-strand | 2000-2003 | 4 | 3 |
| α-helix | 2011-2020 | 10 | |
| α-helix | 2023 | 1 | |
| β-strand | 2024-2026 | 3 | 3 |
| β-strand | 2037-2040 | 4 | 3 |
| α-helix | 2043-2048 | 6 | |
| α-helix | 2050-2055 | 6 | |
| α-helix | 2057-2058 | 2 | |
| β-strand | 2059-2060 | 2 | 3 |
| α-helix | 2063-2071 | 9 | |
| α-helix | 2076-2079 | 4 | |
| β-strand | 2080 | 1 | 3 |
| α-helix | 2081-2082 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 1894-1897 | 4 | 4 |
| α-helix | 1903-1911 | 9 | |
| β-strand | 1915-1916 | 2 | 4 |
| α-helix | 1920-1922 | 3 | |
| β-strand | 1925-1928 | 4 | 4 |
| β-strand | 1934 | 1 | 5 |
| α-helix | 1935-1943 | 9 | |
| β-strand | 1947-1949 | 3 | 4 |
| α-helix | 1951-1959 | 9 | |
| α-helix | 1962-1964 | 3 | |
| α-helix | 1966-1968 | 3 | |
| β-strand | 1969 | 1 | 4 |
| α-helix | 1973-1979 | 7 | |
| α-helix | 1983-1992 | 10 | |
| β-strand | 2000-2003 | 4 | 6 |
| α-helix | 2011-2020 | 10 | |
| β-strand | 2024-2026 | 3 | 6 |
| β-strand | 2037-2040 | 4 | 6 |
| α-helix | 2043-2049 | 7 | |
| α-helix | 2050-2055 | 6 | |
| β-strand | 2059-2060 | 2 | 6 |
| α-helix | 2063-2071 | 9 | |
| α-helix | 2076-2078 | 3 | |
| β-strand | 2080 | 1 | 6 |
| α-helix | 2081-2082 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 141 | 1 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Mediator of DNA damage checkpoint protein 1 | A, B | protein | 200 | Homo sapiens | Q14676 (AlphaFold model) |
| phospho peptide | C, D | protein | 5 |
>3K05_1 Mediator of DNA damage checkpoint protein 1 (chains A, B) GTAPKVLFTGVVDARGERAVLALGGSLAGSAAEASHLVTDRIRRTVKFLCALGRGIPILS LDWLHQSRKAGFFLPPDEYVVTDPEQEKNFGFSLQDALSRARERRLLEGYEIYVTPGVQP PPPQMGEIISCCGGTYLPSMPRSYKPQRVVITCPQDFPHCSIPLRVGLPLLSPEFLLDGV LKQEAKPEAFVLSPLEMSST
>3K05_2 phospho peptide (chains C, D) SQEYX
Comparison of the Structures and Peptide Binding Specificities of the BRCT Domains of MDC1 and BRCA1. Campbell, S.J., Edwards, R.A., Glover, J.N. Structure (2010) 18:167-176. DOI 10.1016/j.str.2009.12.008 · PubMed
Other PDB entries of the same protein (UniProt Q14676 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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