Crystal structure of the MDC1 brct repeat in complex with the histone tail of gamma-H2AX. Determined by X-ray diffraction at 2.41 Å resolution. Released 31 Jan 2006.
Explore 2AZM in 3D Show helices and sheets RCSB PDB PDBe
2AZM contains 30 α-helices and 22 β-strands across 3 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 | 1951-1959 | 9 | |
| α-helix | 1962-1964 | 3 | |
| α-helix | 1965-1968 | 4 | |
| 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 | |
| β-strand | 2024-2026 | 3 | 3 |
| β-strand | 2037-2040 | 4 | 3 |
| α-helix | 2043-2049 | 7 | |
| α-helix | 2050-2055 | 6 | |
| α-helix | 2057-2058 | 2 | |
| β-strand | 2059-2060 | 2 | 3 |
| α-helix | 2063-2066 | 4 | |
| α-helix | 2068-2071 | 4 | |
| α-helix | 2076-2078 | 3 | |
| 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 |
| β-strand | 1925-1927 | 3 | 4 |
| α-helix | 1935-1943 | 9 | |
| β-strand | 1947-1948 | 2 | 4 |
| α-helix | 1951-1959 | 9 | |
| α-helix | 1962-1964 | 3 | |
| α-helix | 1965-1968 | 4 | |
| β-strand | 1969 | 1 | 4 |
| α-helix | 1973-1978 | 6 | |
| α-helix | 1983-1992 | 10 | |
| β-strand | 2000-2003 | 4 | 5 |
| α-helix | 2011-2020 | 10 | |
| β-strand | 2024-2026 | 3 | 5 |
| β-strand | 2037-2040 | 4 | 5 |
| α-helix | 2046-2048 | 3 | |
| α-helix | 2050-2055 | 6 | |
| α-helix | 2057-2058 | 2 | |
| β-strand | 2059-2060 | 2 | 5 |
| α-helix | 2063-2071 | 9 | |
| α-helix | 2076-2078 | 3 | |
| β-strand | 2080 | 1 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 139-140 | 2 | |
| β-strand | 141 | 1 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Mediator of DNA damage checkpoint protein 1 | A, B | protein | 207 | Homo sapiens | Q14676 (AlphaFold model) |
| Gamma-H2AX histone | C, D | protein | 10 | P16104 (AlphaFold model) |
>2AZM_1 Mediator of DNA damage checkpoint protein 1 (chains A, B) RTKLNQESTAPKVLFTGVVDARGERAVLALGGSLAGSAAEASHLVTDRIRRTVKFLCALG RGIPILSLDWLHQSRKAGFFLPPDEYVVTDPEQEKNFGFSLQDALSRARERRLLEGYEIY VTPGVQPPPPQMGEIISCCGGTYLPSMPRSYKPQRVVITCPQDFPHCSIPLRVGLPLLSP EFLLTGVLKQEAKPEAFVLSPLEMSST
>2AZM_2 GAMMA-H2AX HISTONE (chains C, D) KKATQASQEY
MDC1 Directly Binds Phosphorylated Histone H2AX to Regulate Cellular Responses to DNA Double-Strand Breaks. Stucki, M., Clapperton, J.A., Mohammad, D. et al. Cell (2005) 123:1213-1226. DOI 10.1016/j.cell.2005.09.038 · 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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