Ets1 complex with stromelysin-1 promoter DNA. Determined by X-ray diffraction at 3.0 Å resolution. Released 18 Aug 2010.
Explore 3MFK in 3D Show helices and sheets RCSB PDB PDBe
3MFK contains 16 α-helices and 8 β-strands across 2 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 | 304-312 | 9 | |
| α-helix | 323-330 | 8 | |
| α-helix | 337-345 | 9 | |
| α-helix | 348-352 | 5 | |
| β-strand | 355-356 | 2 | 1 |
| β-strand | 362-364 | 3 | 1 |
| α-helix | 368-378 | 11 | |
| α-helix | 386-394 | 9 | |
| α-helix | 396-399 | 4 | |
| β-strand | 404 | 1 | 1 |
| β-strand | 411-413 | 3 | 1 |
| α-helix | 418-422 | 5 | |
| α-helix | 426-432 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 304-312 | 9 | |
| α-helix | 323-330 | 8 | |
| α-helix | 337-344 | 8 | |
| β-strand | 355-356 | 2 | 2 |
| β-strand | 362-364 | 3 | 2 |
| α-helix | 368-378 | 11 | |
| α-helix | 386-399 | 14 | |
| β-strand | 402-404 | 3 | 2 |
| β-strand | 411-414 | 4 | 2 |
| α-helix | 418-422 | 5 | |
| α-helix | 426-433 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein C-ets-1 | A, B | protein | 162 | Homo sapiens | P14921 (AlphaFold model) |
| stromelysin-1 promoter DNA | C | DNA | 16 | ||
| stromelysin-1 promoter DNA | D | DNA | 16 |
>3MFK_1 Protein C-ets-1 (chains A, B) VPSYDSFDSEDYPAALPNHKPKGTFKDYVRDRADLNKDKPVIPAAALAGYTGSGPIQLWQ FLLELLTDKSCQSFISWTGDGWEFKLSDPDEVARRWGKRKNKPKMNYEKLSRGLRYYYDK NIIHKTAGKRYVYRFVCDLQSLLGYTPEELHAMLDVKPDADE
>3MFK_2 stromelysin-1 promoter DNA (chains C) GCAGGAAGTGCTTCCT
>3MFK_3 stromelysin-1 promoter DNA (chains D) CAGGAAGCACTTCCTG
Structural basis of Ets1 cooperative binding to palindromic sequences on stromelysin-1 promoter DNA. Babayeva, N.D., Wilder, P.J., Shiina, M. et al. Cell Cycle (2010) 9:3054-3062. PubMed
Other PDB entries of the same protein (UniProt P14921 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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