Solution structure of the BRCT domain from human DNA repair protein REV1. Determined by solution NMR. Released 14 Aug 2007.
Explore 2EBW in 3D Show helices and sheets RCSB PDB PDBe
2EBW contains 4 α-helices and 5 β-strands across 1 chain. 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 | 53-56 | 4 | 1 |
| α-helix | 64-73 | 10 | |
| β-strand | 77-78 | 2 | 1 |
| β-strand | 89-91 | 3 | 1 |
| α-helix | 99-102 | 4 | |
| β-strand | 109 | 1 | 2 |
| α-helix | 112-120 | 9 | |
| α-helix | 127-129 | 3 | |
| β-strand | 130 | 1 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| DNA repair protein REV1 | A | protein | 97 | Homo sapiens | Q9UBZ9 (AlphaFold model) |
>2EBW_1 DNA repair protein REV1 (chains A) GSSGSSGTSSTIFSGVAIYVNGYTDPSAEELRKLMMLHGGQYHVYYSRSKTTHIIATNLP NAKIKELKGEKVIRPEWIVESIKAGRLLSYIPYQLYT
Solution structure of the BRCT domain from human DNA repair protein REV1. Nagashima, T., Hayashi, F., Yokoyama, S. To be published.
Other PDB entries of the same protein (UniProt Q9UBZ9 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 2EBW 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.