C-terminal domain of human REV1 in complex with DNA-polymerase H (eta). Determined by solution NMR. Released 27 Jun 2012.
Explore 2LSK in 3D Show helices and sheets RCSB PDB PDBe
2LSK contains 5 α-helices and 2 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 |
|---|---|---|---|
| β-strand | 1159 | 1 | 1 |
| β-strand | 1162 | 1 | 1 |
| α-helix | 1165-1177 | 13 | |
| α-helix | 1185-1200 | 16 | |
| α-helix | 1203-1219 | 17 | |
| α-helix | 1224-1243 | 20 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 532-538 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| DNA repair protein REV1 | A | protein | 95 | Homo sapiens | Q9UBZ9 (AlphaFold model) |
| DNA polymerase eta | B | protein | 16 | Homo sapiens | Q9Y253 (AlphaFold model) |
>2LSK_1 DNA repair protein REV1 (chains A) GNLAGAVEFNDVKTLLREWITTISDPMEEDILQVVKYCTDLIEEKDLEKLDLVIKYMKRL MQQSVESVWNMAFDFILDNVQVVLQQTYGSTLKVT
>2LSK_2 DNA polymerase eta (chains B) QSTGTEPFFKQKSLLL
NMR structure and dynamics of the C-terminal domain from human Rev1 and its complex with Rev1 interacting region of DNA polymerase eta. Pozhidaeva, A., Pustovalova, Y., D'Souza, S. et al. Biochemistry (2012) 51:5506-5520. DOI 10.1021/bi300566z · PubMed
Other PDB entries of the same protein (UniProt Q9UBZ9 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 2LSK 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.