Structure of the C-terminal domain from human REV1. Determined by solution NMR. Released 27 Jun 2012.
Explore 2LSY in 3D Show helices and sheets RCSB PDB PDBe
2LSY contains 4 α-helices and 2 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 | 1159 | 1 | 1 |
| β-strand | 1162 | 1 | 1 |
| α-helix | 1165-1178 | 14 | |
| α-helix | 1184-1199 | 16 | |
| α-helix | 1203-1219 | 17 | |
| α-helix | 1224-1243 | 20 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| DNA repair protein REV1 | A | protein | 95 | Homo sapiens | Q9UBZ9 (AlphaFold model) |
>2LSY_1 DNA repair protein REV1 (chains A) GNLAGAVEFNDVKTLLREWITTISDPMEEDILQVVKYCTDLIEEKDLEKLDLVIKYMKRL MQQSVESVWNMAFDFILDNVQVVLQQTYGSTLKVT
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:
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