Solution structure of the mouse Rev1 C-terminal domain. Determined by solution NMR. Released 20 Jun 2012.
Explore 2LSG in 3D Show helices and sheets RCSB PDB PDBe
2LSG contains 4 α-helices and 0 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 |
|---|---|---|---|
| α-helix | 18-30 | 13 | |
| α-helix | 37-52 | 16 | |
| α-helix | 56-72 | 17 | |
| α-helix | 76-96 | 21 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| DNA repair protein REV1 | A | protein | 104 | Mus musculus | Q920Q2 (AlphaFold model) |
>2LSG_1 DNA repair protein REV1 (chains A) GSGGFRPAAPNLAGAVEFSDVKTLLKEWITTISDPMEEDILQVVRYCTDLIEEKDLEKLD LVIKYMKRLMQQSVESVWNMAFDFILDNVQVVLQQTYGSTLKVT
Multifaceted recognition of vertebrate Rev1 by translesion polymerases zeta and kappa. Wojtaszek, J., Liu, J., D'Souza, S. et al. J Biol Chem (2012) 287:26400-26408. DOI 10.1074/jbc.M112.380998 · PubMed
Other PDB entries of the same protein (UniProt Q920Q2 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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