Solution structure of polymerase-interacting domain of human Rev1 in complex with translesional synthesis polymerase kappa. Determined by solution NMR. Released 29 May 2013.
Explore 2LSI in 3D Show helices and sheets RCSB PDB PDBe
2LSI 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 | 1165-1178 | 14 | |
| α-helix | 1184-1199 | 16 | |
| α-helix | 1203-1219 | 17 | |
| α-helix | 1223-1243 | 21 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 567-574 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| DNA repair protein REV1 | A | protein | 99 | Homo sapiens | Q9UBZ9 (AlphaFold model) |
| DNA polymerase kappa | B | protein | 17 | Homo sapiens | Q9UBT6 (AlphaFold model) |
>2LSI_1 DNA repair protein REV1 (chains A) GHMAPNLAGAVEFNDVKTLLREWITTISDPMEEDILQVVKYCTDLIEEKDLEKLDLVIKY MKRLMQQSVESVWNMAFDFILDNVQVVLQQTYGSTLKVT
>2LSI_2 DNA polymerase kappa (chains B) GSHKKSFFDKKRSERKW
Insights into the scaffold mechanism of human Rev1 in translesional synthesis revealed by the structural studies on its polymerase-interacting domain. Liu, D., Ryu, K., Ko, J. et al. To be published.
Other PDB entries of the same protein (UniProt Q9UBZ9 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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