Structure of C-terminal domain of human polymerase Rev1 in complex with PolD3 RIR-motif. Determined by solution NMR. Released 13 Apr 2016.
Explore 2N1G in 3D Show helices and sheets RCSB PDB PDBe
2N1G 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 | 94 | Homo sapiens | Q9UBZ9 (AlphaFold model) |
| DNA polymerase delta subunit 3 | B | protein | 16 | Homo sapiens | Q15054 (AlphaFold model) |
>2N1G_1 DNA repair protein REV1 (chains A) NLAGAVEFNDVKTLLREWITTISDPMEEDILQVVKYCTDLIEEKDLEKLDLVIKYMKRLM QQSVESVWNMAFDFILDNVQVVLQQTYGSTLKVT
>2N1G_2 DNA polymerase delta subunit 3 (chains B) KGNMMSNFFGKAAMNK
Interaction between the Rev1 C-Terminal Domain and the PolD3 Subunit of Pol zeta Suggests a Mechanism of Polymerase Exchange upon Rev1/Pol zeta-Dependent Translesion Synthesis. Pustovalova, Y., Magalhaes, M.T., D'Souza, S. et al. Biochemistry (2016) 55:2043-2053. DOI 10.1021/acs.biochem.5b01282 · 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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