2N1G: C-terminal domain of human polymerase Rev1

Structure of C-terminal domain of human polymerase Rev1 in complex with PolD3 RIR-motif. Determined by solution NMR. Released 13 Apr 2016.

Method
Solution NMR
Organism
Homo sapiens
Chains
2
Atoms
888
Mol. weight
12.73 kDa
Released
13 Apr 2016

Explore 2N1G in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 4 helices, 2 β-strands

ElementResiduesLengthSheet
β-strand115911
β-strand116211
α-helix1165-117814
α-helix1184-119916
α-helix1203-121917
α-helix1224-124320

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
DNA repair protein REV1Aprotein94Homo sapiensQ9UBZ9 (AlphaFold model)
DNA polymerase delta subunit 3Bprotein16Homo sapiensQ15054 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2N1G_1 DNA repair protein REV1 (chains A)
NLAGAVEFNDVKTLLREWITTISDPMEEDILQVVKYCTDLIEEKDLEKLDLVIKYMKRLM
QQSVESVWNMAFDFILDNVQVVLQQTYGSTLKVT
Sequence of entity 2 (B), FASTA
>2N1G_2 DNA polymerase delta subunit 3 (chains B)
KGNMMSNFFGKAAMNK

Primary citation

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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