2LSI: Polymerase-interacting domain of human Rev1

Solution structure of polymerase-interacting domain of human Rev1 in complex with translesional synthesis polymerase kappa. Determined by solution NMR. Released 29 May 2013.

Method
Solution NMR
Organism
Homo sapiens
Chains
2
Atoms
954
Mol. weight
13.61 kDa
Released
29 May 2013

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

Secondary structure: helices and β-sheets

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.

Chain A: 4 helices, 2 β-strands

ElementResiduesLengthSheet
β-strand115911
β-strand116211
α-helix1165-117814
α-helix1184-119916
α-helix1203-121917
α-helix1223-124321
Chain B: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix567-5748

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
DNA repair protein REV1Aprotein99Homo sapiensQ9UBZ9 (AlphaFold model)
DNA polymerase kappaBprotein17Homo sapiensQ9UBT6 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2LSI_1 DNA repair protein REV1 (chains A)
GHMAPNLAGAVEFNDVKTLLREWITTISDPMEEDILQVVKYCTDLIEEKDLEKLDLVIKY
MKRLMQQSVESVWNMAFDFILDNVQVVLQQTYGSTLKVT
Sequence of entity 2 (B), FASTA
>2LSI_2 DNA polymerase kappa (chains B)
GSHKKSFFDKKRSERKW

Primary citation

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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