2LSK: C-terminal domain of human REV1

C-terminal domain of human REV1 in complex with DNA-polymerase H (eta). Determined by solution NMR. Released 27 Jun 2012.

Method
Solution NMR
Organism
Homo sapiens
Chains
2
Atoms
900
Mol. weight
12.84 kDa
Released
27 Jun 2012

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

Secondary structure: helices and β-sheets

2LSK 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-helix1165-117713
α-helix1185-120016
α-helix1203-121917
α-helix1224-124320
Chain B: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix532-5387

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
DNA repair protein REV1Aprotein95Homo sapiensQ9UBZ9 (AlphaFold model)
DNA polymerase etaBprotein16Homo sapiensQ9Y253 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2LSK_1 DNA repair protein REV1 (chains A)
GNLAGAVEFNDVKTLLREWITTISDPMEEDILQVVKYCTDLIEEKDLEKLDLVIKYMKRL
MQQSVESVWNMAFDFILDNVQVVLQQTYGSTLKVT
Sequence of entity 2 (B), FASTA
>2LSK_2 DNA polymerase eta (chains B)
QSTGTEPFFKQKSLLL

Primary citation

NMR structure and dynamics of the C-terminal domain from human Rev1 and its complex with Rev1 interacting region of DNA polymerase eta. Pozhidaeva, A., Pustovalova, Y., D'Souza, S. et al. Biochemistry (2012) 51:5506-5520. DOI 10.1021/bi300566z · PubMed

Other PDB entries of the same protein (UniProt Q9UBZ9 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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