2LSJ: Mouse Rev1 CTD

Solution structure of the mouse Rev1 CTD in complex with the Rev1-interacting Region (RIR)of Pol Kappa. Determined by solution NMR. Released 20 Jun 2012.

Method: Solution NMR
Organism: Mus musculus
Chains: 2
Atoms: 903
Mol. weight: 16.26 kDa
Released: 20 Jun 2012

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

Secondary structure: helices and β-sheets

2LSJ 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

Element	Residues	Length	Sheet
β-strand	27	1	1
β-strand	30	1	1
α-helix	33-45	13
α-helix	52-68	17
α-helix	71-87	17
α-helix	92-109	18

Chain B: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	209-218	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
DNA repair protein REV1	A	protein	119	Mus musculus	Q920Q2 (AlphaFold model)
DNA polymerase kappa	B	protein	25	Mus musculus	Q9QUG2 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2LSJ_1 DNA repair protein REV1 (chains A)
GSGGGAQDLSSLLPGQSSCFRPAAPNLAGAVEFSDVKTLLKEWITTISDPMEEDILQVVR
YCTDLIEEKDLEKLDLVIKYMKRLMQQSVESVWNMAFDFILDNVQVVLQQTYGSTLKVT

Sequence of entity 2 (B), FASTA

>2LSJ_2 DNA polymerase kappa (chains B)
SHMSHKKSFFDKKRSERISNCQDTS

Primary citation

Multifaceted recognition of vertebrate Rev1 by translesion polymerases zeta and kappa. Wojtaszek, J., Liu, J., D'Souza, S. et al. J Biol Chem (2012) 287:26400-26408. DOI 10.1074/jbc.M112.380998 · PubMed

Other PDB entries of the same protein (UniProt Q920Q2 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6C8C 1.5 Å, Chimeric Pol kappa RIR Rev1 C-terminal domain in complex with JHRE06
6C59 2.03 Å, Chimeric Pol kappa RIR Rev1 C-terminal domain
4FJO 2.72 Å, Structure of the Rev1 CTD-Rev3/7-Pol kappa RIR complex
2LSG Solution structure of the mouse Rev1 C-terminal domain

Browse structure collections

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