6C1T: MBD2

MBD2 in complex with a partially methylated DNA. Determined by X-ray diffraction at 1.84 Å resolution. Released 14 Feb 2018.

Method
X-ray diffraction
Resolution
1.84 Å
Organisms
Homo sapiens, synthetic construct
Chains
4
Atoms
1,559
Mol. weight
25.11 kDa
Released
14 Feb 2018

Explore 6C1T in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6C1T contains 4 α-helices and 12 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.

Chains A and D: 2 helices, 6 β-strands

ElementResiduesLengthSheet
β-strand150-15121
β-strand160-16561
β-strand175-18061
β-strand186-18721
α-helix190-1978
α-helix198-2003
β-strand206-20722
β-strand212-21322

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Methyl-CpG-binding domain protein 2A, Dprotein79Homo sapiensQ9UBB5 (AlphaFold model)
12-mer DNABDNA12synthetic construct
12-mer DNACDNA12synthetic construct
Sequence of entity 1 (A, D), FASTA
>6C1T_1 Methyl-CpG-binding domain protein 2 (chains A, D)
GATESGKRMDCPALPPGWKKEEVIRKSGLSAGKSDVYYFSPSGKKFRSKPQLARYLGNTV
DLSSFDFRTGKMMPSKLQK
Sequence of entity 2 (B), FASTA
>6C1T_2 12-mer DNA (chains B)
GCCTACACTCCG
Sequence of entity 3 (C), FASTA
>6C1T_3 12-mer DNA (chains C)
CGGAGTGTAGGC

Primary citation

Structural basis for the ability of MBD domains to bind methyl-CG and TG sites in DNA. Liu, K., Xu, C., Lei, M. et al. J Biol Chem (2018) 293:7344-7354. DOI 10.1074/jbc.RA118.001785 · PubMed

Other PDB entries of the same protein (UniProt Q9UBB5 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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