6C9L: MEF2B Apo Protein Structure

MEF2B Apo Protein Structure. Determined by X-ray diffraction at 2.3 Å resolution. Released 7 Feb 2018.

Method
X-ray diffraction
Resolution
2.3 Å
Organism
Homo sapiens
Chains
6
Atoms
4,098
Mol. weight
66.23 kDa
Released
7 Feb 2018

Explore 6C9L in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6C9L contains 23 α-helices and 16 β-strands across 6 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, 3 β-strands

ElementResiduesLengthSheet
α-helix14-3926
β-strand42-4871
β-strand54-5851
α-helix62-7110
α-helix75-762
β-strand77-8041
α-helix81-899
Chain B: 5 helices, 3 β-strands
ElementResiduesLengthSheet
α-helix8-103
α-helix14-163
α-helix17-3923
β-strand42-4871
β-strand54-5851
α-helix62-7110
β-strand77-8041
α-helix81-899
Chain C: 5 helices, 3 β-strands
ElementResiduesLengthSheet
α-helix8-103
α-helix14-163
α-helix17-3923
β-strand42-4872
β-strand54-5852
α-helix62-7110
β-strand77-8042
α-helix81-888
Chain D: 4 helices, 3 β-strands
ElementResiduesLengthSheet
α-helix14-3926
β-strand42-4872
β-strand54-5852
α-helix62-7110
α-helix75-762
β-strand77-7932
α-helix81-899
Chain E: 2 helices, 2 β-strands
ElementResiduesLengthSheet
α-helix14-3926
β-strand42-4873
β-strand54-5853
α-helix62-7110
Chain F: 3 helices, 2 β-strands
ElementResiduesLengthSheet
α-helix14-3926
β-strand42-4873
β-strand54-5853
α-helix62-7211
α-helix81-888

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Myocyte-specific enhancer factor 2BA, B, C, D, E, Fprotein93Homo sapiensQ02080 (AlphaFold model)
Sequence of entity 1 (A, B, C, D, E, F), FASTA
>6C9L_1 Myocyte-specific enhancer factor 2B (chains A, B, C, D, E, F)
MGRKKIQISRILDQRNRQVTFTKRKFGLMKKAYELSVLCDCEIALIIFNSANRLFQYAST
DMDRVLLKYTEYSEPHESRTNTDILETLKRRGI

Primary citation

Crystal Structure of Apo MEF2B Reveals New Insights in DNA Binding and Cofactor Interaction. Lei, X., Shi, H., Kou, Y. et al. Biochemistry (2018) 57:4047-4051. DOI 10.1021/acs.biochem.8b00439 · PubMed

Other PDB entries of the same protein (UniProt Q02080 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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