2AGH: Myb proto-oncogene protein

Structural basis for cooperative transcription factor binding to the CBP coactivator. Determined by solution NMR. Released 22 Nov 2005.

Method
Solution NMR
Organisms
Mus musculus, Homo sapiens
Chains
3
Atoms
1,161
Mol. weight
16.61 kDa
Released
22 Nov 2005

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

Secondary structure: helices and β-sheets

2AGH contains 8 α-helices and 0 β-strands across 3 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: 2 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix293-30311
α-helix305-3106
Chain B: 5 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix592-5943
α-helix597-61115
α-helix617-6204
α-helix625-64117
α-helix646-66722
Chain C: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix847-85610

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Myb proto-oncogene proteinAprotein25Mus musculusP06876 (AlphaFold model)
Crebbp proteinBprotein87Mus musculusP45481 (AlphaFold model)
Zinc finger protein HRXCprotein31Homo sapiensQ03164
Sequence of entity 1 (A), FASTA
>2AGH_1 Myb proto-oncogene protein (chains A)
KEKRIKELELLLMSTENELKGQQAL
Sequence of entity 2 (B), FASTA
>2AGH_2 Crebbp protein (chains B)
GVRKGWHEHVTQDLRSHLVHKLVQAIFPTPDPAALKDRRMENLVAYAKKVEGDMYESANS
RDEYYHLLAEKIYKIQKELEEKRRSRL
Sequence of entity 3 (C), FASTA
>2AGH_3 Zinc finger protein HRX (chains C)
SDDGNILPSDIMDFVLKNTPSMQALGESPES

Primary citation

Structural Basis for Cooperative Transcription Factor Binding to the CBP Coactivator. De Guzman, R.N., Goto, N.K., Dyson, H.J. et al. J Mol Biol (2006) 355:1005-1013. DOI 10.1016/j.jmb.2005.09.059 · PubMed

Other PDB entries of the same protein (UniProt P06876 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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