2MH0: P300 Taz2:ETAD1 complex

Solution NMR structure of the p300 Taz2:ETAD1 complex. Determined by solution NMR. Released 12 Nov 2014.

Method
Solution NMR
Organism
Homo sapiens
Chains
2
Atoms
994
Mol. weight
14.38 kDa
Released
12 Nov 2014

Explore 2MH0 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2MH0 contains 5 α-helices and 0 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: 1 helix, 0 β-strands

ElementResiduesLengthSheet
α-helix12-2514
Chain B: 4 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix1727-174721
α-helix1756-176914
α-helix1780-179516
α-helix1804-18107

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Transcription factor E2-alphaAprotein39Homo sapiensP15923 (AlphaFold model)
Histone acetyltransferase p300Bprotein92Homo sapiensQ09472 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2MH0_1 Transcription factor E2-alpha (chains A)
GSMNQPQRMAPVGTDKELSDLLDFSMMFPLPVTNGKGRP
Sequence of entity 2 (B), FASTA
>2MH0_2 Histone acetyltransferase p300 (chains B)
GSATQSPGDSRRLSIQRAIQSLVHAAQCRNANCSLPSCQKMKRVVQHTKGCKRKTNGGCP
ICKQLIALAAYHAKHCQENKCPVPFCLNIKQK

Primary citation

Structural insights into TAZ2 domain-mediated CBP/p300 recruitment by transactivation domain 1 of the lymphopoietic transcription factor E2A. Lochhead, M.R., Brown, A.D., Kirlin, A.C. et al. J Biol Chem (2020) 295:4303-4315. DOI 10.1074/jbc.RA119.011078 · PubMed

Other PDB entries of the same protein (UniProt P15923 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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