3T92: Taz2:C/EBPepsilon-TAD chimera protein

Crystal structure of the Taz2:C/EBPepsilon-TAD chimera protein. Determined by X-ray diffraction at 1.5 Å resolution. Released 8 Aug 2012.

Method
X-ray diffraction
Resolution
1.5 Å
Organism
Homo sapiens
Chains
1
Atoms
1,128
Mol. weight
14.11 kDa
Ligands
ZN, TCE, TAM, ACN
Released
8 Aug 2012

Explore 3T92 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3T92 contains 5 α-helices and 0 β-strands across 1 chain. 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: 5 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix8-2518
α-helix34-4815
α-helix58-7114
α-helix84-10724
α-helix110-1178

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Histone acetyltransferase P300 TAZ2-ccaat/enhancer-binding protein epsilonAprotein121Homo sapiensQ09472 (AlphaFold model), Q15744 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>3T92_1 HISTONE ACETYLTRANSFERASE P300 TAZ2-CCAAT/ENHANCER-BINDING PROTEIN EPSILON (chains A)
ATQSPGDSRRLSIQRAIQSLVHAAQCRNANCSLPSCQKMKRVVQHTKGCKRKTNGGCPIC
KQLIALAAYHAKHCQENKCPVPFCLNIKQKLRQQQLEASIDLSAYIESGEEQLLSDLFAV
K

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn3
TCE3,3',3''-phosphanetriyltripropanoic acidC9 H15 O6 P1
TAMTris(hydroxyethyl)aminomethaneC7 H17 N O31
ACNAcetoneC3 H6 O1

Primary citation

Structural insights into interactions of C/EBP transcriptional activators with the Taz2 domain of p300. Bhaumik, P., Davis, J., Tropea, J.E. et al. Acta Crystallogr D Biol Crystallogr (2014) 70:1914-1921. DOI 10.1107/S1399004714009262 · PubMed

Other PDB entries of the same protein (UniProt Q09472 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

About this viewer

MolViewer shows 3T92 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.