5ZMC: Protein C-ets-1

Structural Basis for Reactivation of -146C>T Mutant TERT Promoter by cooperative binding of p52 and ETS1/2. Determined by X-ray diffraction at 2.99 Å resolution. Released 19 Sept 2018.

Method: X-ray diffraction
Resolution: 2.99 Å
Organism: Homo sapiens
Chains: 4
Atoms: 2,393
Mol. weight: 56.08 kDa
Released: 19 Sept 2018

Explore 5ZMC in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5ZMC contains 8 α-helices and 17 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: 2 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	228	1	2
β-strand	230-233	4	3
β-strand	237-239	3	4
β-strand	245-250	6	3
β-strand	259-263	5	4
β-strand	271-273	3	4
β-strand	275	1	3
α-helix	278-280	3
β-strand	281-282	2	3
β-strand	286-290	5	3
α-helix	291-294	4
β-strand	303-310	8	4
β-strand	317	1	4
β-strand	318	1	2
β-strand	321-326	6	4

Chain B: 6 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	337-345	9
α-helix	348-350	3
β-strand	355-356	2	1
β-strand	362-364	3	1
α-helix	368-378	11
α-helix	386-395	10
β-strand	402-404	3	1
β-strand	411-414	4	1
α-helix	418-421	4
α-helix	426-432	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
DNA (5'-d(pcpgpgpgpgpapcpcpcpgpgpapapgpgpg)-3')	C	DNA	16	Homo sapiens
DNA (5'-d(pgpcpcpcptptpcpcpgpgpgptpcpcpcpc)-3')	D	DNA	16	Homo sapiens
Protein C-ets-1	B	protein	111	Homo sapiens	P14921 (AlphaFold model)
Nuclear factor NF-kappa-B p100 subunit	A	protein	295	Homo sapiens	Q00653 (AlphaFold model)

Sequence of entity 1 (C), FASTA

>5ZMC_1 DNA (5'-D(P*CP*GP*GP*GP*GP*AP*CP*CP*CP*GP*GP*AP*AP*GP*GP*G)-3') (chains C)
CGGGGACCCGGAAGGG

Sequence of entity 2 (D), FASTA

>5ZMC_2 DNA (5'-D(P*GP*CP*CP*CP*TP*TP*CP*CP*GP*GP*GP*TP*CP*CP*CP*C)-3') (chains D)
GCCCTTCCGGGTCCCC

Sequence of entity 3 (B), FASTA

>5ZMC_3 Protein C-ets-1 (chains B)
GSGPIQLWQFLLELLTDKSCQSFISWTGDGWEFKLSDPDEVARRWGKRKNKPKMNYEKLS
RGLRYYYDKNIIHKTAGKRYVYRFVCDLQSLLGYTPEELHAMLDVKPDADE

Sequence of entity 4 (A), FASTA

>5ZMC_4 Nuclear factor NF-kappa-B p100 subunit (chains A)
ADGPYLVIVEQPKQRGFRFRYGCEGPSHGGLPGASSEKGRKTYPTVKICNYEGPAKIEVD
LVTHSDPPRAHAHSLVGKQCSELGICAVSVGPKDMTAQFNNLGVLHVTKKNMMGTMIQKL
QRQRLRSRPQGLTEAEQRELEQEAKELKKVMDLSIVRLRFSAFLRASDGSFSLPLKPVIS
QPIHDSKSPGASNLKISRMDKTAGSVRGGDEVYLLCDKVQKDDIEVRFYEDDENGWQAFG
DFSPTDVHKQYAIVFRTPPYHKMKIERPVTVFLQLKRKRGGDVSDSKQFTYYPLV

Primary citation

Structural basis for reactivating the mutant TERT promoter by cooperative binding of p52 and ETS1. Xu, X., Li, Y., Bharath, S.R. et al. Nat Commun (2018) 9:3183-3183. DOI 10.1038/s41467-018-05644-0 · PubMed

Other PDB entries of the same protein (UniProt P14921 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1GVJ 1.53 Å, Ets-1 DNA binding and autoinhibitory domains
4LG0 2.19 Å, Structure of a ternary FOXO1-ETS1 DNA complex
4L18 2.3 Å, Crystal structure of Runx1 and Ets1 bound to TCR alpha promoter (crystal form 3)
3WTS 2.35 Å, Crystal structure of the complex comprised of ETS1, RUNX1, CBFBETA, and the tcralpha…
3WTT 2.35 Å, Crystal structure of the complex comprised of phosphorylated ETS1, RUNX1, CBFBETA, and…
3WU1 2.4 Å, Crystal structure of the ETS1-RUNX1-DNA ternary complex
4L0Y 2.5 Å, Crystal structure of Runx1 and Ets1 bound to TCR alpha promoter (crystal form 1)
2NNY 2.58 Å, Crystal structure of the Ets1 dimer DNA complex.
3WU0 2.6 Å, Crystal structure of phosphorylated ETS-1 DNA binding and autoinhibitory domains (276-441)
3WTZ 2.61 Å, Crystal structure of ETS-1 DNA binding and autoinhibitory domains (276-441)
3WTU 2.7 Å, Crystal structure of the complex comprised of ETS1 (V170A), RUNX1, CBFBETA, and the…
3WTV 2.7 Å, Crystal structure of the complex comprised of ETS1(V170G), RUNX1, CBFBETA, and the…

Browse structure collections

About this viewer

MolViewer shows 5ZMC 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.