1DUX: Ets-domain protein elk-1

Elk-1/DNA structure reveals how residues distal from DNA-binding surface affect DNA-recognition. Determined by X-ray diffraction at 2.1 Å resolution. Released 17 Apr 2000.

Method: X-ray diffraction
Resolution: 2.1 Å
Organism: Homo sapiens
Chains: 6
Atoms: 2,775
Mol. weight: 38.02 kDa
Released: 17 Apr 2000

Explore 1DUX in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1DUX contains 6 α-helices and 8 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 C: 3 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	7-17	11
β-strand	25-28	4	1
β-strand	33-35	3	1
α-helix	39-48	10
α-helix	57-68	12
β-strand	73-75	3	1
β-strand	82-85	4	1

Chain F: 3 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	7-17	11
β-strand	25-28	4	2
β-strand	33-35	3	2
α-helix	39-49	11
α-helix	57-68	12
β-strand	73-75	3	2
β-strand	82-85	4	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
DNA (5'-d(tpgpapcpcpgpgpapapgptpgp*t)-3')	A, D	DNA	13
DNA (5'-d(apcpapcptptpcpcpgpgptpcp*a)-3')	B, E	DNA	13
Ets-domain protein elk-1	C, F	protein	94	Homo sapiens	P19419 (AlphaFold model)

Sequence of entity 1 (A, D), FASTA

>1DUX_1 DNA (5'-D(*TP*GP*AP*CP*CP*GP*GP*AP*AP*GP*TP*GP*T)-3') (chains A, D)
TGACCGGAAGTGT

Sequence of entity 2 (B, E), FASTA

>1DUX_2 DNA (5'-D(*AP*CP*AP*CP*TP*TP*CP*CP*GP*GP*TP*CP*A)-3') (chains B, E)
ACACTTCCGGTCA

Sequence of entity 3 (C, F), FASTA

>1DUX_3 ETS-DOMAIN PROTEIN ELK-1 (chains C, F)
MDPSVTLWQFLLQLLREQGNGHIISWTSRDGGEFKLVDAEEVARLWGLRKNKTNMNYDKL
SRALRYYYDKNIIRKVSGQKFVYKFVSYPEVAGC

Primary citation

Structure of the elk-1-DNA complex reveals how DNA-distal residues affect ETS domain recognition of DNA. Mo, Y., Vaessen, B., Johnston, K. et al. Nat Struct Biol (2000) 7:292-297. DOI 10.1038/74055 · PubMed

Other PDB entries of the same protein (UniProt P19419 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5VVT 2.8 Å, Structural Investigations of the Substrate Specificity of Human O-GlcNAcase
9F6Y 2.98 Å, CryoEM structure of Human Mediator subunit MED23 complexed with phosphorylated Elk-1…

Browse structure collections

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