9CP6: DNA binding domain of FLI1

Crystal structure of the DNA binding domain of FLI1 (residues 259-371). Determined by X-ray diffraction at 1.66 Å resolution. Released 12 Mar 2025.

Method
X-ray diffraction
Resolution
1.66 Å
Organism
Homo sapiens
Chains
1
Atoms
864
Mol. weight
13.5 kDa
Released
12 Mar 2025

Explore 9CP6 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9CP6 contains 7 α-helices and 4 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: 7 helices, 4 β-strands

ElementResiduesLengthSheet
α-helix283-2919
α-helix294-2963
β-strand301-30221
β-strand308-31031
α-helix314-32512
α-helix332-34110
α-helix343-3453
β-strand348-35031
α-helix3511
β-strand357-36041
α-helix362-3687

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Friend leukemia integration 1 transcription factorAprotein117Homo sapiensQ01543 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>9CP6_1 Friend leukemia integration 1 transcription factor (chains A)
GPHMQPDPYQILGPTSSRLANPGSGQIQLWQFLLELLSDSANASCITWEGTNGEFKMTDP
DEVARRWGERKSKPNMNYDKLSRALRYYYDKNIMTKVHGKRYAYKFDFHGIAQALQP

Primary citation

Structure and cooperative formation of a FLI1 filament on contiguous GGAA DNA sites. Hou, C., Tsodikov, O.V. Nucleic Acids Res (2025) 53. DOI 10.1093/nar/gkaf205 · PubMed

Other PDB entries of the same protein (UniProt Q01543 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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