› 6y24

X-ray diffraction
1.86Å resolution

Crystal structure of fourth KH domain of FUBP1

Released:
DOI: 10.2210/pdb6y24/pdb
PDB entry 6y24 coloured by chain, front view.
PDB entry 6y24 coloured by chain, side view.
PDB entry 6y24 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Comparative structural analyses and nucleotide-binding characterization of the four KH domains of FUBP1.
Ni X, Knapp S, Chaikuad A
Sci Rep 10 13459 (2020)
PMID: 32778776

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-188354 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Far upstream element-binding protein 1 Chain: A
Molecule details ›
Chain: A
Length: 93 amino acids
Theoretical weight: 10.02 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q96AE4 (Residues: 365-455; Coverage: 14%)
Gene name: FUBP1
Sequence domains: KH domain

Ligands and Environments

1 bound ligand:
Ligand EDO 5 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.2
Spacegroup: C2221
Unit cell:
a: 69.996Å b: 89.054Å c: 28.711Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 0.194 0.243
Expression system: Escherichia coli

Quick links

Citations

1 citations in other articles

The circACTN4 interacts with FUBP1 to promote tumorigenesis and progression of breast cancer by regulating the expression of proto-oncogene MYC.
Wang et al. (2021)