› 6y2c

X-ray diffraction
2Å resolution

Crystal structure of the third KH domain of FUBP1

Released:
DOI: 10.2210/pdb6y2c/pdb
PDB entry 6y2c coloured by chain, front view.
PDB entry 6y2c coloured by chain, side view.
PDB entry 6y2c 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 Chains: A, B
Molecule details ›
Chains: A, B
Length: 93 amino acids
Theoretical weight: 10.18 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q96AE4 (Residues: 261-351; Coverage: 14%)
Gene name: FUBP1
Sequence domains: KH domain

Ligands and Environments

2 bound ligands:
Ligand EDO 8 x EDO
Ligand ZN 3 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.2
Spacegroup: P3221
Unit cell:
a: 47.409Å b: 47.409Å c: 147.893Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.205 0.203 0.24
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)