› 6y2d

X-ray diffraction
1.9Å resolution

Crystal structure of the second KH domain of FUBP1

Released:
DOI: 10.2210/pdb6y2d/pdb
PDB entry 6y2d coloured by chain, front view.
PDB entry 6y2d coloured by chain, side view.
PDB entry 6y2d 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, C, D
Molecule details ›
Chains: A, B, C, D
Length: 77 amino acids
Theoretical weight: 8.33 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q96AE4 (Residues: 185-259; Coverage: 12%)
Gene name: FUBP1
Sequence domains: KH domain

Ligands and Environments

2 bound ligands:
Ligand SO4 4 x SO4
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P21
Unit cell:
a: 28.888Å b: 82.181Å c: 49.371Å
α: 90° β: 91.04° γ: 90°
R-values:
R R work R free
0.198 0.195 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)