› 3k1x

X-ray diffraction
1.98Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fibroblast growth factor 1 Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 130 amino acids
Theoretical weight: 14.75 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P05230 (Residues: 24-153; Coverage: 84%)
Gene names: FGF1, FGFA
Sequence domains: Fibroblast growth factor
Structure domains: Trefoil (Acidic Fibroblast Growth Factor, subunit A)

Ligands and Environments

1 bound ligand:
Ligand DBX 2 x DBX
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM16
Spacegroup: P2
Unit cell:
a: 97.022Å b: 47.349Å c: 97.975Å
α: 90° β: 106.64° γ: 90°
R-values:
R R work R free
0.232 0.227 0.29
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Do Aspirin and Flavonoids Prevent Cancer through a Common Mechanism Involving Hydroxybenzoic Acids?-The Metabolite Hypothesis.
Sankaranarayanan et al. (2020)
7 more

3 mentions without citation

Gentisic acid, a compound associated with plant defense and a metabolite of aspirin, heads a new class of in vivo fibroblast growth factor inhibitors.
Fernández et al. (2010)
2 more