3cqa

X-ray diffraction
1.8Å resolution

Crystal structure of human fibroblast growth factor-1 with mutations Glu81Ala and Lys101Ala

Released:
Source organism: Homo sapiens
Primary publication:
Engineering an improved crystal contact across a solvent-mediated interface of human fibroblast growth factor 1.
Acta Crystallogr Sect F Struct Biol Cryst Commun 65 1136-40 (2009)
PMID: 19923735

Function and Biology Details

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
PDBe Complex ID:
PDB-CPX-138603 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fibroblast growth factor 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 144 amino acids
Theoretical weight: 16.29 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P05230 (Residues: 16-155; Coverage: 90%)
Gene names: FGF1, FGFA
Sequence domains: Fibroblast growth factor
Structure domains: Trefoil (Acidic Fibroblast Growth Factor, subunit A)

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: C2221
Unit cell:
a: 73.34Å b: 97.91Å c: 108.48Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.191 0.191 0.212
Expression system: Escherichia coli BL21(DE3)