PDBe 4q9p

X-ray diffraction
1.8Å resolution

Crystal structure of C16T/K12V/C117V/P134V mutant of human acidic fibroblast growth factor

Released:
Source organism: Homo sapiens
Primary publication:
Mutation choice to eliminate buried free cysteines in protein therapeutics.
J Pharm Sci 104 566-76 (2015)
PMID: 25312595

Function and Biology Details

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fibroblast growth factor 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 146 amino acids
Theoretical weight: 16.65 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: NEW 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

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-BM
Spacegroup: P41212
Unit cell:
a: 53.687Å b: 53.687Å c: 217.973Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.175 0.173 0.21
Expression system: Escherichia coli BL21(DE3)