› 3o3q

X-ray diffraction
1.6Å resolution

Crystal structure of "L44F/M67I/L73V/A103G/deletion 104-106/F108Y/V109L/L111I/C117V/R119G/deletion 120-122" mutant form of Human acidic fibroblast growth factor

Released:
DOI: 10.2210/pdb3o3q/pdb
PDB entry 3o3q coloured by chain, front view.
PDB entry 3o3q coloured by chain, side view.
PDB entry 3o3q coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
A polypeptide "building block" for the β-trefoil fold identified by "top-down symmetric deconstruction".
Lee J, Blaber SI, Dubey VK, Blaber M
J Mol Biol 407 744-63 (2011)
PMID: 21315087

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-138603 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fibroblast growth factor 1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 140 amino acids
Theoretical weight: 15.92 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P05230 (Residues: 16-155; Coverage: 87%)
  • Best match: P05230-2 (Residues: 16-56)
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 GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-BM
Spacegroup: P1
Unit cell:
a: 46.92Å b: 56.89Å c: 61.92Å
α: 64.94° β: 89.76° γ: 71.27°
R-values:
R R work R free
0.172 0.17 0.203
Expression system: Escherichia coli

Quick links

Citations

7 review citations

Protein design at the interface of the pre-biotic and biotic worlds.
Longo et al. (2012)
6 more

1 mention without citation

Pharmacokinetic properties of 2nd-generation fibroblast growth factor-1 mutants for therapeutic application.
Xia et al. (2012)