› 1jt3

X-ray diffraction
1.95Å resolution

Human Acidic Fibroblast Growth Factor. 141 Amino Acid Form with Amino Histidine Tag AND LEU 73 REPLACED BY VAL (L73V)

Released:
DOI: 10.2210/pdb1jt3/pdb
PDB entry 1jt3 coloured by chain, front view.
PDB entry 1jt3 coloured by chain, side view.
PDB entry 1jt3 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure and stability effects of mutations designed to increase the primary sequence symmetry within the core region of a beta-trefoil.
Brych SR, Blaber SI, Logan TM, Blaber M
Protein Sci 10 2587-99 (2001)
PMID: 11714927

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
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: 146 amino acids
Theoretical weight: 16.67 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
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

1 bound ligand:
Ligand SO4 3 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: C2221
Unit cell:
a: 73.316Å b: 97.903Å c: 108.69Å
α: 90° β: 90° γ: 90°
Expression system: Escherichia coli

Quick links

Citations

3 review citations

FGF-1: from biology through engineering to potential medical applications.
Zakrzewska et al. (2008)
2 more

1 mention without citation

Effect of glycosylation and additional domains on the thermostability of a family 10 xylanase produced by Thermopolyspora flexuosa.
Anbarasan et al. (2010)