› 1jt5

X-ray diffraction
1.85Å resolution

Human Acidic Fibroblast Growth Factor. 141 Amino Acid Form with Amino Terminal His Tag AND LEU 73 REPLACED BY VAL AND VAL 109 REPLACED BY LEU (L73V/V109L)

Released:
DOI: 10.2210/pdb1jt5/pdb
PDB entry 1jt5 coloured by chain, front view.
PDB entry 1jt5 coloured by chain, side view.
PDB entry 1jt5 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: 16.69 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 4 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: C2221
Unit cell:
a: 74.163Å b: 97.923Å c: 108.749Å
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