› 1rml

Solution NMR

NMR STUDY OF ACID FIBROBLAST GROWTH FACTOR BOUND TO 1,3,6-NAPHTHALENE TRISULPHONATE, 26 STRUCTURES

Released:
DOI: 10.2210/pdb1rml/pdb
PDB entry 1rml coloured by chain, ensemble of 26 models, front view.
PDB entry 1rml coloured by chain, ensemble of 26 models, side view.
PDB entry 1rml coloured by chain, ensemble of 26 models, top view.
Source organism: Homo sapiens
Primary publication:
Solution structure of acidic fibroblast growth factor bound to 1,3, 6-naphthalenetrisulfonate: a minimal model for the anti-tumoral action of suramins and suradistas.
Lozano RM, Jiménez M, Santoro J, Rico M, Giménez-Gallego G
J Mol Biol 281 899-915 (1998)
PMID: 9719643

Function and Biology Details

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

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 Chain: A
Molecule details ›
Chain: A
Length: 155 amino acids
Theoretical weight: 17.48 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P05230 (Residues: 1-155; Coverage: 100%)
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 NTS 1 x NTS
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: VARIABLE TARGET FUNCTION
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Tyrosine kinase inhibitors targeted to the epidermal growth factor receptor subfamily: role as anticancer agents.
Noonberg et al. (2000)
3 more

1 mention without citation

Experimental support for the foldability-function tradeoff hypothesis: segregation of the folding nucleus and functional regions in fibroblast growth factor-1.
Longo et al. (2012)