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Solution NMR

BASIC FIBROBLAST GROWTH FACTOR (FGF-2) MUTANT WITH CYS 78 REPLACED BY SER AND CYS 96 REPLACED BY SER, NMR

Released:
DOI: 10.2210/pdb1bld/pdb
PDB entry 1bld coloured by chain, ensemble of 30 models, front view.
PDB entry 1bld coloured by chain, ensemble of 30 models, side view.
PDB entry 1bld coloured by chain, ensemble of 30 models, top view.
Source organism: Homo sapiens
Primary publication:
High-resolution solution structure of basic fibroblast growth factor determined by multidimensional heteronuclear magnetic resonance spectroscopy.
Moy FJ, Seddon AP, Böhlen P, Powers R
Biochemistry 35 13552-61 (1996)
PMID: 8885834

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140533 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fibroblast growth factor 2 Chain: A
Molecule details ›
Chain: A
Length: 155 amino acids
Theoretical weight: 17.35 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P09038 (Residues: 134-288; Coverage: 54%)
Gene names: FGF2, FGFB
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
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Fibroblast growth factor-2.
Okada-Ban et al. (2000)
3 more

5 mentions without citation

Key steps in unconventional secretion of fibroblast growth factor 2 reconstituted with purified components.
Steringer et al. (2017)
4 more