› 1k5v

X-ray diffraction
2.1Å resolution

Human acidic fibroblast growth factor. 141 amino acid form with amino terminal His tag with Asn106 replaced by Gly (N106G).

Released:
DOI: 10.2210/pdb1k5v/pdb
PDB entry 1k5v coloured by chain, front view.
PDB entry 1k5v coloured by chain, side view.
PDB entry 1k5v coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Alternative type I and I' turn conformations in the beta8/beta9 beta-hairpin of human acidic fibroblast growth factor.
Kim J, Blaber SI, Blaber M
Protein Sci 11 459-66 (2002)
PMID: 11847269

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 Chains: A, B
Molecule details ›
Chains: A, B
Length: 146 amino acids
Theoretical weight: 16.63 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 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P212121
Unit cell:
a: 46.6Å b: 60.12Å c: 101.32Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.234 0.226 0.308
Expression system: Escherichia coli

Quick links

Citations

6 citation in other articles

Highly stable mutants of human fibroblast growth factor-1 exhibit prolonged biological action.
Zakrzewska et al. (2005)
5 more

1 mention without citation

Computational Analysis of Crystallization Additives for the Identification of New Allosteric Sites.
Fogha et al. (2020)