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X-ray diffraction
1.95Å resolution

Crystal Structure of a Multiple Mutant (L44F, L73V, V109L, L111I, C117V) of Human Acidic Fibroblast Growth Factor

Released:
Source organism: Homo sapiens
Primary publication:
Accommodation of a highly symmetric core within a symmetric protein superfold.
Protein Sci 12 2704-18 (2003)
PMID: 14627732

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-138603 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fibroblast growth factor 1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 143 amino acids
Theoretical weight: 16.43 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P05230 (Residues: 16-152; Coverage: 88%)
Gene names: FGF1, FGFA
Sequence domains: Fibroblast growth factor
Structure domains: Trefoil (Acidic Fibroblast Growth Factor, subunit A)

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: C2
Unit cell:
a: 96.747Å b: 74.033Å c: 109.085Å
α: 90° β: 89.98° γ: 90°
R-values:
R R work R free
0.196 0.194 0.253
Expression system: Escherichia coli