Structure analysis

Crystal structure of K112N/N114A mutant of Human acidic fibroblast growth factor

X-ray diffraction
1.75Å resolution
Source organism: Homo sapiens
Assembly composition:
monomeric (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: monomeric
Accessible surface area: 6818.39 Å2
Buried surface area: 347.28 Å2
Dissociation area: 78.11 Å2
Dissociation energy (ΔGdiss): 1.96 kcal/mol
Dissociation entropy (TΔSdiss): -1.06 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-138603
Assembly 2
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Multimeric state: monomeric
Accessible surface area: 6673.77 Å2
Buried surface area: 354.48 Å2
Dissociation area: 81.45 Å2
Dissociation energy (ΔGdiss): 1.99 kcal/mol
Dissociation entropy (TΔSdiss): -1.06 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-138603

Macromolecules

Chains: A, B
Length: 146 amino acids
Theoretical weight: 16.63 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P05230 (Residues: 16-155; Coverage: 90%)
Gene names: FGF1, FGFA
Pfam: Fibroblast growth factor
InterPro:
CATH: Trefoil (Acidic Fibroblast Growth Factor, subunit A)

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