Structure analysis

Crystal Structure Analysis of FGF1-Disaccharide(NI23) complex

X-ray diffraction
2.34Å resolution
Source organism: Homo sapiens
Assembly composition:
monomeric (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1
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Multimeric state: monomeric
Accessible surface area: 6338.68 Å2
Buried surface area: 439.1 Å2
Dissociation area: 129.57 Å2
Dissociation energy (ΔGdiss): 10.29 kcal/mol
Dissociation entropy (TΔSdiss): 0.64 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-138603
Assembly 2 (preferred)
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Multimeric state: monomeric
Accessible surface area: 6616.96 Å2
Buried surface area: 202.92 Å2
Dissociation area: 101.46 Å2
Dissociation energy (ΔGdiss): -3.81 kcal/mol
Dissociation entropy (TΔSdiss): 4.09 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-138603
Assembly 3
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Multimeric state: monomeric
Accessible surface area: 6502.67 Å2
Buried surface area: 309.17 Å2
Dissociation area: 61.21 Å2
Dissociation energy (ΔGdiss): 3.78 kcal/mol
Dissociation entropy (TΔSdiss): 0.62 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-138603

Macromolecules

Chains: A, B, C
Length: 141 amino acids
Theoretical weight: 15.99 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
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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