Structure analysis

Crystal structure of C117I mutant of Human acidic fibroblast growth factor

X-ray diffraction
2Å 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: 6941.3 Å2
Buried surface area: 368.04 Å2
Dissociation area: 82.92 Å2
Dissociation energy (ΔGdiss): 13.46 kcal/mol
Dissociation entropy (TΔSdiss): 0.59 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-138603
Assembly 2 (preferred)
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Multimeric state: monomeric
Accessible surface area: 6796.36 Å2
Buried surface area: 190.52 Å2
Dissociation area: 95.26 Å2
Dissociation energy (ΔGdiss): 15.12 kcal/mol
Dissociation entropy (TΔSdiss): 0.61 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-138603

Macromolecules

Chains: A, B
Length: 146 amino acids
Theoretical weight: 16.7 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P05230 (Residues: 16-155; Coverage: 90%)
  • Best match: P05230-2 (Residues: 16-56)
Gene names: FGF1, FGFA
Pfam: Fibroblast growth factor
InterPro:
CATH: Trefoil (Acidic Fibroblast Growth Factor, subunit A)

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