Structure analysis

SOLVING THE STRUCTURE OF HUMAN H FERRITIN BY GENETICALLY ENGINEERING INTERMOLECULAR CRYSTAL CONTACTS

X-ray diffraction
2.4Å resolution
Source organism: Homo sapiens
Assembly composition:
homo 24-mer (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: homo 24-mer
Accessible surface area: 135820.1 Å2
Buried surface area: 94643.98 Å2
Dissociation area: 542.63 Å2
Dissociation energy (ΔGdiss): 96.84 kcal/mol
Dissociation entropy (TΔSdiss): 0.42 kcal/mol
Symmetry number: 24
PDBe Complex ID: PDB-CPX-136244

Macromolecules

Chain: A
Length: 183 amino acids
Theoretical weight: 21.25 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P02794 (Residues: 1-183; Coverage: 100%)
Gene names: FTH, FTH1, FTHL6, OK/SW-cl.84, PIG15
Pfam: Ferritin-like domain
InterPro:
CATH: Ferritin
SCOP: Ferritin

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