Structure analysis

MIF4G domain of DAP5

X-ray diffraction
2.3Å resolution
Source organism: Homo sapiens
Assemblies composition:
monomeric (preferred)
homo dimer
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1
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Multimeric state: monomeric
Accessible surface area: 13800 Å2
Buried surface area: 300 Å2
Dissociation area: 50 Å2
Dissociation energy (ΔGdiss): 8 kcal/mol
Dissociation entropy (TΔSdiss): 1 kcal/mol
Interface energy (ΔGint): -18 kcal/mol
Symmetry number: 1
Assembly 2 (preferred)
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Multimeric state: monomeric

Binding statistics and energies are not available for this assembly
Assembly 3
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Multimeric state: homo dimer

Binding statistics and energies are not available for this assembly

Macromolecules

Chains: A, B
Length: 268 amino acids
Theoretical weight: 30.74 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P78344 (Residues: 61-323; Coverage: 29%)
Gene names: DAP5, EIF4G2, OK/SW-cl.75
Pfam: MIF4G domain
InterPro:
CATH: Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat

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