Structure analysis

Crystal structure of MID domain from hAGO2 in complex with AMP

X-ray diffraction
2.095Å 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: 7300 Å2
Buried surface area: 650 Å2
Dissociation area: 50 Å2
Dissociation energy (ΔGdiss): 3 kcal/mol
Dissociation entropy (TΔSdiss): 1 kcal/mol
Interface energy (ΔGint): -7 kcal/mol
Symmetry number: 1
Assembly 2
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Multimeric state: monomeric
Accessible surface area: 7200 Å2
Buried surface area: 700 Å2
Dissociation area: 100 Å2
Dissociation energy (ΔGdiss): 5 kcal/mol
Dissociation entropy (TΔSdiss): 1 kcal/mol
Interface energy (ΔGint): -6 kcal/mol
Symmetry number: 1
Assembly 3 (preferred)
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Multimeric state: monomeric
Accessible surface area: 7400 Å2
Buried surface area: 950 Å2
Dissociation area: 0 Å2
Dissociation energy (ΔGdiss): 0 kcal/mol
Dissociation entropy (TΔSdiss): 1 kcal/mol
Interface energy (ΔGint): -11 kcal/mol
Symmetry number: 1

Macromolecules

Chains: A, B, C
Length: 138 amino acids
Theoretical weight: 15.33 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9UKV8 (Residues: 439-575; Coverage: 16%)
Gene names: AGO2, EIF2C2
InterPro:
CATH: Rossmann fold

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