Structure analysis

Crystal structure of the kelch domain of human KLHL2 (Mayven)

X-ray diffraction
1.99Å resolution
Source organism: Homo sapiens
Assembly composition:
monomeric (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: monomeric
Accessible surface area: 11716.44 Å2
Buried surface area: 762.09 Å2
Dissociation area: 64.37 Å2
Dissociation energy (ΔGdiss): -0.89 kcal/mol
Dissociation entropy (TΔSdiss): -0.29 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-131857
Assembly 2
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Multimeric state: monomeric
Accessible surface area: 11713.0 Å2
Buried surface area: 766.92 Å2
Dissociation area: 73.17 Å2
Dissociation energy (ΔGdiss): -0.71 kcal/mol
Dissociation entropy (TΔSdiss): -0.32 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-131857

Macromolecules

Chains: A, B
Length: 302 amino acids
Theoretical weight: 32.83 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O95198 (Residues: 294-591; Coverage: 50%)
Gene name: KLHL2
Pfam: Kelch motif
InterPro:
CATH: Kelch-type beta propeller

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