Structure analysis

Crystal structure of N-terminal truncated human B12-chaperone CblD (108-296)

X-ray diffraction
1.9Å resolution
Source organism: Homo sapiens
Assembly composition:
homo dimer (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: homo dimer
Accessible surface area: 17848.2 Å2
Buried surface area: 2876.91 Å2
Dissociation area: 1,438.46 Å2
Dissociation energy (ΔGdiss): 13.71 kcal/mol
Dissociation entropy (TΔSdiss): 12.65 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-190580

Macromolecules

Chains: A, B
Length: 192 amino acids
Theoretical weight: 21.84 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q9H3L0 (Residues: 108-296; Coverage: 64%)
Gene names: C2orf25, CL25022, HSPC161, MMADHC, My011
Pfam: Methylmalonic aciduria and homocystinuria type D protein
InterPro: Methylmalonic aciduria and homocystinuria type D protein

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