PDBe 5cuz

X-ray diffraction
2.31Å resolution

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


Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Methylmalonic aciduria and homocystinuria type D protein, mitochondrial Chain: A
Molecule details ›
Chain: A
Length: 192 amino acids
Theoretical weight: 22.07 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
  • Canonical: Q9H3L0 (Residues: 108-296; Coverage: 64%)
Gene names: C2orf25, CL25022, HSPC161, MMADHC, My011

Ligands and Environments

No bound ligands

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-B
Spacegroup: I222
Unit cell:
a: 65.341Å b: 66.226Å c: 71.885Å
α: 90° β: 90° γ: 90°
R R work R free
0.211 0.208 0.263
Expression system: Escherichia coli BL21