PDBe 5cv0

X-ray diffraction
1.9Å resolution

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

Released:

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
Macromolecule:
Methylmalonic aciduria and homocystinuria type D protein, mitochondrial Chains: A, B
Molecule details ›
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

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-B
Spacegroup: P21
Unit cell:
a: 47.638Å b: 67.111Å c: 66.219Å
α: 90° β: 110.54° γ: 90°
R-values:
R R work R free
0.188 0.186 0.227
Expression system: Escherichia coli BL21