› 2v3p

X-ray diffraction
2.9Å resolution

Crystallographic analysis of beta-axial ligand substitutions in cobalamin bound to transcobalamin

Released:
DOI: 10.2210/pdb2v3p/pdb
PDB entry 2v3p coloured by chain, front view.
PDB entry 2v3p coloured by chain, side view.
PDB entry 2v3p coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
Vitamin B12 transport proteins: crystallographic analysis of beta-axial ligand substitutions in cobalamin bound to transcobalamin.
Wuerges J, Geremia S, Fedosov SN, Randaccio L
IUBMB Life 59 722-9 (2007)
PMID: 17943552

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-195034 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Transcobalamin-2 Chain: A
Molecule details ›
Chain: A
Length: 414 amino acids
Theoretical weight: 46.32 KDa
Source organism: Bos taurus
Expression system: Komagataella pastoris
UniProt:
  • Canonical: Q9XSC9 (Residues: 19-432; Coverage: 100%)
Gene name: TCN2
Sequence domains: Eukaryotic cobalamin-binding protein
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand B12 1 x B12
Ligand CL 3 x CL
Ligand SO3 1 x SO3
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ELETTRA BEAMLINE 5.2R
Spacegroup: P3121
Unit cell:
a: 100.39Å b: 100.39Å c: 129.742Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.196 0.194 0.25
Expression system: Komagataella pastoris

Quick links

Citations

6 review citations

Advances in the understanding of cobalamin assimilation and metabolism.
Quadros EV. (2010)
5 more