Cobalt in PDB 2v3p: Crystallographic Analysis of Beta-Axial Ligand Substitutions in Cobalamin Bound to Transcobalamin

The structure of Crystallographic Analysis of Beta-Axial Ligand Substitutions in Cobalamin Bound to Transcobalamin, PDB code: 2v3p was solved by J.Wuerges, S.Geremia, L.Randaccio, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.98 / 2.90
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	100.390, 100.390, 129.742, 90.00, 90.00, 120.00
R / Rfree (%)	19.4 / 25

The structure of Crystallographic Analysis of Beta-Axial Ligand Substitutions in Cobalamin Bound to Transcobalamin also contains other interesting chemical elements:

Chlorine

(Cl)

3 atoms

The binding sites of Cobalt atom in the Crystallographic Analysis of Beta-Axial Ligand Substitutions in Cobalamin Bound to Transcobalamin (pdb code 2v3p). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total only one binding site of Cobalt was determined in the Crystallographic Analysis of Beta-Axial Ligand Substitutions in Cobalamin Bound to Transcobalamin, PDB code: 2v3p:

Cobalt binding site 1 out of 1 in the Crystallographic Analysis of Beta-Axial Ligand Substitutions in Cobalamin Bound to Transcobalamin


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of Crystallographic Analysis of Beta-Axial Ligand Substitutions in Cobalamin Bound to Transcobalamin within 5.0Å range: probe atom residue distance (Å) B Occ A:Co1415 b:30.2 occ:1.00 CO A:B121415 0.0 30.2 1.0 N21 A:B121415 1.9 29.9 1.0 N24 A:B121415 1.9 29.3 1.0 N23 A:B121415 1.9 30.2 1.0 N22 A:B121415 1.9 29.6 1.0 N3B A:B121415 2.1 29.4 1.0 S A:SO31419 2.3 34.8 0.5 C19 A:B121415 2.8 29.6 1.0 C9 A:B121415 2.8 28.8 1.0 C11 A:B121415 2.8 29.6 1.0 C1 A:B121415 2.9 29.7 1.0 C4 A:B121415 2.9 30.2 1.0 C16 A:B121415 2.9 28.8 1.0 C14 A:B121415 2.9 30.1 1.0 C6 A:B121415 3.0 29.2 1.0 C2B A:B121415 3.0 29.0 1.0 O3 A:SO31419 3.1 35.0 0.5 O1 A:SO31419 3.1 35.7 0.5 O2 A:SO31419 3.1 34.6 0.5 C9B A:B121415 3.2 29.8 1.0 C10 A:B121415 3.2 28.7 1.0 C5 A:B121415 3.3 29.1 1.0 C15 A:B121415 3.3 28.6 1.0 C20 A:B121415 3.6 29.9 1.0 C4B A:B121415 3.7 29.8 1.0 C2 A:B121415 4.0 29.1 1.0 C18 A:B121415 4.1 28.5 1.0 C8 A:B121415 4.1 28.4 1.0 C3 A:B121415 4.1 30.2 1.0 C12 A:B121415 4.2 29.0 1.0 C17 A:B121415 4.2 28.4 1.0 C13 A:B121415 4.2 30.7 1.0 N1B A:B121415 4.2 28.9 1.0 C7 A:B121415 4.3 29.0 1.0 C8B A:B121415 4.3 28.7 1.0 C26 A:B121415 4.4 27.4 1.0 C47 A:B121415 4.8 27.6 1.0 C35 A:B121415 4.8 28.2 1.0 C53 A:B121415 4.8 26.6 1.0 C41 A:B121415 4.9 26.7 1.0 C48 A:B121415 4.9 32.9 1.0

J.Wuerges, S.Geremia, S.N.Fedosov, L.Randaccio. Vitamin B12 Transport Proteins: Crystallographic Analysis of Beta-Axial Ligand Substitutions in Cobalamin Bound to Transcobalamin. Iubmb Life V. 59 722 2007.
ISSN: ISSN 1521-6543
PubMed: 17943552
DOI: 10.1080/15216540701673413