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Cobalt in PDB 2bb5: Structure of Human Transcobalamin in Complex with Cobalamin

Protein crystallography data

The structure of Structure of Human Transcobalamin in Complex with Cobalamin, PDB code: 2bb5 was solved by J.Wuerges, G.Garau, S.Geremia, S.N.Fedosov, T.E.Petersen, L.Randaccio, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 3.20
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 49.127, 145.497, 165.043, 90.00, 90.00, 90.00
R / Rfree (%) 25.7 / 28.8

Cobalt Binding Sites:

The binding sites of Cobalt atom in the Structure of Human Transcobalamin in Complex with Cobalamin (pdb code 2bb5). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total 2 binding sites of Cobalt where determined in the Structure of Human Transcobalamin in Complex with Cobalamin, PDB code: 2bb5:
Jump to Cobalt binding site number: 1; 2;

Cobalt binding site 1 out of 2 in 2bb5

Go back to Cobalt Binding Sites List in 2bb5
Cobalt binding site 1 out of 2 in the Structure of Human Transcobalamin in Complex with Cobalamin


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of Structure of Human Transcobalamin in Complex with Cobalamin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Co0

b:23.2
occ:1.00
CO A:B120 0.0 23.2 1.0
N21 A:B120 1.9 22.6 1.0
N22 A:B120 1.9 23.8 1.0
N24 A:B120 1.9 22.3 1.0
N23 A:B120 1.9 23.8 1.0
N3B A:B120 2.1 23.1 1.0
C9 A:B120 2.8 24.5 1.0
NE2 A:HIS173 2.8 58.1 1.0
C19 A:B120 2.8 21.4 1.0
C11 A:B120 2.8 24.8 1.0
C1 A:B120 2.9 21.2 1.0
C4 A:B120 2.9 22.8 1.0
C16 A:B120 2.9 21.8 1.0
C6 A:B120 3.0 23.8 1.0
C14 A:B120 3.0 23.7 1.0
C2B A:B120 3.0 23.4 1.0
C10 A:B120 3.1 25.2 1.0
C9B A:B120 3.2 22.9 1.0
C5 A:B120 3.3 23.4 1.0
C15 A:B120 3.4 22.7 1.0
C20 A:B120 3.6 20.0 1.0
CD2 A:HIS173 3.6 56.5 1.0
C4B A:B120 3.8 23.4 1.0
CE1 A:HIS173 3.8 60.7 1.0
C8 A:B120 4.1 24.6 1.0
C2 A:B120 4.1 21.1 1.0
C18 A:B120 4.1 20.4 1.0
C12 A:B120 4.2 25.4 1.0
C3 A:B120 4.2 21.9 1.0
N1B A:B120 4.2 23.1 1.0
C17 A:B120 4.2 20.5 1.0
C13 A:B120 4.2 24.8 1.0
C7 A:B120 4.2 24.1 1.0
C8B A:B120 4.3 23.0 1.0
C26 A:B120 4.4 21.8 1.0
C41 A:B120 4.7 24.1 1.0
C46 A:B120 4.7 25.8 1.0
C35 A:B120 4.8 23.7 1.0
CG A:HIS173 4.8 57.5 1.0
C53 A:B120 4.8 22.4 1.0
ND1 A:HIS173 4.9 60.7 1.0

Cobalt binding site 2 out of 2 in 2bb5

Go back to Cobalt Binding Sites List in 2bb5
Cobalt binding site 2 out of 2 in the Structure of Human Transcobalamin in Complex with Cobalamin


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 2 of Structure of Human Transcobalamin in Complex with Cobalamin within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Co410

b:25.1
occ:1.00
CO B:B12410 0.0 25.1 1.0
N21 B:B12410 1.9 23.1 1.0
N23 B:B12410 1.9 25.8 1.0
N24 B:B12410 1.9 24.3 1.0
N22 B:B12410 1.9 24.9 1.0
N3B B:B12410 2.1 25.1 1.0
NE2 B:HIS173 2.8 51.7 1.0
C9 B:B12410 2.8 25.9 1.0
C11 B:B12410 2.8 26.7 1.0
C19 B:B12410 2.8 22.9 1.0
C4 B:B12410 2.9 22.5 1.0
C1 B:B12410 2.9 22.1 1.0
C16 B:B12410 2.9 24.5 1.0
C14 B:B12410 2.9 26.4 1.0
C6 B:B12410 3.0 24.5 1.0
C2B B:B12410 3.0 26.0 1.0
C10 B:B12410 3.1 26.7 1.0
C9B B:B12410 3.2 24.6 1.0
C5 B:B12410 3.3 23.4 1.0
C15 B:B12410 3.4 25.9 1.0
CD2 B:HIS173 3.5 51.5 1.0
C20 B:B12410 3.6 21.7 1.0
C4B B:B12410 3.8 24.2 1.0
CE1 B:HIS173 3.9 53.7 1.0
C2 B:B12410 4.1 21.3 1.0
C8 B:B12410 4.1 25.8 1.0
C18 B:B12410 4.1 22.7 1.0
C12 B:B12410 4.1 27.9 1.0
C3 B:B12410 4.1 21.4 1.0
C13 B:B12410 4.2 27.6 1.0
N1B B:B12410 4.2 26.0 1.0
C17 B:B12410 4.2 23.4 1.0
C7 B:B12410 4.2 25.1 1.0
C8B B:B12410 4.3 25.1 1.0
C26 B:B12410 4.4 22.3 1.0
C46 B:B12410 4.7 28.1 1.0
CG B:HIS173 4.7 52.7 1.0
C41 B:B12410 4.8 25.6 1.0
C35 B:B12410 4.8 22.5 1.0
C53 B:B12410 4.8 26.6 1.0
ND1 B:HIS173 4.9 54.8 1.0
C48 B:B12410 4.9 28.4 1.0

Reference:

J.Wuerges, G.Garau, S.Geremia, S.N.Fedosov, T.E.Petersen, L.Randaccio. Structural Basis For Mammalian Vitamin B12 Transport By Transcobalamin. Proc.Natl.Acad.Sci.Usa V. 103 4386 2006.
ISSN: ISSN 0027-8424
PubMed: 16537422
DOI: 10.1073/PNAS.0509099103
Page generated: Sun Dec 13 10:37:09 2020

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