Cobalt in PDB 1n4a: The Ligand Bound Structure of E.Coli Btuf, the Periplasmic Binding Protein For Vitamin B12

The structure of The Ligand Bound Structure of E.Coli Btuf, the Periplasmic Binding Protein For Vitamin B12, PDB code: 1n4a was solved by N.K.Karpowich, P.C.Smith, J.F.Hunt, Northeast Structural Genomicsconsortium (Nesg), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.00
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	131.730, 92.020, 44.690, 90.00, 90.00, 90.00
R / Rfree (%)	23.4 / 26.1

The binding sites of Cobalt atom in the The Ligand Bound Structure of E.Coli Btuf, the Periplasmic Binding Protein For Vitamin B12 (pdb code 1n4a). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total 2 binding sites of Cobalt where determined in the The Ligand Bound Structure of E.Coli Btuf, the Periplasmic Binding Protein For Vitamin B12, PDB code: 1n4a:
Jump to Cobalt binding site number: 1; 2;

Cobalt binding site 1 out of 2 in the The Ligand Bound Structure of E.Coli Btuf, the Periplasmic Binding Protein For Vitamin B12


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of The Ligand Bound Structure of E.Coli Btuf, the Periplasmic Binding Protein For Vitamin B12 within 5.0Å range: probe atom residue distance (Å) B Occ A:Co501 b:13.0 occ:1.00 CO A:CNC501 0.0 13.0 1.0 N24 A:CNC501 1.9 15.6 1.0 N21 A:CNC501 1.9 16.6 1.0 N23 A:CNC501 1.9 15.0 1.0 N22 A:CNC501 1.9 15.1 1.0 C1A A:CNC501 1.9 21.9 1.0 N3B A:CNC501 2.2 17.9 1.0 C19 A:CNC501 2.8 17.2 1.0 C9 A:CNC501 2.9 14.6 1.0 C11 A:CNC501 2.9 13.4 1.0 C1 A:CNC501 2.9 15.2 1.0 C4 A:CNC501 2.9 15.3 1.0 C16 A:CNC501 2.9 15.6 1.0 C14 A:CNC501 3.0 15.6 1.0 C6 A:CNC501 3.0 16.5 1.0 N1A A:CNC501 3.1 25.0 1.0 C2B A:CNC501 3.1 15.6 1.0 C10 A:CNC501 3.2 12.3 1.0 C9B A:CNC501 3.3 17.4 1.0 C5 A:CNC501 3.4 14.7 1.0 C15 A:CNC501 3.4 14.8 1.0 C20 A:CNC501 3.5 16.1 1.0 C4B A:CNC501 3.8 18.0 1.0 C18 A:CNC501 4.1 16.5 1.0 C2 A:CNC501 4.1 16.9 1.0 C17 A:CNC501 4.2 18.0 1.0 C12 A:CNC501 4.2 15.8 1.0 C3 A:CNC501 4.2 16.4 1.0 C8 A:CNC501 4.2 15.7 1.0 C13 A:CNC501 4.3 14.5 1.0 C7 A:CNC501 4.3 14.9 1.0 N1B A:CNC501 4.3 18.4 1.0 C8B A:CNC501 4.4 16.7 1.0 C26 A:CNC501 4.6 20.2 1.0 OE2 A:GLU223 4.6 31.1 1.0 C54 A:CNC501 4.8 18.7 1.0 C46 A:CNC501 4.8 16.4 1.0 C35 A:CNC501 4.9 15.0 1.0 C53 A:CNC501 4.9 14.0 1.0 C37 A:CNC501 5.0 16.4 1.0 C48 A:CNC501 5.0 18.1 1.0

Cobalt binding site 2 out of 2 in the The Ligand Bound Structure of E.Coli Btuf, the Periplasmic Binding Protein For Vitamin B12


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 2 of The Ligand Bound Structure of E.Coli Btuf, the Periplasmic Binding Protein For Vitamin B12 within 5.0Å range: probe atom residue distance (Å) B Occ B:Co5501 b:27.9 occ:1.00 CO B:CNC5501 0.0 27.9 1.0 N21 B:CNC5501 1.9 34.7 1.0 N24 B:CNC5501 1.9 36.9 1.0 N23 B:CNC5501 1.9 32.4 1.0 N22 B:CNC5501 1.9 30.0 1.0 C1A B:CNC5501 2.0 35.4 1.0 N3B B:CNC5501 2.2 30.6 1.0 C19 B:CNC5501 2.8 38.1 1.0 C9 B:CNC5501 2.9 26.5 1.0 C11 B:CNC5501 2.9 29.9 1.0 C2B B:CNC5501 2.9 31.3 1.0 C1 B:CNC5501 2.9 37.7 1.0 C4 B:CNC5501 2.9 34.7 1.0 C16 B:CNC5501 3.0 37.8 1.0 C14 B:CNC5501 3.0 33.1 1.0 C6 B:CNC5501 3.0 28.6 1.0 N1A B:CNC5501 3.1 36.1 1.0 C10 B:CNC5501 3.2 28.2 1.0 C9B B:CNC5501 3.4 30.7 1.0 C5 B:CNC5501 3.4 31.6 1.0 C15 B:CNC5501 3.4 36.1 1.0 C20 B:CNC5501 3.5 38.4 1.0 C4B B:CNC5501 4.1 28.4 1.0 C2 B:CNC5501 4.1 38.9 1.0 C18 B:CNC5501 4.1 42.2 1.0 N1B B:CNC5501 4.2 32.5 1.0 C3 B:CNC5501 4.2 37.9 1.0 C12 B:CNC5501 4.2 29.9 1.0 C17 B:CNC5501 4.2 42.0 1.0 C8 B:CNC5501 4.2 24.1 1.0 C13 B:CNC5501 4.2 31.2 1.0 C7 B:CNC5501 4.3 25.0 1.0 C8B B:CNC5501 4.4 30.0 1.0 C26 B:CNC5501 4.5 40.7 1.0 C35 B:CNC5501 4.9 29.8 1.0 C46 B:CNC5501 4.9 30.2 1.0 C54 B:CNC5501 4.9 42.5 1.0 C53 B:CNC5501 4.9 36.6 1.0 C37 B:CNC5501 5.0 23.7 1.0

N.K.Karpowich, H.H.Huang, P.C.Smith, J.F.Hunt. Crystal Structures of the Btuf Periplasmic-Binding Protein For Vitamin B12 Suggest A Functionally Important Reduction in Protein Mobility Upon Ligand Binding. J.Biol.Chem. V. 278 8429 2003.
ISSN: ISSN 0021-9258
PubMed: 12468528
DOI: 10.1074/JBC.M212239200