Cobalt in PDB 2oi6: E. Coli Glmu- Complex with Udp-Glcnac, Coa and Glcn-1-PO4

All present enzymatic activity of E. Coli Glmu- Complex with Udp-Glcnac, Coa and Glcn-1-PO4:
2.3.1.157; 2.7.7.23;

The structure of E. Coli Glmu- Complex with Udp-Glcnac, Coa and Glcn-1-PO4, PDB code: 2oi6 was solved by L.R.Olsen, M.W.Vetting, S.L.Roderick, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	38.96 / 2.20
Space group	H 3 2
Cell size a, b, c (Å), α, β, γ (°)	102.760, 102.760, 644.828, 90.00, 90.00, 120.00
R / Rfree (%)	17.8 / 20.8

The structure of E. Coli Glmu- Complex with Udp-Glcnac, Coa and Glcn-1-PO4 also contains other interesting chemical elements:

Magnesium

(Mg)

3 atoms

The binding sites of Cobalt atom in the E. Coli Glmu- Complex with Udp-Glcnac, Coa and Glcn-1-PO4 (pdb code 2oi6). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total 2 binding sites of Cobalt where determined in the E. Coli Glmu- Complex with Udp-Glcnac, Coa and Glcn-1-PO4, PDB code: 2oi6:
Jump to Cobalt binding site number: 1; 2;

Cobalt binding site 1 out of 2 in the E. Coli Glmu- Complex with Udp-Glcnac, Coa and Glcn-1-PO4


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of E. Coli Glmu- Complex with Udp-Glcnac, Coa and Glcn-1-PO4 within 5.0Å range: probe atom residue distance (Å) B Occ A:Co6003 b:40.2 occ:0.33 OD2 A:ASP406 2.0 24.0 1.0 O A:HOH8454 2.3 32.5 1.0 CG A:ASP406 3.0 21.9 1.0 OD1 A:ASP406 3.4 23.5 1.0 OE1 A:GLN408 3.6 29.0 1.0 MG A:MG6004 4.0 43.4 0.3 CB A:ASP406 4.2 18.6 1.0 O A:ASP406 4.2 18.2 1.0 O A:HOH8393 4.8 26.9 1.0 CD A:GLN408 4.9 24.5 1.0

Cobalt binding site 2 out of 2 in the E. Coli Glmu- Complex with Udp-Glcnac, Coa and Glcn-1-PO4


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 2 of E. Coli Glmu- Complex with Udp-Glcnac, Coa and Glcn-1-PO4 within 5.0Å range: probe atom residue distance (Å) B Occ B:Co6002 b:43.6 occ:0.33 OD2 B:ASP406 2.1 28.7 1.0 O B:HOH8543 2.5 41.5 1.0 CG B:ASP406 2.9 23.3 1.0 OD1 B:ASP406 3.1 23.4 1.0 MG B:MG6001 3.4 20.9 0.3 NE2 B:GLN408 3.8 29.6 1.0 O B:ASP406 4.2 16.6 1.0 CB B:ASP406 4.3 17.8 1.0 O B:HOH8399 4.6 28.2 1.0 O B:HOH8502 4.6 36.3 1.0 CD B:GLN408 4.9 27.9 1.0

L.R.Olsen, M.W.Vetting, S.L.Roderick. Structure of the E. Coli Bifunctional Glmu Acetyltransferase Active Site with Substrates and Products. Protein Sci. V. 16 1230 2007.
ISSN: ISSN 0961-8368
PubMed: 17473010
DOI: 10.1110/PS.072779707