Magnesium 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:

Cobalt

(Co)

2 atoms

The binding sites of Magnesium 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 Magnesium atom.
In total 3 binding sites of Magnesium where determined in the E. Coli Glmu- Complex with Udp-Glcnac, Coa and Glcn-1-PO4, PDB code: 2oi6:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in the E. Coli Glmu- Complex with Udp-Glcnac, Coa and Glcn-1-PO4


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg 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:Mg6004 b:43.4 occ:0.33 OD1 A:ASP406 2.2 23.5 1.0 O A:HOH8388 2.3 19.5 1.0 CG A:ASP406 3.2 21.9 1.0 OD2 A:ASP406 3.5 24.0 1.0 CO A:CO6003 4.0 40.2 0.3 O A:HOH8147 4.3 23.0 1.0 O A:HOH8393 4.3 26.9 1.0 O A:GLY381 4.5 15.4 1.0 CB A:ASP406 4.5 18.6 1.0 CA A:ASP406 5.0 17.1 1.0

Magnesium binding site 2 out of 3 in the E. Coli Glmu- Complex with Udp-Glcnac, Coa and Glcn-1-PO4


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg 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:Mg6000 b:17.7 occ:1.00 OD1 B:ASN227 2.0 14.3 1.0 OD2 B:ASP105 2.0 14.3 1.0 O2A B:UD14001 2.2 14.8 1.0 O B:HOH8374 2.2 13.3 1.0 O B:HOH8218 2.2 14.1 1.0 O2B B:UD14001 2.2 15.7 1.0 CG B:ASN227 3.0 12.6 1.0 CG B:ASP105 3.1 15.4 1.0 PA B:UD14001 3.3 17.8 1.0 ND2 B:ASN227 3.3 12.4 1.0 PB B:UD14001 3.4 18.0 1.0 OD1 B:ASP105 3.5 13.8 1.0 O3A B:UD14001 3.5 16.3 1.0 NZ B:LYS25 3.6 20.2 1.0 O6' B:UD14001 4.0 18.2 1.0 O5B B:UD14001 4.2 17.0 1.0 O B:VAL226 4.2 14.2 1.0 O5' B:UD14001 4.2 17.4 1.0 C5B B:UD14001 4.3 17.0 1.0 O1B B:UD14001 4.3 17.8 1.0 CB B:ASN227 4.4 12.4 1.0 O1A B:UD14001 4.4 17.1 1.0 CB B:ASP105 4.4 12.9 1.0 O B:HOH8017 4.4 12.7 1.0 O1' B:UD14001 4.5 16.0 1.0 C B:VAL226 4.5 14.3 1.0 N B:VAL226 4.7 16.3 1.0 CA B:ASN227 4.7 14.5 1.0 C1' B:UD14001 4.7 16.8 1.0 N B:ASN227 4.8 14.2 1.0 C5' B:UD14001 4.8 17.1 1.0 C6' B:UD14001 5.0 20.3 1.0

Magnesium binding site 3 out of 3 in the E. Coli Glmu- Complex with Udp-Glcnac, Coa and Glcn-1-PO4


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 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:Mg6001 b:20.9 occ:0.33 OD1 B:ASP406 2.1 23.4 1.0 O B:HOH8389 2.3 18.3 1.0 CG B:ASP406 3.1 23.3 1.0 CO B:CO6002 3.4 43.6 0.3 OD2 B:ASP406 3.5 28.7 1.0 O B:HOH8399 4.2 28.2 1.0 CB B:ASP406 4.4 17.8 1.0 O B:GLY381 4.5 16.0 1.0 O B:HOH8403 4.5 21.8 1.0 CA B:ASP406 4.9 16.5 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