Cobalt in PDB 2v0h: Characterization of Substrate Binding and Catalysis of the Potential Antibacterial Target N-Acetylglucosamine-1- Phosphate Uridyltransferase (Glmu)

The structure of Characterization of Substrate Binding and Catalysis of the Potential Antibacterial Target N-Acetylglucosamine-1- Phosphate Uridyltransferase (Glmu), PDB code: 2v0h was solved by I.Mochalkin, S.Lightle, J.F.Ohren, N.Y.Chirgadze, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	111.80 / 1.79
Space group	H 3 2
Cell size a, b, c (Å), α, β, γ (°)	108.459, 108.459, 327.154, 90.00, 90.00, 120.00
R / Rfree (%)	19.1 / 21.4

The binding sites of Cobalt atom in the Characterization of Substrate Binding and Catalysis of the Potential Antibacterial Target N-Acetylglucosamine-1- Phosphate Uridyltransferase (Glmu) (pdb code 2v0h). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total 2 binding sites of Cobalt where determined in the Characterization of Substrate Binding and Catalysis of the Potential Antibacterial Target N-Acetylglucosamine-1- Phosphate Uridyltransferase (Glmu), PDB code: 2v0h:
Jump to Cobalt binding site number: 1; 2;

Cobalt binding site 1 out of 2 in the Characterization of Substrate Binding and Catalysis of the Potential Antibacterial Target N-Acetylglucosamine-1- Phosphate Uridyltransferase (Glmu)


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of Characterization of Substrate Binding and Catalysis of the Potential Antibacterial Target N-Acetylglucosamine-1- Phosphate Uridyltransferase (Glmu) within 5.0Å range: probe atom residue distance (Å) B Occ A:Co1463 b:13.9 occ:0.33 OD1 A:ASP406 2.1 12.8 1.0 O A:HOH2496 2.1 14.1 1.0 CG A:ASP406 3.1 13.2 1.0 OD2 A:ASP406 3.4 7.8 0.3 CO A:CO1464 3.9 15.6 0.3 O A:HOH2388 4.3 16.1 1.0 CB A:ASP406 4.4 13.3 1.0 O A:GLY381 4.5 13.0 1.0 O A:HOH2372 4.5 20.9 1.0 CA A:ASP406 4.9 13.6 1.0

Cobalt binding site 2 out of 2 in the Characterization of Substrate Binding and Catalysis of the Potential Antibacterial Target N-Acetylglucosamine-1- Phosphate Uridyltransferase (Glmu)


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 2 of Characterization of Substrate Binding and Catalysis of the Potential Antibacterial Target N-Acetylglucosamine-1- Phosphate Uridyltransferase (Glmu) within 5.0Å range: probe atom residue distance (Å) B Occ A:Co1464 b:15.6 occ:0.33 OD2 A:ASP406 2.0 7.8 0.3 O A:HOH2497 2.2 15.7 1.0 CG A:ASP406 3.0 13.2 1.0 OD1 A:ASP406 3.4 12.8 1.0 CO A:CO1463 3.9 13.9 0.3 OE1 A:GLN408 4.0 19.1 1.0 O A:ASP406 4.0 14.7 1.0 O A:HOH2432 4.1 27.7 1.0 CB A:ASP406 4.2 13.3 1.0 O A:HOH2388 4.8 16.1 1.0 C A:ASP406 4.9 14.0 1.0

I.Mochalkin, S.Lightle, Y.Zhu, J.F.Ohren, C.Spessard, N.Y.Chirgadze, C.Banotai, M.Melnick, L.Mcdowell. Characterization of Substrate Binding and Catalysis in the Potential Antibacterial Target N- Acetylglucosamine-1-Phosphate Uridyltransferase (Glmu). Protein Sci. V. 16 2657 2007.
ISSN: ISSN 0961-8368
PubMed: 18029420
DOI: 10.1110/PS.073135107