Magnesium in PDB 3qvf: Crystal Structure of Fosfomycin Resistance Kinase Foma From Streptomyces Wedmorensis Complexed with Mgadp and Fosfomycin Vanadate

The structure of Crystal Structure of Fosfomycin Resistance Kinase Foma From Streptomyces Wedmorensis Complexed with Mgadp and Fosfomycin Vanadate, PDB code: 3qvf was solved by S.Pakhomova, S.G.Bartlett, P.A.Doerner, M.E.Newcomer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	27.32 / 1.85
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	87.380, 87.380, 79.000, 90.00, 90.00, 120.00
R / Rfree (%)	16.4 / 21.9

The structure of Crystal Structure of Fosfomycin Resistance Kinase Foma From Streptomyces Wedmorensis Complexed with Mgadp and Fosfomycin Vanadate also contains other interesting chemical elements:

Vanadium

(V)

1 atom

The binding sites of Magnesium atom in the Crystal Structure of Fosfomycin Resistance Kinase Foma From Streptomyces Wedmorensis Complexed with Mgadp and Fosfomycin Vanadate (pdb code 3qvf). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Crystal Structure of Fosfomycin Resistance Kinase Foma From Streptomyces Wedmorensis Complexed with Mgadp and Fosfomycin Vanadate, PDB code: 3qvf:

Magnesium binding site 1 out of 1 in the Crystal Structure of Fosfomycin Resistance Kinase Foma From Streptomyces Wedmorensis Complexed with Mgadp and Fosfomycin Vanadate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Fosfomycin Resistance Kinase Foma From Streptomyces Wedmorensis Complexed with Mgadp and Fosfomycin Vanadate within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg5000 b:43.4 occ:1.00 O A:HOH357 2.0 26.4 1.0 O A:HOH375 2.0 30.4 1.0 O A:HOH330 2.1 30.2 1.0 O1B A:ADP1260 2.1 43.6 1.0 O2A A:ADP1260 2.2 44.6 1.0 O3 A:FV14001 2.4 47.6 1.0 PB A:ADP1260 3.4 44.9 1.0 PA A:ADP1260 3.4 44.8 1.0 OD2 A:ASP150 3.4 52.6 1.0 V A:FV14001 3.6 66.0 1.0 O3A A:ADP1260 3.7 44.9 1.0 O2 A:FV14001 3.7 38.9 1.0 OD2 A:ASP208 3.9 62.6 1.0 NZ A:LYS216 3.9 41.0 1.0 OG1 A:THR210 4.1 42.4 1.0 O3B A:ADP1260 4.1 48.1 1.0 CA A:ALA212 4.2 39.6 1.0 O5' A:ADP1260 4.2 41.6 1.0 O3P A:FV14001 4.3 31.9 1.0 CG A:ASP150 4.5 37.6 1.0 O2B A:ADP1260 4.5 46.4 1.0 O A:ALA212 4.5 37.4 1.0 O1A A:ADP1260 4.5 41.8 1.0 NZ A:LYS9 4.6 35.9 1.0 N A:ALA212 4.6 40.3 1.0 NZ A:LYS18 4.6 64.8 1.0 CE A:LYS216 4.6 38.2 1.0 C A:ALA212 4.7 35.9 1.0 O2P A:FV14001 4.7 34.2 1.0 O A:HOH399 4.7 37.0 1.0 OD1 A:ASP150 4.8 37.9 1.0 NE2 A:HIS58 4.8 49.6 1.0 CG A:ASP208 5.0 61.1 1.0 OG A:SER148 5.0 30.3 1.0

S.Pakhomova, S.G.Bartlett, P.A.Doerner, M.E.Newcomer. Structural and Biochemical Insights Into the Mechanism of Fosfomycin Phosphorylation By Fosfomycin Resistance Kinase Foma. Biochemistry V. 50 6909 2011.
ISSN: ISSN 0006-2960
PubMed: 21728358
DOI: 10.1021/BI2004334