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

Protein crystallography data

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

Other elements in 3qvf:

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

Magnesium Binding Sites:

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 3qvf

Go back to Magnesium Binding Sites List in 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

Reference:

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
Page generated: Mon Dec 14 08:43:23 2020

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