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Magnesium in PDB 3qun: Crystal Structure of Fosfomycin Resistance Kinase Foma From Streptomyces Wedmorensis Complexed with Mgatp

Protein crystallography data

The structure of Crystal Structure of Fosfomycin Resistance Kinase Foma From Streptomyces Wedmorensis Complexed with Mgatp, PDB code: 3qun 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) 23.01 / 1.87
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 85.876, 85.876, 80.152, 90.00, 90.00, 120.00
R / Rfree (%) 18.5 / 20.5

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Fosfomycin Resistance Kinase Foma From Streptomyces Wedmorensis Complexed with Mgatp (pdb code 3qun). 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 Mgatp, PDB code: 3qun:

Magnesium binding site 1 out of 1 in 3qun

Go back to Magnesium Binding Sites List in 3qun
Magnesium binding site 1 out of 1 in the Crystal Structure of Fosfomycin Resistance Kinase Foma From Streptomyces Wedmorensis Complexed with Mgatp


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 Mgatp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg2026

b:59.9
occ:1.00
O2G A:ATP1260 2.2 60.9 1.0
O2A A:ATP1260 2.2 54.5 1.0
O1B A:ATP1260 2.8 53.6 1.0
O3 A:GOL3545 2.9 51.5 1.0
O A:HOH297 3.1 43.3 1.0
C3 A:GOL3545 3.1 52.9 1.0
PA A:ATP1260 3.5 53.4 1.0
PG A:ATP1260 3.6 65.1 1.0
C2 A:GOL3545 3.7 52.4 1.0
PB A:ATP1260 4.0 54.9 1.0
OD2 A:ASP150 4.0 40.5 1.0
O1G A:ATP1260 4.0 47.2 1.0
NZ A:LYS216 4.1 37.1 1.0
O3A A:ATP1260 4.1 51.9 1.0
CA A:ALA212 4.2 43.1 1.0
O3B A:ATP1260 4.3 53.5 1.0
CB A:ALA212 4.4 44.5 1.0
O1A A:ATP1260 4.4 52.6 1.0
O2 A:GOL3545 4.4 58.2 1.0
O5' A:ATP1260 4.5 51.5 1.0
O A:ALA212 4.7 37.6 1.0
O3G A:ATP1260 4.7 62.6 1.0
C A:ALA212 4.8 39.3 1.0
O1 A:GOL3545 4.8 51.1 1.0
C1 A:GOL3545 4.9 51.2 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: Thu Aug 15 10:10:48 2024

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