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Magnesium in PDB 1qhy: Chloramphenicol Phosphotransferase From Streptomyces Venezuelae in Complex with Atpgammas and Chloramphenicol

Protein crystallography data

The structure of Chloramphenicol Phosphotransferase From Streptomyces Venezuelae in Complex with Atpgammas and Chloramphenicol, PDB code: 1qhy was solved by T.Izard, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.60
Space group I 41 3 2
Cell size a, b, c (Å), α, β, γ (°) 200.000, 200.000, 200.000, 90.00, 90.00, 90.00
R / Rfree (%) 23.3 / 24.7

Other elements in 1qhy:

The structure of Chloramphenicol Phosphotransferase From Streptomyces Venezuelae in Complex with Atpgammas and Chloramphenicol also contains other interesting chemical elements:

Chlorine (Cl) 4 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Chloramphenicol Phosphotransferase From Streptomyces Venezuelae in Complex with Atpgammas and Chloramphenicol (pdb code 1qhy). 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 Chloramphenicol Phosphotransferase From Streptomyces Venezuelae in Complex with Atpgammas and Chloramphenicol, PDB code: 1qhy:

Magnesium binding site 1 out of 1 in 1qhy

Go back to Magnesium Binding Sites List in 1qhy
Magnesium binding site 1 out of 1 in the Chloramphenicol Phosphotransferase From Streptomyces Venezuelae in Complex with Atpgammas and Chloramphenicol


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Chloramphenicol Phosphotransferase From Streptomyces Venezuelae in Complex with Atpgammas and Chloramphenicol within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg500

b:49.0
occ:1.00
O2G A:AGS501 2.3 59.0 0.5
OD2 A:ASP92 2.5 69.1 1.0
OG A:SER17 2.5 57.8 1.0
O2B A:AGS501 2.6 59.0 1.0
CG A:ASP92 3.3 69.1 1.0
O A:HOH1007 3.4 47.0 1.0
OD1 A:ASP92 3.5 69.1 1.0
PB A:AGS501 3.5 59.0 1.0
O A:HOH1016 3.6 46.7 1.0
N A:SER17 3.8 37.4 1.0
O1B A:AGS501 3.8 59.0 1.0
CB A:SER17 3.8 57.8 1.0
O3B A:AGS501 3.9 59.0 1.0
CB A:LYS16 4.1 44.1 1.0
O3G A:AGS501 4.2 59.0 0.5
CE A:LYS16 4.2 44.1 1.0
CA A:SER17 4.2 37.4 1.0
OD2 A:ASP37 4.4 76.3 1.0
NZ A:LYS16 4.4 44.1 1.0
O A:HOH1028 4.5 46.5 1.0
CG A:ASP37 4.6 76.3 1.0
C A:LYS16 4.7 39.0 1.0
CB A:ASP92 4.7 69.1 1.0
O3A A:AGS501 4.8 59.0 0.5
S1G A:AGS501 4.9 59.0 0.5
OD1 A:ASP37 4.9 76.3 1.0
CA A:LYS16 4.9 39.0 1.0
O4 A:CLM999 4.9 88.3 1.0

Reference:

T.Izard, J.Ellis. The Crystal Structures of Chloramphenicol Phosphotransferase Reveal A Novel Inactivation Mechanism Embo J. V. 19 2690 2000.
ISSN: ISSN 0261-4189
PubMed: 10835366
DOI: 10.1093/EMBOJ/19.1.1
Page generated: Tue Aug 13 11:52:21 2024

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