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Magnesium in PDB 1qhx: Chloramphenicol Phosphotransferase in Complex with Atp From Streptomyces Venezuelae

Protein crystallography data

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

Resolution Low / High (Å) 99.00 / 2.50
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 (%) 22.8 / 23.8

Magnesium Binding Sites:

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

Magnesium binding site 1 out of 1 in 1qhx

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


Mono view


Stereo pair view

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

b:48.4
occ:1.00
OD2 A:ASP92 2.4 47.0 1.0
O1G A:ATP501 2.5 37.4 0.5
O2B A:ATP501 2.6 37.4 1.0
OG A:SER17 2.6 33.4 1.0
O A:HOH560 3.3 46.2 1.0
O A:HOH563 3.3 41.9 1.0
OD2 A:ASP37 3.4 63.5 1.0
PG A:ATP501 3.4 37.4 0.5
PB A:ATP501 3.5 37.4 1.0
CG A:ASP92 3.5 47.0 1.0
O3B A:ATP501 3.6 37.4 1.0
O2G A:ATP501 3.7 37.4 0.5
CE A:LYS16 3.9 30.3 1.0
N A:SER17 4.0 32.6 1.0
CB A:SER17 4.0 33.4 1.0
OD1 A:ASP92 4.0 47.0 1.0
O1B A:ATP501 4.1 37.4 1.0
CB A:LYS16 4.1 30.3 1.0
NZ A:LYS16 4.3 30.3 1.0
CG A:ASP37 4.4 63.5 1.0
CA A:SER17 4.5 32.6 1.0
CG1 A:VAL36 4.6 52.1 1.0
CB A:ASP92 4.7 47.0 1.0
O3G A:ATP501 4.8 37.4 0.5
C A:LYS16 4.8 33.3 1.0
O3A A:ATP501 4.8 37.4 0.5
OD1 A:ASP37 4.9 63.5 1.0
CA A:LYS16 4.9 33.3 1.0
CD A:LYS16 4.9 30.3 1.0
CG A:LYS16 5.0 30.3 1.0
O A:HOH589 5.0 37.5 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 11:51:59 2024

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