Atomistry » Magnesium » PDB 1enn-1f6n » 1f48
Atomistry »
  Magnesium »
    PDB 1enn-1f6n »
      1f48 »

Magnesium in PDB 1f48: Crystal Structure of the Escherichia Coli Arsenite-Translocating Atpase

Protein crystallography data

The structure of Crystal Structure of the Escherichia Coli Arsenite-Translocating Atpase, PDB code: 1f48 was solved by T.Zhou, S.Radaev, B.P.Rosen, D.L.Gatti, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 26.37 / 2.30
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 73.523, 75.715, 222.714, 90.00, 90.00, 90.00
R / Rfree (%) 20.6 / 26.3

Other elements in 1f48:

The structure of Crystal Structure of the Escherichia Coli Arsenite-Translocating Atpase also contains other interesting chemical elements:

Cadmium (Cd) 6 atoms
Antimony (Sb) 4 atoms
Chlorine (Cl) 3 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of the Escherichia Coli Arsenite-Translocating Atpase (pdb code 1f48). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of the Escherichia Coli Arsenite-Translocating Atpase, PDB code: 1f48:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 1f48

Go back to Magnesium Binding Sites List in 1f48
Magnesium binding site 1 out of 2 in the Crystal Structure of the Escherichia Coli Arsenite-Translocating Atpase


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 the Escherichia Coli Arsenite-Translocating Atpase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg592

b:32.1
occ:1.00
OD1 A:ASP45 2.0 41.6 1.0
O3B A:ADP590 2.1 30.5 1.0
O A:HOH905 2.1 44.9 1.0
OG1 A:THR22 2.2 35.1 1.0
O A:HOH906 2.3 26.4 1.0
O A:HOH911 2.3 46.3 1.0
CG A:ASP45 3.0 44.3 1.0
PB A:ADP590 3.2 34.7 1.0
OD2 A:ASP45 3.3 41.2 1.0
CB A:THR22 3.4 31.0 1.0
O2B A:ADP590 3.4 32.1 1.0
O2A A:ADP590 4.0 36.1 1.0
N A:THR22 4.0 28.4 1.0
OD2 A:ASP142 4.1 35.1 1.0
O A:HOH873 4.2 53.1 1.0
O3A A:ADP590 4.3 33.5 1.0
CB A:ASP45 4.3 41.3 1.0
CA A:THR22 4.3 27.7 1.0
O1B A:ADP590 4.3 33.7 1.0
CG2 A:THR22 4.4 33.8 1.0
PA A:ADP590 4.6 32.9 1.0
NZ A:LYS21 4.7 29.8 1.0
CG A:ASP142 4.7 36.0 1.0
O A:HOH872 4.7 37.6 1.0
O A:ASP142 4.8 27.2 1.0
CB A:LYS21 4.8 33.6 1.0
OG1 A:THR502 4.8 32.0 1.0
CE A:LYS21 4.8 34.4 1.0
O A:HOH784 4.9 60.7 1.0

Magnesium binding site 2 out of 2 in 1f48

Go back to Magnesium Binding Sites List in 1f48
Magnesium binding site 2 out of 2 in the Crystal Structure of the Escherichia Coli Arsenite-Translocating Atpase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of the Escherichia Coli Arsenite-Translocating Atpase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg593

b:35.0
occ:1.00
O A:HOH722 2.1 34.8 1.0
O3B A:ADP591 2.2 31.3 1.0
O A:HOH908 2.3 41.9 1.0
O A:HOH907 2.3 35.9 1.0
OG1 A:THR341 2.3 32.3 1.0
O A:HOH725 2.3 38.3 1.0
PB A:ADP591 3.5 38.6 1.0
CB A:THR341 3.5 29.8 1.0
O2B A:ADP591 3.7 38.1 1.0
OD2 A:ASP447 4.0 35.9 1.0
O A:HOH812 4.0 42.0 1.0
O A:HOH852 4.0 57.2 1.0
O3A A:ADP591 4.2 40.1 1.0
N A:THR341 4.3 37.5 1.0
O2A A:ADP591 4.4 35.7 1.0
CA A:THR341 4.4 34.2 1.0
CB A:ASP364 4.5 75.5 1.0
O A:HOH820 4.5 54.0 1.0
CG2 A:THR341 4.5 31.2 1.0
CG A:ASP447 4.6 36.0 1.0
OG A:SER363 4.6 68.1 1.0
O1B A:ADP591 4.7 35.0 1.0
OD1 A:ASP364 4.7 73.4 1.0
O A:ASP447 4.8 39.9 1.0
NZ A:LYS340 4.9 29.7 1.0
O A:HOH749 5.0 38.2 1.0
PA A:ADP591 5.0 40.4 1.0

Reference:

T.Zhou, S.Radaev, B.P.Rosen, D.L.Gatti. Structure of the Arsa Atpase: the Catalytic Subunit of A Heavy Metal Resistance Pump. Embo J. V. 19 4838 2000.
ISSN: ISSN 0261-4189
PubMed: 10970874
DOI: 10.1093/EMBOJ/19.17.4838
Page generated: Mon Dec 14 05:53:06 2020

Last articles

Zn in 7VD8
Zn in 7V1R
Zn in 7V1Q
Zn in 7VPF
Zn in 7T85
Zn in 7T5F
Zn in 7NF9
Zn in 7M4M
Zn in 7M4O
Zn in 7M4N
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy