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Magnesium in PDB 1ii0: Crystal Structure of the Escherichia Coli Arsenite-Translocating Atpase

Enzymatic activity of Crystal Structure of the Escherichia Coli Arsenite-Translocating Atpase

All present enzymatic activity of Crystal Structure of the Escherichia Coli Arsenite-Translocating Atpase:
3.6.3.16;

Protein crystallography data

The structure of Crystal Structure of the Escherichia Coli Arsenite-Translocating Atpase, PDB code: 1ii0 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) 28.61 / 2.40
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 76.727, 222.189, 74.126, 90.00, 90.00, 90.00
R / Rfree (%) 21 / 25.2

Other elements in 1ii0:

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

Cadmium (Cd) 17 atoms
Arsenic (As) 2 atoms
Chlorine (Cl) 7 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of the Escherichia Coli Arsenite-Translocating Atpase (pdb code 1ii0). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Crystal Structure of the Escherichia Coli Arsenite-Translocating Atpase, PDB code: 1ii0:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in 1ii0

Go back to Magnesium Binding Sites List in 1ii0
Magnesium binding site 1 out of 4 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:17.4
occ:1.00
 O3B A:ADP590 2.0 28.3 1.0
OD1 A:ASP45 2.1 31.9 1.0
O A:HOH2309 2.1 22.2 1.0
O A:HOH2260 2.1 36.2 1.0
OG1 A:THR22 2.2 24.5 1.0
O A:HOH2164 2.2 26.6 1.0
CG A:ASP45 3.1 34.0 1.0
PB A:ADP590 3.1 28.1 1.0
CB A:THR22 3.3 24.3 1.0
O1B A:ADP590 3.4 28.4 1.0
OD2 A:ASP45 3.5 33.2 1.0
O3A A:ADP590 3.6 29.3 1.0
N A:THR22 3.9 24.5 1.0
OD2 A:ASP142 4.0 25.5 1.0
O1A A:ADP590 4.0 29.3 1.0
CA A:THR22 4.2 24.2 1.0
CG2 A:THR22 4.4 23.4 1.0
CB A:ASP45 4.4 34.9 1.0
O2B A:ADP590 4.5 26.2 1.0
O A:HOH2059 4.5 32.7 1.0
PA A:ADP590 4.6 29.2 1.0
OG1 A:THR502 4.8 30.1 1.0
O A:HOH2176 4.8 38.2 1.0
O A:ASP142 4.8 24.4 1.0
CG A:ASP142 4.8 25.8 1.0
CB A:LYS21 4.8 23.6 1.0
O2A A:ADP590 4.9 29.8 1.0
CE A:LYS21 4.9 19.2 1.0
O A:HOH2014 4.9 19.0 1.0

Magnesium binding site 2 out of 4 in 1ii0

Go back to Magnesium Binding Sites List in 1ii0
Magnesium binding site 2 out of 4 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:29.2
occ:1.00
 O A:HOH2083 2.0 42.1 1.0
O1B A:ATP591 2.1 29.5 1.0
O2G A:ATP591 2.1 29.2 1.0
OG1 A:THR341 2.1 25.3 1.0
O A:HOH2323 2.1 21.6 1.0
O A:HOH2175 2.2 21.1 1.0
PB A:ATP591 3.2 29.5 1.0
O3B A:ATP591 3.2 30.7 1.0
PG A:ATP591 3.3 30.4 1.0
CB A:THR341 3.3 24.4 1.0
OD2 A:ASP447 3.7 29.6 1.0
N A:THR341 3.8 23.4 1.0
CA A:THR341 4.1 24.1 1.0
O1G A:ATP591 4.2 29.2 1.0
O2B A:ATP591 4.2 29.6 1.0
O3A A:ATP591 4.3 30.5 1.0
O3G A:ATP591 4.4 32.6 1.0
O2A A:ATP591 4.4 32.8 1.0
CG A:ASP447 4.4 28.5 1.0
CG2 A:THR341 4.4 23.1 1.0
O A:ASP447 4.5 28.4 1.0
CB A:LYS340 4.6 23.8 1.0
PA A:ATP591 4.8 31.5 1.0
C A:LYS340 4.9 23.6 1.0
CB A:ASP364 4.9 51.1 1.0
CE A:LYS340 4.9 23.6 1.0
CB A:ASP447 4.9 28.7 1.0
O1A A:ATP591 5.0 31.6 1.0
OG A:SER363 5.0 44.5 1.0

Magnesium binding site 3 out of 4 in 1ii0

Go back to Magnesium Binding Sites List in 1ii0
Magnesium binding site 3 out of 4 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 3 of Crystal Structure of the Escherichia Coli Arsenite-Translocating Atpase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg1592

b:16.5
occ:1.00
 OD1 B:ASP1045 1.8 45.1 1.0
OG1 B:THR1022 2.0 27.9 1.0
O B:HOH2012 2.1 16.5 1.0
O3B B:ADP1590 2.1 32.9 1.0
O B:HOH2007 2.1 14.8 1.0
O B:HOH2236 2.2 24.9 1.0
CG B:ASP1045 2.7 45.3 1.0
OD2 B:ASP1045 3.0 44.6 1.0
CB B:THR1022 3.2 27.9 1.0
PB B:ADP1590 3.3 33.4 1.0
O1B B:ADP1590 3.5 34.5 1.0
OD2 B:ASP1142 4.0 27.5 1.0
N B:THR1022 4.0 28.1 1.0
O3A B:ADP1590 4.1 34.4 1.0
O B:HOH3004 4.1 31.4 1.0
O1A B:ADP1590 4.1 35.4 1.0
CB B:ASP1045 4.1 44.9 1.0
CA B:THR1022 4.2 27.8 1.0
CG2 B:THR1022 4.2 27.5 1.0
O B:HOH2002 4.6 21.2 1.0
O2B B:ADP1590 4.6 32.9 1.0
O B:HOH2197 4.6 32.2 1.0
CG B:ASP1142 4.7 27.0 1.0
PA B:ADP1590 4.8 34.6 1.0
O B:ASP1142 4.8 27.5 1.0
OG1 B:THR1502 4.9 28.2 1.0
CB B:ASP1142 5.0 26.4 1.0
CE B:LYS1021 5.0 26.6 1.0

Magnesium binding site 4 out of 4 in 1ii0

Go back to Magnesium Binding Sites List in 1ii0
Magnesium binding site 4 out of 4 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 4 of Crystal Structure of the Escherichia Coli Arsenite-Translocating Atpase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg1593

b:23.1
occ:1.00
 O B:HOH2102 1.8 27.7 1.0
O B:HOH2073 1.9 30.5 1.0
O2G B:ATP1591 2.1 28.1 1.0
OG1 B:THR1341 2.1 24.3 1.0
O B:HOH2209 2.3 25.4 1.0
O1B B:ATP1591 2.3 27.9 1.0
O3B B:ATP1591 3.2 28.6 1.0
PG B:ATP1591 3.3 28.1 1.0
CB B:THR1341 3.3 25.1 1.0
PB B:ATP1591 3.4 27.2 1.0
OD2 B:ASP1447 4.0 26.6 1.0
O2A B:ATP1591 4.0 31.0 1.0
O3G B:ATP1591 4.1 28.9 1.0
N B:THR1341 4.2 24.6 1.0
O B:HOH3008 4.2 37.8 1.0
CG2 B:THR1341 4.2 24.9 1.0
CA B:THR1341 4.3 24.8 1.0
OD2 B:ASP1364 4.4 54.9 1.0
O1G B:ATP1591 4.4 27.9 1.0
O3A B:ATP1591 4.4 29.4 1.0
O2B B:ATP1591 4.5 28.6 1.0
CB B:ASP1364 4.7 53.7 1.0
CG B:ASP1447 4.7 27.1 1.0
PA B:ATP1591 4.7 30.8 1.0
O B:ASP1447 4.7 27.7 1.0
CG B:ASP1364 5.0 54.9 1.0

Reference:

T.Zhou, S.Radaev, B.P.Rosen, D.L.Gatti. Conformational Changes in Four Regions of the Escherichia Coli Arsa Atpase Link Atp Hydrolysis to Ion Translocation. J.Biol.Chem. V. 276 30414 2001.
ISSN: ISSN 0021-9258
PubMed: 11395509
DOI: 10.1074/JBC.M103671200
Page generated: Tue Aug 13 04:59:31 2024

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