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Magnesium in PDB 1ii9: Crystal Structure of the Escherichia Coli Arsenite-Translocating Atpase in Complex with Amp-Pnp

Enzymatic activity of Crystal Structure of the Escherichia Coli Arsenite-Translocating Atpase in Complex with Amp-Pnp

All present enzymatic activity of Crystal Structure of the Escherichia Coli Arsenite-Translocating Atpase in Complex with Amp-Pnp:
3.6.3.16;

Protein crystallography data

The structure of Crystal Structure of the Escherichia Coli Arsenite-Translocating Atpase in Complex with Amp-Pnp, PDB code: 1ii9 was solved by T.Zhou, S.Radaev, D.L.Gatti, B.P.Rosen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 36.52 / 2.60
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 76.623, 222.527, 74.047, 90.00, 90.00, 90.00
R / Rfree (%) 19.1 / 26.5

Other elements in 1ii9:

The structure of Crystal Structure of the Escherichia Coli Arsenite-Translocating Atpase in Complex with Amp-Pnp also contains other interesting chemical elements:

Cadmium (Cd) 18 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 in Complex with Amp-Pnp (pdb code 1ii9). 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 in Complex with Amp-Pnp, PDB code: 1ii9:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in 1ii9

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Magnesium binding site 1 out of 4 in the Crystal Structure of the Escherichia Coli Arsenite-Translocating Atpase in Complex with Amp-Pnp


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 in Complex with Amp-Pnp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg592

b:17.3
occ:1.00
 O3B A:ADP590 2.0 45.7 1.0
OD1 A:ASP45 2.1 35.7 1.0
O A:HOH3001 2.1 35.7 1.0
OG1 A:THR22 2.2 26.8 1.0
O A:HOH3000 2.3 21.7 1.0
O A:HOH2063 2.8 45.6 1.0
PB A:ADP590 2.9 39.4 1.0
CG A:ASP45 3.0 43.5 1.0
O1B A:ADP590 3.1 42.9 1.0
OD2 A:ASP45 3.2 42.1 1.0
CB A:THR22 3.5 33.2 1.0
O3A A:ADP590 3.6 44.7 1.0
N A:THR22 4.1 29.1 1.0
O A:HOH3015 4.1 34.8 1.0
OD2 A:ASP142 4.2 33.2 1.0
O1A A:ADP590 4.3 43.8 1.0
O2B A:ADP590 4.3 37.0 1.0
CB A:ASP45 4.3 44.5 1.0
CA A:THR22 4.4 32.0 1.0
CG2 A:THR22 4.5 27.6 1.0
PA A:ADP590 4.7 37.7 1.0
O A:HOH2052 4.7 35.4 1.0
CE A:LYS21 4.8 19.5 1.0
OG1 A:THR502 4.8 48.1 1.0
NZ A:LYS21 4.9 22.4 1.0
CB A:LYS21 5.0 23.5 1.0
CG A:ASP142 5.0 35.0 1.0

Magnesium binding site 2 out of 4 in 1ii9

Go back to Magnesium Binding Sites List in 1ii9
Magnesium binding site 2 out of 4 in the Crystal Structure of the Escherichia Coli Arsenite-Translocating Atpase in Complex with Amp-Pnp


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 in Complex with Amp-Pnp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg593

b:21.9
occ:1.00
 O A:HOH2011 2.0 33.5 1.0
O A:HOH2030 2.0 26.6 1.0
O2G A:ANP591 2.0 29.8 1.0
O1B A:ANP591 2.0 32.0 1.0
O A:HOH3002 2.1 27.4 1.0
OG1 A:THR341 2.3 25.1 1.0
N3B A:ANP591 3.0 38.4 1.0
PG A:ANP591 3.1 36.9 1.0
PB A:ANP591 3.2 36.2 1.0
CB A:THR341 3.3 27.5 1.0
N A:THR341 3.9 24.3 1.0
O3G A:ANP591 3.9 34.5 1.0
O A:HOH2304 4.1 31.3 1.0
OD2 A:ASP447 4.1 37.2 1.0
CA A:THR341 4.2 29.0 1.0
O3A A:ANP591 4.2 35.6 1.0
O1G A:ANP591 4.3 27.6 1.0
O2B A:ANP591 4.3 34.0 1.0
CG2 A:THR341 4.4 22.1 1.0
CG A:ASP447 4.4 30.7 1.0
O2A A:ANP591 4.4 41.5 1.0
CB A:ASP364 4.7 57.3 1.0
OD2 A:ASP364 4.7 64.0 1.0
OG A:SER363 4.7 40.4 1.0
NZ A:LYS340 4.8 31.8 1.0
O A:ASP447 4.8 30.7 1.0
CB A:LYS340 4.8 28.3 1.0
OD1 A:ASP447 4.8 33.4 1.0
CB A:ASP447 4.9 30.1 1.0
PA A:ANP591 4.9 37.2 1.0
CE A:LYS340 4.9 28.1 1.0
C A:LYS340 5.0 24.7 1.0

Magnesium binding site 3 out of 4 in 1ii9

Go back to Magnesium Binding Sites List in 1ii9
Magnesium binding site 3 out of 4 in the Crystal Structure of the Escherichia Coli Arsenite-Translocating Atpase in Complex with Amp-Pnp


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 in Complex with Amp-Pnp within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg1592

b:25.0
occ:1.00
 OD1 B:ASP1045 1.7 53.5 1.0
O3B B:ADP1590 2.0 35.8 1.0
O B:HOH3003 2.1 23.8 1.0
OG1 B:THR1022 2.2 28.4 1.0
O B:HOH2006 2.2 25.4 1.0
O B:HOH2186 2.4 35.0 1.0
CG B:ASP1045 2.8 57.9 1.0
PB B:ADP1590 3.1 42.3 1.0
CB B:THR1022 3.2 24.0 1.0
O1B B:ADP1590 3.2 35.9 1.0
OD2 B:ASP1045 3.3 54.6 1.0
O1A B:ADP1590 3.7 47.7 1.0
N B:THR1022 4.0 28.7 1.0
O3A B:ADP1590 4.1 42.6 1.0
CB B:ASP1045 4.1 57.3 1.0
CA B:THR1022 4.2 27.9 1.0
CG2 B:THR1022 4.2 22.6 1.0
OD2 B:ASP1142 4.3 37.4 1.0
O2B B:ADP1590 4.3 37.0 1.0
PA B:ADP1590 4.5 40.6 1.0
OG1 B:THR1502 4.7 37.8 1.0
O B:HOH2022 4.9 35.0 1.0
CG B:ASP1142 4.9 39.2 1.0
O B:ASP1142 4.9 37.2 1.0

Magnesium binding site 4 out of 4 in 1ii9

Go back to Magnesium Binding Sites List in 1ii9
Magnesium binding site 4 out of 4 in the Crystal Structure of the Escherichia Coli Arsenite-Translocating Atpase in Complex with Amp-Pnp


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 in Complex with Amp-Pnp within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg1593

b:14.2
occ:1.00
 O B:HOH3010 1.8 35.2 1.0
O B:HOH3009 1.9 36.1 1.0
O1B B:ANP1591 2.2 23.2 1.0
O2G B:ANP1591 2.2 23.3 1.0
OG1 B:THR1341 2.3 30.2 1.0
O B:HOH2018 2.3 37.6 1.0
N3B B:ANP1591 2.9 35.4 1.0
PG B:ANP1591 3.1 29.3 1.0
PB B:ANP1591 3.2 30.1 1.0
CB B:THR1341 3.4 34.1 1.0
O3G B:ANP1591 3.7 39.2 1.0
O2A B:ANP1591 4.1 32.2 1.0
OD2 B:ASP1447 4.2 23.7 1.0
O3A B:ANP1591 4.2 25.1 1.0
N B:THR1341 4.3 30.3 1.0
O1G B:ANP1591 4.3 27.2 1.0
O B:HOH3011 4.3 41.1 1.0
CG2 B:THR1341 4.4 25.1 1.0
OD2 B:ASP1364 4.4 66.7 1.0
CA B:THR1341 4.5 29.5 1.0
O2B B:ANP1591 4.6 34.2 1.0
CB B:ASP1364 4.6 62.3 1.0
PA B:ANP1591 4.7 32.7 1.0
NZ B:LYS1340 4.8 34.8 1.0
O B:ASP1447 4.8 32.2 1.0
CG B:ASP1447 4.8 29.2 1.0
O1A B:ANP1591 4.9 34.1 1.0
CE B:LYS1340 4.9 38.4 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 05:00:02 2024

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