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Aluminium in PDB 1ihu: Crystal Structure of the Escherichia Coli Arsenite-Translocating Atpase in Complex with Mg-Adp-ALF3

Enzymatic activity of Crystal Structure of the Escherichia Coli Arsenite-Translocating Atpase in Complex with Mg-Adp-ALF3

All present enzymatic activity of Crystal Structure of the Escherichia Coli Arsenite-Translocating Atpase in Complex with Mg-Adp-ALF3:
3.6.3.16;

Protein crystallography data

The structure of Crystal Structure of the Escherichia Coli Arsenite-Translocating Atpase in Complex with Mg-Adp-ALF3, PDB code: 1ihu 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) 25.15 / 2.15
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 73.897, 75.945, 222.607, 90.00, 90.00, 90.00
R / Rfree (%) 21.5 / 26.2

Other elements in 1ihu:

The structure of Crystal Structure of the Escherichia Coli Arsenite-Translocating Atpase in Complex with Mg-Adp-ALF3 also contains other interesting chemical elements:

Fluorine (F) 3 atoms
Magnesium (Mg) 2 atoms
Cadmium (Cd) 8 atoms
Arsenic (As) 1 atom
Chlorine (Cl) 3 atoms

Aluminium Binding Sites:

The binding sites of Aluminium atom in the Crystal Structure of the Escherichia Coli Arsenite-Translocating Atpase in Complex with Mg-Adp-ALF3 (pdb code 1ihu). This binding sites where shown within 5.0 Angstroms radius around Aluminium atom.
In total only one binding site of Aluminium was determined in the Crystal Structure of the Escherichia Coli Arsenite-Translocating Atpase in Complex with Mg-Adp-ALF3, PDB code: 1ihu:

Aluminium binding site 1 out of 1 in 1ihu

Go back to Aluminium Binding Sites List in 1ihu
Aluminium binding site 1 out of 1 in the Crystal Structure of the Escherichia Coli Arsenite-Translocating Atpase in Complex with Mg-Adp-ALF3


Mono view


Stereo pair view

A full contact list of Aluminium with other atoms in the Al binding site number 1 of Crystal Structure of the Escherichia Coli Arsenite-Translocating Atpase in Complex with Mg-Adp-ALF3 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Al700

b:57.4
occ:1.00
 AL A:AF3700 0.0 57.4 1.0
F3 A:AF3700 1.6 64.4 1.0
F2 A:AF3700 1.7 49.4 1.0
F1 A:AF3700 1.7 60.0 1.0
O1B A:ADP591 2.3 42.0 1.0
O A:HOH893 2.4 60.6 1.0
PB A:ADP591 3.3 34.9 1.0
MG A:MG593 3.4 28.9 1.0
O3B A:ADP591 3.5 30.8 1.0
NZ A:LYS340 3.8 26.4 1.0
O A:HOH888 3.8 47.5 1.0
N A:GLY337 3.9 30.6 1.0
O A:HOH879 4.1 33.1 1.0
O2B A:ADP591 4.1 37.9 1.0
O A:HOH878 4.2 31.6 1.0
CA A:GLY336 4.3 30.9 1.0
O A:HOH880 4.5 31.3 1.0
C A:GLY336 4.6 29.6 1.0
O3A A:ADP591 4.7 34.1 1.0
CE A:LYS340 4.7 25.0 1.0
O A:HOH818 4.8 39.0 1.0
CA A:GLY337 4.9 27.3 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: Sun Jul 6 21:35:04 2025

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