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Fluorine 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:

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

Fluorine Binding Sites:

The binding sites of Fluorine 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 Fluorine atom.
In total 3 binding sites of Fluorine where determined in the Crystal Structure of the Escherichia Coli Arsenite-Translocating Atpase in Complex with Mg-Adp-ALF3, PDB code: 1ihu:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in 1ihu

Go back to Fluorine Binding Sites List in 1ihu
Fluorine binding site 1 out of 3 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 Fluorine with other atoms in the F 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:F700

b:60.0
occ:1.00
 F1 A:AF3700 0.0 60.0 1.0
AL A:AF3700 1.7 57.4 1.0
NZ A:LYS340 2.7 26.4 1.0
F3 A:AF3700 2.8 64.4 1.0
F2 A:AF3700 3.0 49.4 1.0
O A:HOH888 3.2 47.5 1.0
O1B A:ADP591 3.3 42.0 1.0
CA A:GLY336 3.4 30.9 1.0
CE A:LYS340 3.5 25.0 1.0
O A:HOH893 3.6 60.6 1.0
PB A:ADP591 3.9 34.9 1.0
N A:GLY337 3.9 30.6 1.0
O2B A:ADP591 4.0 37.9 1.0
C A:GLY336 4.2 29.6 1.0
O3B A:ADP591 4.2 30.8 1.0
O A:HOH879 4.2 33.1 1.0
N A:GLY336 4.2 28.6 1.0
O A:LYS335 4.3 28.9 1.0
MG A:MG593 4.4 28.9 1.0
C A:LYS335 4.6 31.9 1.0
CD A:LYS340 4.9 22.4 1.0

Fluorine binding site 2 out of 3 in 1ihu

Go back to Fluorine Binding Sites List in 1ihu
Fluorine binding site 2 out of 3 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 Fluorine with other atoms in the F binding site number 2 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:F700

b:49.4
occ:1.00
 F2 A:AF3700 0.0 49.4 1.0
AL A:AF3700 1.7 57.4 1.0
MG A:MG593 1.9 28.9 1.0
O A:HOH893 2.5 60.6 1.0
O A:HOH878 2.7 31.6 1.0
O1B A:ADP591 2.8 42.0 1.0
O3B A:ADP591 2.8 30.8 1.0
F3 A:AF3700 2.9 64.4 1.0
O A:HOH880 2.9 31.3 1.0
F1 A:AF3700 3.0 60.0 1.0
O A:HOH879 3.1 33.1 1.0
PB A:ADP591 3.3 34.9 1.0
O A:HOH888 3.8 47.5 1.0
OG1 A:THR341 4.1 32.7 1.0
O A:HOH818 4.2 39.0 1.0
O2B A:ADP591 4.4 37.9 1.0
O1A A:ADP591 4.5 33.8 1.0
O3A A:ADP591 4.5 34.1 1.0
NZ A:LYS340 4.5 26.4 1.0
O A:HOH728 4.8 45.4 1.0

Fluorine binding site 3 out of 3 in 1ihu

Go back to Fluorine Binding Sites List in 1ihu
Fluorine binding site 3 out of 3 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 Fluorine with other atoms in the F binding site number 3 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:F700

b:64.4
occ:1.00
 F3 A:AF3700 0.0 64.4 1.0
AL A:AF3700 1.6 57.4 1.0
O1B A:ADP591 2.6 42.0 1.0
O A:HOH893 2.8 60.6 1.0
F1 A:AF3700 2.8 60.0 1.0
F2 A:AF3700 2.9 49.4 1.0
N A:GLY337 3.3 30.6 1.0
CA A:GLY336 3.9 30.9 1.0
PB A:ADP591 4.0 34.9 1.0
C A:GLY336 4.1 29.6 1.0
CA A:GLY337 4.2 27.3 1.0
O A:HOH728 4.5 45.4 1.0
O3B A:ADP591 4.6 30.8 1.0
MG A:MG593 4.7 28.9 1.0
O A:HOH878 4.8 31.6 1.0
O2B A:ADP591 4.8 37.9 1.0
NZ A:LYS340 4.9 26.4 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: Mon Jul 14 10:58:20 2025

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