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Arsenic 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
Aluminium (Al) 1 atom
Cadmium (Cd) 8 atoms
Chlorine (Cl) 3 atoms

Arsenic Binding Sites:

The binding sites of Arsenic 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 Arsenic atom.
In total only one binding site of Arsenic was determined in the Crystal Structure of the Escherichia Coli Arsenite-Translocating Atpase in Complex with Mg-Adp-ALF3, PDB code: 1ihu:

Arsenic binding site 1 out of 1 in 1ihu

Go back to Arsenic Binding Sites List in 1ihu
Arsenic 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 Arsenic with other atoms in the As 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:As701

b:73.5
occ:0.50
AS A:TAS701 0.0 73.5 0.5
O1 A:TAS701 1.7 60.4 0.5
O2 A:TAS701 1.8 58.6 0.5
O3 A:TAS701 1.8 56.8 0.5
NH2 A:ARG543 3.3 35.0 1.0
NH2 A:ARG206 3.6 54.9 1.0
O4' A:ADP590 3.7 31.6 1.0
N3 A:ADP590 3.9 43.0 1.0
NH1 A:ARG206 3.9 55.5 1.0
C4 A:ADP590 4.0 39.5 1.0
C1' A:ADP590 4.0 36.6 1.0
N9 A:ADP590 4.0 38.0 1.0
CZ A:ARG543 4.1 36.0 1.0
O A:HOH828 4.1 40.2 1.0
CZ A:ARG206 4.2 52.9 1.0
O A:HOH746 4.4 29.9 1.0
C2 A:ADP590 4.6 37.0 1.0
NE A:ARG543 4.6 40.8 1.0
O A:HOH739 4.7 35.8 1.0
C5 A:ADP590 4.7 41.8 1.0
C8 A:ADP590 4.8 38.9 1.0
OD1 A:ASN281 4.8 43.5 1.0
NH1 A:ARG543 4.9 33.2 1.0
C4' A:ADP590 4.9 36.9 1.0
CD1 A:LEU277 4.9 33.5 1.0
CD A:GLU500 4.9 46.4 1.0
CG A:GLU500 4.9 41.4 1.0
C5' A:ADP590 5.0 41.9 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 Oct 27 16:46:42 2020

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