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Magnesium in PDB 3ehg: Crystal Structure of the Atp-Binding Domain of Desk in Complex with Atp

Enzymatic activity of Crystal Structure of the Atp-Binding Domain of Desk in Complex with Atp

All present enzymatic activity of Crystal Structure of the Atp-Binding Domain of Desk in Complex with Atp:
2.7.13.3;

Protein crystallography data

The structure of Crystal Structure of the Atp-Binding Domain of Desk in Complex with Atp, PDB code: 3ehg was solved by F.Trajtenberg, A.Buschiazzo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 42.03 / 1.74
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 40.379, 49.078, 81.436, 90.00, 90.00, 90.00
R / Rfree (%) 16.4 / 21.5

Other elements in 3ehg:

The structure of Crystal Structure of the Atp-Binding Domain of Desk in Complex with Atp also contains other interesting chemical elements:

Iodine (I) 12 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of the Atp-Binding Domain of Desk in Complex with Atp (pdb code 3ehg). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Crystal Structure of the Atp-Binding Domain of Desk in Complex with Atp, PDB code: 3ehg:

Magnesium binding site 1 out of 1 in 3ehg

Go back to Magnesium Binding Sites List in 3ehg
Magnesium binding site 1 out of 1 in the Crystal Structure of the Atp-Binding Domain of Desk in Complex with Atp


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 Atp-Binding Domain of Desk in Complex with Atp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg371

b:16.6
occ:1.00
 OE2 A:GLU289 2.0 17.1 1.0
O1A A:ATP1 2.0 15.7 1.0
O2B A:ATP1 2.0 15.9 1.0
O A:HOH165 2.1 28.4 1.0
O3G A:ATP1 2.1 17.1 1.0
OD1 A:ASN293 2.1 15.8 1.0
CG A:ASN293 3.1 17.5 1.0
CD A:GLU289 3.1 18.3 1.0
PB A:ATP1 3.1 17.4 1.0
PG A:ATP1 3.2 19.3 1.0
PA A:ATP1 3.2 16.6 1.0
O3A A:ATP1 3.4 16.4 1.0
ND2 A:ASN293 3.4 17.2 1.0
OE1 A:GLU289 3.5 20.3 1.0
O3B A:ATP1 3.6 18.6 1.0
O2G A:ATP1 3.6 19.7 1.0
O5' A:ATP1 4.2 16.8 1.0
CA A:GLY336 4.2 18.4 1.0
N A:GLY336 4.2 19.2 1.0
NE2 A:HIS297 4.3 17.9 1.0
CG A:GLU289 4.4 18.7 1.0
O2A A:ATP1 4.4 18.2 1.0
CB A:ASN293 4.5 16.0 1.0
CE A:LYS296 4.5 35.1 1.0
O1B A:ATP1 4.5 18.5 1.0
O1G A:ATP1 4.5 22.4 1.0
NZ A:LYS296 4.6 38.0 1.0
CA A:ASN293 4.8 15.9 1.0
O A:GLU289 4.9 17.4 1.0
CD2 A:HIS297 5.0 17.4 1.0
C A:GLY336 5.0 17.3 1.0

Reference:

F.Trajtenberg, M.Grana, N.Ruetalo, H.Botti, A.Buschiazzo. Structural and Enzymatic Insights Into the Atp Binding and Autophosphorylation Mechanism of A Sensor Histidine Kinase J.Biol.Chem. V. 285 24892 2010.
ISSN: ISSN 0021-9258
PubMed: 20507988
DOI: 10.1074/JBC.M110.147843
Page generated: Mon Dec 14 08:06:23 2020

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