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Magnesium in PDB 2ogx: The Crystal Structure of the Molybdenum Storage Protein From Azotobacter Vinelandii Loaded with Polyoxotungstates (Wsto)

Protein crystallography data

The structure of The Crystal Structure of the Molybdenum Storage Protein From Azotobacter Vinelandii Loaded with Polyoxotungstates (Wsto), PDB code: 2ogx was solved by J.Schemberg, E.Warkentin, U.Ermler, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 1.60
Space group P 63 2 2
Cell size a, b, c (Å), α, β, γ (°) 114.400, 114.400, 233.700, 90.00, 90.00, 120.00
R / Rfree (%) 17.3 / 19.6

Other elements in 2ogx:

The structure of The Crystal Structure of the Molybdenum Storage Protein From Azotobacter Vinelandii Loaded with Polyoxotungstates (Wsto) also contains other interesting chemical elements:

Tungsten (W) 24 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the The Crystal Structure of the Molybdenum Storage Protein From Azotobacter Vinelandii Loaded with Polyoxotungstates (Wsto) (pdb code 2ogx). 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 The Crystal Structure of the Molybdenum Storage Protein From Azotobacter Vinelandii Loaded with Polyoxotungstates (Wsto), PDB code: 2ogx:

Magnesium binding site 1 out of 1 in 2ogx

Go back to Magnesium Binding Sites List in 2ogx
Magnesium binding site 1 out of 1 in the The Crystal Structure of the Molybdenum Storage Protein From Azotobacter Vinelandii Loaded with Polyoxotungstates (Wsto)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of The Crystal Structure of the Molybdenum Storage Protein From Azotobacter Vinelandii Loaded with Polyoxotungstates (Wsto) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg291

b:29.8
occ:1.00
O2B A:ATP281 2.0 21.4 1.0
O A:HOH3438 2.0 22.3 1.0
O2A A:ATP281 2.1 25.1 1.0
OE2 A:GLU190 2.1 14.1 0.4
O A:PRO227 2.1 20.6 1.0
OE2 A:GLU190 2.5 31.7 0.6
CD A:GLU190 2.9 21.3 0.4
CD A:GLU190 3.2 24.8 0.6
OE1 A:GLU190 3.3 30.2 0.4
C A:PRO227 3.3 19.0 1.0
PB A:ATP281 3.3 22.0 1.0
PA A:ATP281 3.3 24.1 1.0
O3A A:ATP281 3.6 23.6 1.0
OE1 A:GLU190 3.7 18.3 0.6
OD2 A:ASP171 3.9 24.7 1.0
O B:HOH3090 3.9 26.8 1.0
NZ A:LYS45 4.0 17.6 1.0
CG A:GLU190 4.0 24.6 1.0
CA A:PRO227 4.1 19.9 1.0
C5' A:ATP281 4.1 28.9 1.0
OD1 A:ASP171 4.2 20.9 1.0
O3G A:ATP281 4.2 21.1 1.0
N A:VAL228 4.3 18.9 1.0
O1A A:ATP281 4.3 32.2 1.0
O3B A:ATP281 4.3 20.0 1.0
O5' A:ATP281 4.3 32.8 1.0
O1B A:ATP281 4.3 20.3 1.0
CA A:VAL228 4.4 19.2 1.0
O A:HOH3054 4.4 31.6 1.0
CB A:PRO227 4.4 20.3 1.0
CG A:ASP171 4.4 20.6 1.0
PG A:ATP281 4.8 19.2 1.0
O1G A:ATP281 4.9 18.6 1.0
O A:HOH3031 4.9 23.0 1.0
CG1 A:VAL228 5.0 21.1 1.0

Reference:

J.Schemberg, K.Schneider, U.Demmer, E.Warkentin, A.Muller, U.Ermler. Towards Biological Supramolecular Chemistry: A Variety of Pocket-Templated, Individual Metal Oxide Cluster Nucleations in the Cavity of A Mo/W-Storage Protein. Angew.Chem.Int.Ed.Engl. V. 46 2408 2007.
ISSN: ISSN 1433-7851
PubMed: 17304608
DOI: 10.1002/ANIE.200604858
Page generated: Mon Dec 14 07:32:18 2020

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