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Magnesium in PDB 3zwk: The 3-Dimensional Structure of Mpgp From Thermus Thermophilus HB27, in Complex with the Metavanadate

Enzymatic activity of The 3-Dimensional Structure of Mpgp From Thermus Thermophilus HB27, in Complex with the Metavanadate

All present enzymatic activity of The 3-Dimensional Structure of Mpgp From Thermus Thermophilus HB27, in Complex with the Metavanadate:
3.1.3.70;

Protein crystallography data

The structure of The 3-Dimensional Structure of Mpgp From Thermus Thermophilus HB27, in Complex with the Metavanadate, PDB code: 3zwk was solved by S.Goncalves, A.M.Esteves, H.Santos, N.Borges, P.M.Matias, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.276 / 2.10
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 39.968, 71.364, 92.974, 90.00, 95.46, 90.00
R / Rfree (%) 15.55 / 21.08

Other elements in 3zwk:

The structure of The 3-Dimensional Structure of Mpgp From Thermus Thermophilus HB27, in Complex with the Metavanadate also contains other interesting chemical elements:

Vanadium (V) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the The 3-Dimensional Structure of Mpgp From Thermus Thermophilus HB27, in Complex with the Metavanadate (pdb code 3zwk). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the The 3-Dimensional Structure of Mpgp From Thermus Thermophilus HB27, in Complex with the Metavanadate, PDB code: 3zwk:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 3zwk

Go back to Magnesium Binding Sites List in 3zwk
Magnesium binding site 1 out of 2 in the The 3-Dimensional Structure of Mpgp From Thermus Thermophilus HB27, in Complex with the Metavanadate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of The 3-Dimensional Structure of Mpgp From Thermus Thermophilus HB27, in Complex with the Metavanadate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg260

b:45.2
occ:1.00
OD2 A:ASP6 2.4 58.7 1.0
O A:ASP8 2.6 38.7 1.0
OD1 A:ASP202 2.6 47.0 1.0
O A:HOH2007 2.7 43.8 1.0
CG A:ASP6 3.2 49.4 1.0
OD1 A:ASP6 3.2 44.4 1.0
CG A:ASP202 3.6 56.7 1.0
C A:ASP8 3.7 44.5 1.0
OD2 A:ASP202 4.0 58.5 1.0
CA A:ASP8 4.4 47.9 1.0
CB A:ASP8 4.4 57.5 1.0
N A:ASP8 4.5 35.8 1.0
O A:HOH2006 4.5 24.8 1.0
CB A:ASP6 4.6 28.7 1.0
OD2 A:ASP206 4.6 36.0 1.0
N A:GLY9 4.8 44.2 1.0
CB A:ASP202 4.8 50.7 1.0
CB A:SER203 4.9 40.3 1.0
CA A:GLY9 5.0 46.9 1.0

Magnesium binding site 2 out of 2 in 3zwk

Go back to Magnesium Binding Sites List in 3zwk
Magnesium binding site 2 out of 2 in the The 3-Dimensional Structure of Mpgp From Thermus Thermophilus HB27, in Complex with the Metavanadate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of The 3-Dimensional Structure of Mpgp From Thermus Thermophilus HB27, in Complex with the Metavanadate within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg260

b:33.2
occ:1.00
OD2 B:ASP6 2.4 63.8 1.0
O B:ASP8 2.4 51.2 1.0
OD1 B:ASP202 2.5 50.9 1.0
O B:HOH2005 2.6 57.1 1.0
O B:HOH2003 2.6 37.0 1.0
O3 B:VN3261 2.6 35.1 0.6
V B:VN3261 3.1 55.0 0.6
CG B:ASP6 3.1 53.8 1.0
OD1 B:ASP6 3.3 50.6 1.0
CG B:ASP202 3.4 55.4 1.0
C B:ASP8 3.5 45.6 1.0
OD2 B:ASP202 3.5 60.0 1.0
O B:HOH2133 3.9 50.2 1.0
CB B:ASP8 4.1 57.8 1.0
O1 B:VN3261 4.1 22.4 0.6
CA B:ASP8 4.1 45.6 1.0
OG B:SER203 4.2 44.1 1.0
N B:ASP8 4.2 35.8 1.0
O B:HOH2170 4.3 54.6 0.8
O B:GLY165 4.3 46.0 1.0
OD2 B:ASP206 4.3 38.4 1.0
O2 B:VN3261 4.4 28.3 0.6
CB B:ASP6 4.4 39.7 1.0
N B:GLY9 4.6 40.1 1.0
CB B:SER203 4.7 46.7 1.0
OG1 B:THR10 4.7 53.5 1.0
CB B:ASP202 4.7 45.7 1.0
CA B:GLY9 4.8 46.5 1.0
C B:LEU7 4.9 40.0 1.0

Reference:

S.Goncalves, A.M.Esteves, H.Santos, N.Borges, P.M.Matias. The Three-Dimensional Structure of Mannosyl-3- Phosphoglycerate Phosphatase From Thermus Thermophilus HB27: A New Member of the Haloalkanoic Acid Dehalogenase Superfamily. Biochemistry V. 50 9551 2011.
ISSN: ISSN 0006-2960
PubMed: 21961705
DOI: 10.1021/BI201171H
Page generated: Mon Aug 11 05:23:06 2025

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