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Magnesium in PDB 6ayu: Crystal Structure of Fructose-1,6-Bisphosphatase T84S From Mycobacterium Tuberculosis

Enzymatic activity of Crystal Structure of Fructose-1,6-Bisphosphatase T84S From Mycobacterium Tuberculosis

All present enzymatic activity of Crystal Structure of Fructose-1,6-Bisphosphatase T84S From Mycobacterium Tuberculosis:
3.1.3.11;

Protein crystallography data

The structure of Crystal Structure of Fructose-1,6-Bisphosphatase T84S From Mycobacterium Tuberculosis, PDB code: 6ayu was solved by C.Abad-Zapatero, N.Wolf, H.J.Gutka, F.Movahedzadeh, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 38.50 / 2.20
Space group P 61 2 2
Cell size a, b, c (Å), α, β, γ (°) 130.890, 130.890, 142.848, 90.00, 90.00, 120.00
R / Rfree (%) 20.4 / 25.2

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Fructose-1,6-Bisphosphatase T84S From Mycobacterium Tuberculosis (pdb code 6ayu). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the Crystal Structure of Fructose-1,6-Bisphosphatase T84S From Mycobacterium Tuberculosis, PDB code: 6ayu:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in 6ayu

Go back to Magnesium Binding Sites List in 6ayu
Magnesium binding site 1 out of 3 in the Crystal Structure of Fructose-1,6-Bisphosphatase T84S From Mycobacterium Tuberculosis


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 Fructose-1,6-Bisphosphatase T84S From Mycobacterium Tuberculosis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg402

b:57.0
occ:1.00
OD2 A:ASP79 2.4 60.1 1.0
OE2 A:GLU208 2.7 49.1 1.0
OD1 A:ASP82 2.8 42.9 1.0
O2 A:GOL407 3.0 80.1 1.0
CG A:ASP79 3.2 51.4 1.0
OD1 A:ASP79 3.3 51.7 1.0
O1 A:F6P401 3.3 67.0 1.0
CG A:GLU208 3.4 39.3 1.0
CA A:ASP82 3.4 48.2 1.0
CD A:GLU208 3.5 47.8 1.0
N A:GLY83 3.7 57.0 1.0
CG A:ASP82 3.7 48.7 1.0
C1 A:F6P401 3.7 59.6 1.0
C A:ASP82 3.9 52.6 1.0
O A:ILE81 3.9 46.8 1.0
CB A:ASP82 3.9 46.1 1.0
C3 A:F6P401 4.0 49.2 1.0
C2 A:GOL407 4.1 84.1 1.0
O3 A:F6P401 4.2 45.3 1.0
O A:HOH530 4.3 67.3 1.0
O A:HOH554 4.4 61.2 1.0
O A:HOH567 4.4 64.0 1.0
N A:ASP82 4.4 43.0 1.0
C2 A:F6P401 4.5 61.3 1.0
O1 A:GOL407 4.5 71.5 1.0
C A:ILE81 4.6 45.9 1.0
CB A:ASP79 4.6 44.8 1.0
OE1 A:GLU208 4.7 46.6 1.0
C1 A:GOL407 4.8 82.8 1.0
CA A:GLY83 4.9 58.1 1.0
O A:ASP82 4.9 50.3 1.0
OD2 A:ASP82 4.9 51.2 1.0
CB A:GLU208 4.9 40.7 1.0

Magnesium binding site 2 out of 3 in 6ayu

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Magnesium binding site 2 out of 3 in the Crystal Structure of Fructose-1,6-Bisphosphatase T84S From Mycobacterium Tuberculosis


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of Fructose-1,6-Bisphosphatase T84S From Mycobacterium Tuberculosis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg406

b:57.2
occ:1.00
O A:ARG192 2.3 64.3 1.0
O A:THR197 2.4 50.0 1.0
OG A:SER195 2.8 60.9 1.0
O A:ALA190 2.8 53.6 1.0
O A:SER189 2.9 54.9 1.0
C A:ALA190 3.5 51.5 1.0
C A:ARG192 3.5 61.4 1.0
C A:THR197 3.6 54.3 1.0
O A:PRO193 3.8 91.0 1.0
CB A:SER195 3.9 60.1 1.0
CA A:ALA190 4.0 48.9 1.0
N A:SER195 4.0 65.0 1.0
C A:SER189 4.0 54.9 1.0
C A:PRO193 4.1 80.8 1.0
N A:ARG192 4.1 54.2 1.0
O A:HOH508 4.3 50.4 1.0
CA A:ARG192 4.3 59.9 1.0
N A:THR197 4.3 56.0 1.0
CA A:ASP198 4.4 49.8 1.0
OG1 A:THR197 4.4 65.3 1.0
C A:CYS191 4.4 57.6 1.0
N A:CYS191 4.4 49.5 1.0
N A:ASP198 4.4 55.7 1.0
N A:PRO193 4.5 68.2 1.0
CA A:SER195 4.5 56.5 1.0
N A:ALA190 4.5 50.4 1.0
CA A:PRO193 4.5 72.0 1.0
CA A:THR197 4.5 59.6 1.0
N A:HIS194 4.6 74.7 1.0
N A:GLY196 4.7 55.0 1.0
CB A:ARG192 4.8 56.1 1.0
CA A:CYS191 4.8 51.0 1.0
O A:CYS191 4.9 56.5 1.0
C A:SER195 4.9 58.9 1.0
OD1 A:ASP198 4.9 57.7 1.0

Magnesium binding site 3 out of 3 in 6ayu

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Magnesium binding site 3 out of 3 in the Crystal Structure of Fructose-1,6-Bisphosphatase T84S From Mycobacterium Tuberculosis


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Crystal Structure of Fructose-1,6-Bisphosphatase T84S From Mycobacterium Tuberculosis within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg403

b:63.2
occ:1.00
OD2 B:ASP79 2.3 56.6 1.0
OD1 B:ASP82 2.4 53.0 1.0
OE2 B:GLU208 2.8 56.5 1.0
CG B:ASP79 3.2 59.9 1.0
CG B:ASP82 3.3 52.6 1.0
O B:HOH510 3.4 60.5 1.0
C1 B:F6P401 3.4 59.0 1.0
CG B:GLU208 3.4 50.9 1.0
CA B:ASP82 3.4 55.7 1.0
OD1 B:ASP79 3.5 58.0 1.0
CD B:GLU208 3.5 54.6 1.0
CB B:ASP82 3.8 51.9 1.0
C3 B:F6P401 3.8 62.9 1.0
O3 B:F6P401 3.9 57.1 1.0
N B:GLY83 4.0 57.7 1.0
C B:ASP82 4.0 60.4 1.0
O1 B:F6P401 4.1 75.3 1.0
C2 B:F6P401 4.2 64.0 1.0
O B:ILE81 4.3 52.9 1.0
O B:HOH578 4.4 69.8 1.0
OD2 B:ASP82 4.4 52.3 1.0
N B:ASP82 4.5 53.0 1.0
CB B:ASP79 4.6 51.7 1.0
OE1 B:GLU208 4.8 46.5 1.0
C B:ILE81 4.8 51.7 1.0
CB B:GLU208 4.9 46.2 1.0
O B:ASP82 4.9 54.3 1.0

Reference:

N.M.Wolf, H.J.Gutka, F.Movahedzadeh, C.Abad-Zapatero. Structures of the Mycobacterium Tuberculosis Glpx Protein (Class II Fructose-1,6-Bisphosphatase): Implications For the Active Oligomeric State, Catalytic Mechanism and Citrate Inhibition. Acta Crystallogr D Struct V. 74 321 2018BIOL.
ISSN: ISSN 2059-7983
PubMed: 29652259
DOI: 10.1107/S2059798318002838
Page generated: Mon Sep 30 19:24:56 2024

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