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Magnesium in PDB 4il8: Crystal Structure of An H329A Mutant of P. Aeruginosa Pmm/Pgm

Enzymatic activity of Crystal Structure of An H329A Mutant of P. Aeruginosa Pmm/Pgm

All present enzymatic activity of Crystal Structure of An H329A Mutant of P. Aeruginosa Pmm/Pgm:
5.4.2.2; 5.4.2.8;

Protein crystallography data

The structure of Crystal Structure of An H329A Mutant of P. Aeruginosa Pmm/Pgm, PDB code: 4il8 was solved by Y.Lee, R.Mehra-Chaudhary, C.Furdui, L.Beamer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 57.38 / 1.80
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 70.962, 72.906, 93.030, 90.00, 90.00, 90.00
R / Rfree (%) 18.6 / 21.9

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of An H329A Mutant of P. Aeruginosa Pmm/Pgm (pdb code 4il8). 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 An H329A Mutant of P. Aeruginosa Pmm/Pgm, PDB code: 4il8:

Magnesium binding site 1 out of 1 in 4il8

Go back to Magnesium Binding Sites List in 4il8
Magnesium binding site 1 out of 1 in the Crystal Structure of An H329A Mutant of P. Aeruginosa Pmm/Pgm


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 An H329A Mutant of P. Aeruginosa Pmm/Pgm within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg501

b:25.1
occ:1.00
OD2 A:ASP242 2.1 27.2 1.0
OD1 A:ASP246 2.1 28.6 1.0
OD2 A:ASP244 2.2 28.0 1.0
O3P A:SEP108 2.2 32.7 0.2
OG A:SEP108 2.6 35.5 1.0
O A:HOH628 2.9 35.1 1.0
P A:SEP108 2.9 33.8 0.2
CG A:ASP246 3.1 25.7 1.0
CG A:ASP242 3.1 26.4 1.0
CG A:ASP244 3.1 23.7 1.0
OD2 A:ASP246 3.3 30.2 1.0
OD1 A:ASP244 3.4 24.6 1.0
OD1 A:ASP242 3.5 26.4 1.0
CB A:SEP108 3.7 33.1 1.0
O2P A:SEP108 3.9 33.1 0.2
CD A:ARG247 4.1 27.5 0.5
NE A:ARG247 4.2 29.0 0.5
CA A:SEP108 4.2 33.2 1.0
O1P A:SEP108 4.2 32.8 0.2
N A:ASP246 4.4 18.9 1.0
NE A:ARG247 4.4 28.8 0.5
CB A:ASP246 4.4 21.5 1.0
CG A:ARG247 4.4 24.5 0.5
CB A:ASP242 4.4 24.2 1.0
CG A:ARG247 4.4 24.6 0.5
CB A:ASP244 4.5 20.4 1.0
N A:ASP244 4.6 21.7 1.0
C A:SEP108 4.6 33.8 1.0
CD A:ARG247 4.7 27.8 0.5
CA A:ASP246 4.7 20.7 1.0
N A:ARG247 4.8 21.6 1.0
O A:HOH779 4.8 24.7 1.0
N A:HIS109 4.8 35.0 1.0
O A:HOH922 4.9 48.0 1.0
N A:GLY245 4.9 19.0 1.0
CA A:ASP244 4.9 20.4 1.0
ND1 A:HIS109 4.9 43.7 1.0

Reference:

Y.Lee, R.Mehra-Chaudhary, C.Furdui, L.J.Beamer. Identification of An Essential Active-Site Residue in the Alpha-D-Phosphohexomutase Enzyme Superfamily. Febs J. V. 280 2622 2013.
ISSN: ISSN 1742-464X
PubMed: 23517223
DOI: 10.1111/FEBS.12249
Page generated: Fri Aug 16 16:46:53 2024

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