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Magnesium in PDB 3n0s: Crystal Structure of BA2930 Mutant (H183A) in Complex with Accoa

Enzymatic activity of Crystal Structure of BA2930 Mutant (H183A) in Complex with Accoa

All present enzymatic activity of Crystal Structure of BA2930 Mutant (H183A) in Complex with Accoa:
2.3.1.81;

Protein crystallography data

The structure of Crystal Structure of BA2930 Mutant (H183A) in Complex with Accoa, PDB code: 3n0s was solved by M.M.Klimecka, M.Chruszcz, P.J.Porebski, M.Cymborowski, W.F.Anderson, W.Minor, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 2.15
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 72.036, 109.441, 74.048, 90.00, 111.86, 90.00
R / Rfree (%) 17.3 / 22.8

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of BA2930 Mutant (H183A) in Complex with Accoa (pdb code 3n0s). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of BA2930 Mutant (H183A) in Complex with Accoa, PDB code: 3n0s:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 3n0s

Go back to Magnesium Binding Sites List in 3n0s
Magnesium binding site 1 out of 2 in the Crystal Structure of BA2930 Mutant (H183A) in Complex with Accoa


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 BA2930 Mutant (H183A) in Complex with Accoa within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg267

b:45.3
occ:1.00
O D:HOH496 2.1 44.5 1.0
O D:HOH497 2.1 44.3 1.0
O D:HOH405 2.1 43.0 1.0
O D:HOH475 2.1 49.0 1.0
O D:HOH397 2.1 42.5 1.0
O D:HOH398 2.1 39.5 1.0
CA D:THR119 4.1 12.2 1.0
O D:THR119 4.1 13.5 1.0
O D:ARG118 4.2 11.7 1.0
ND1 D:HIS103 4.2 21.5 1.0
C D:THR119 4.4 12.9 1.0
O D:HOH307 4.5 32.6 1.0
O D:HIS103 4.7 16.6 1.0
O D:HOH312 4.8 28.9 1.0
O D:TYR120 4.8 14.2 1.0
CB D:THR119 4.8 14.1 1.0
O B:HOH442 4.9 49.3 1.0
CA D:HIS103 5.0 15.8 1.0

Magnesium binding site 2 out of 2 in 3n0s

Go back to Magnesium Binding Sites List in 3n0s
Magnesium binding site 2 out of 2 in the Crystal Structure of BA2930 Mutant (H183A) in Complex with Accoa


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 BA2930 Mutant (H183A) in Complex with Accoa within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg267

b:37.6
occ:1.00
O B:HOH393 2.0 35.1 1.0
O B:HOH495 2.1 39.7 1.0
O B:HOH494 2.1 40.1 1.0
O B:HOH412 2.1 31.2 1.0
O B:HOH411 2.1 36.1 1.0
O B:HOH408 2.1 34.1 1.0
O B:THR119 3.9 15.8 1.0
O B:ARG118 4.3 13.7 1.0
C B:THR119 4.4 15.3 1.0
CA B:THR119 4.4 15.4 1.0
O B:TYR120 4.4 14.4 1.0
O B:HOH410 4.6 35.5 1.0
ND1 B:HIS103 4.7 18.9 1.0

Reference:

M.M.Klimecka, M.Chruszcz, J.Font, T.Skarina, I.Shumilin, O.Onopryienko, P.J.Porebski, M.Cymborowski, M.D.Zimmerman, J.Hasseman, I.J.Glomski, L.Lebioda, A.Savchenko, A.Edwards, W.Minor. Structural Analysis of A Putative Aminoglycoside N-Acetyltransferase From Bacillus Anthracis. J.Mol.Biol. V. 410 411 2011.
ISSN: ISSN 0022-2836
PubMed: 21601576
DOI: 10.1016/J.JMB.2011.04.076
Page generated: Mon Dec 14 08:27:25 2020

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