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Magnesium in PDB 5a8n: Crystal Structure of the Native Form of Beta-Glucanase SDGLUC5_26A From Saccharophagus Degradans

Enzymatic activity of Crystal Structure of the Native Form of Beta-Glucanase SDGLUC5_26A From Saccharophagus Degradans

All present enzymatic activity of Crystal Structure of the Native Form of Beta-Glucanase SDGLUC5_26A From Saccharophagus Degradans:
3.2.1.73;

Protein crystallography data

The structure of Crystal Structure of the Native Form of Beta-Glucanase SDGLUC5_26A From Saccharophagus Degradans, PDB code: 5a8n was solved by G.Sulzenbacher, M.Lafond, T.Freyd, B.Henrissat, R.M.Coutinho, J.G.Berrin, M.L.Garron, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 32.91 / 2.05
Space group P 41 3 2
Cell size a, b, c (Å), α, β, γ (°) 143.341, 143.341, 143.341, 90.00, 90.00, 90.00
R / Rfree (%) 15.1 / 18

Other elements in 5a8n:

The structure of Crystal Structure of the Native Form of Beta-Glucanase SDGLUC5_26A From Saccharophagus Degradans also contains other interesting chemical elements:

Chlorine (Cl) 2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of the Native Form of Beta-Glucanase SDGLUC5_26A From Saccharophagus Degradans (pdb code 5a8n). 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 the Native Form of Beta-Glucanase SDGLUC5_26A From Saccharophagus Degradans, PDB code: 5a8n:

Magnesium binding site 1 out of 1 in 5a8n

Go back to Magnesium Binding Sites List in 5a8n
Magnesium binding site 1 out of 1 in the Crystal Structure of the Native Form of Beta-Glucanase SDGLUC5_26A From Saccharophagus Degradans


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 the Native Form of Beta-Glucanase SDGLUC5_26A From Saccharophagus Degradans within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1367

b:37.3
occ:1.00
 O A:HOH2178 2.2 33.1 1.0
O A:VAL181 2.3 26.3 1.0
O A:HOH2173 2.3 29.7 1.0
O A:VAL178 2.3 25.2 1.0
O A:HOH2175 2.5 32.2 1.0
C A:VAL178 3.4 25.8 1.0
C A:VAL181 3.5 26.1 1.0
N A:VAL178 4.1 26.3 1.0
CB A:VAL181 4.1 27.9 1.0
CA A:VAL181 4.2 26.7 1.0
CG2 A:VAL223 4.2 40.8 1.0
CA A:VAL178 4.2 25.1 1.0
O A:TYR175 4.3 26.4 1.0
N A:PRO179 4.3 25.7 1.0
N A:VAL181 4.3 25.5 1.0
CA A:PRO179 4.3 26.7 1.0
C A:PRO179 4.5 25.3 1.0
N A:ALA182 4.5 25.6 1.0
CB A:VAL223 4.5 35.3 1.0
O A:PRO179 4.5 25.1 1.0
OD2 A:ASP220 4.6 30.5 1.0
CB A:VAL178 4.6 25.5 1.0
O A:HOH2047 4.6 32.8 1.0
OG1 A:THR222 4.6 36.6 1.0
CA A:ALA182 4.6 25.0 1.0
CE2 A:PHE50 4.7 29.4 1.0
O A:HOH2045 4.7 26.5 1.0
CG1 A:VAL181 4.8 29.9 1.0
CA A:VAL223 4.8 32.5 1.0
CD2 A:PHE50 4.9 29.3 1.0
OH A:TYR184 4.9 27.2 1.0
O A:THR222 5.0 39.6 1.0

Reference:

M.Lafond, G.Sulzenbacher, T.Freyd, B.Henrissat, J.G.Berrin, M.L.Garron. The Quaternary Structure of A Glycoside Hydrolase Dictates Specificity Towards Beta-Glucans J.Biol.Chem. V. 291 7183 2016.
ISSN: ISSN 0021-9258
PubMed: 26755730
DOI: 10.1074/JBC.M115.695999
Page generated: Mon Dec 14 19:59:45 2020

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