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Magnesium in PDB 4crq: Crystal Structure of the Catalytic Domain of the Modular Laminarinase Zglamc Mutant E142S

Enzymatic activity of Crystal Structure of the Catalytic Domain of the Modular Laminarinase Zglamc Mutant E142S

All present enzymatic activity of Crystal Structure of the Catalytic Domain of the Modular Laminarinase Zglamc Mutant E142S:
3.2.1.39;

Protein crystallography data

The structure of Crystal Structure of the Catalytic Domain of the Modular Laminarinase Zglamc Mutant E142S, PDB code: 4crq was solved by A.Labourel, M.Jam, L.Legentil, B.Sylla, E.Ficko-Blean, J.H.Hehemann, V.Ferrieres, M.Czjzek, G.Michel, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.98 / 1.50
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 67.108, 68.061, 143.282, 90.00, 90.00, 90.00
R / Rfree (%) 14.802 / 18.576

Other elements in 4crq:

The structure of Crystal Structure of the Catalytic Domain of the Modular Laminarinase Zglamc Mutant E142S also contains other interesting chemical elements:

Chlorine (Cl) 3 atoms
Calcium (Ca) 2 atoms
Sodium (Na) 2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of the Catalytic Domain of the Modular Laminarinase Zglamc Mutant E142S (pdb code 4crq). 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 Catalytic Domain of the Modular Laminarinase Zglamc Mutant E142S, PDB code: 4crq:

Magnesium binding site 1 out of 1 in 4crq

Go back to Magnesium Binding Sites List in 4crq
Magnesium binding site 1 out of 1 in the Crystal Structure of the Catalytic Domain of the Modular Laminarinase Zglamc Mutant E142S


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 Catalytic Domain of the Modular Laminarinase Zglamc Mutant E142S within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1258

b:19.1
occ:1.00
 N A:TYR178 3.3 20.7 1.0
O A:HOH2194 3.3 40.8 1.0
N B:TYR178 3.3 18.9 1.0
O A:HOH2193 3.4 44.7 1.0
CD2 B:TYR178 3.8 19.2 1.0
CB A:GLN177 3.8 20.5 1.0
CB B:GLN177 3.8 19.1 1.0
CD2 A:TYR178 3.8 19.5 1.0
CA A:GLN177 3.9 17.2 1.0
CA B:GLN177 4.0 18.0 1.0
CB B:TYR178 4.1 19.3 1.0
C A:GLN177 4.1 19.8 1.0
C B:GLN177 4.1 18.4 1.0
CB A:TYR178 4.2 17.6 1.0
CG A:GLN177 4.2 22.7 1.0
CA B:TYR178 4.3 18.4 1.0
CA A:TYR178 4.3 18.5 1.0
CG B:GLN177 4.3 19.9 1.0
CG B:TYR178 4.4 18.1 1.0
CG A:TYR178 4.5 18.5 1.0
O A:TYR178 4.7 19.6 1.0
O B:TYR178 4.7 19.3 1.0
CE2 B:TYR178 4.8 20.9 1.0
CE2 A:TYR178 4.8 20.3 1.0
NH2 B:ARG107 4.9 19.9 1.0
NH2 A:ARG107 4.9 20.1 1.0

Reference:

A.Labourel, M.Jam, L.Legentil, B.Sylla, J.H.Hehemann, V.Ferrieres, M.Czjzek, G.Michel. Structural and Biochemical Characterization of the Laminarina Zglamc[GH16] From Zobellia Galactanivorans Suggests Preferred Recognition of Branched Laminarin Acta Crystallogr.,Sect.D V. 71 173 2015.
ISSN: ISSN 0907-4449
DOI: 10.1107/S139900471402450X
Page generated: Thu Aug 15 16:52:17 2024

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