Magnesium in PDB 6zij: Crystal Structure of Two-Domain Laccase Mutant R240H From Streptomyces Griseoflavus

All present enzymatic activity of Crystal Structure of Two-Domain Laccase Mutant R240H From Streptomyces Griseoflavus:
1.10.3.2;

The structure of Crystal Structure of Two-Domain Laccase Mutant R240H From Streptomyces Griseoflavus, PDB code: 6zij was solved by A.G.Gabdulkhakov, T.V.Tishchenko, I.A.Kolyadenko, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.83 / 1.60
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	75.04, 94.32, 116.83, 90, 90.69, 90
R / Rfree (%)	14.5 / 18.1

The structure of Crystal Structure of Two-Domain Laccase Mutant R240H From Streptomyces Griseoflavus also contains other interesting chemical elements:

Copper

(Cu)

24 atoms

The binding sites of Magnesium atom in the Crystal Structure of Two-Domain Laccase Mutant R240H From Streptomyces Griseoflavus (pdb code 6zij). 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 Two-Domain Laccase Mutant R240H From Streptomyces Griseoflavus, PDB code: 6zij:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in the Crystal Structure of Two-Domain Laccase Mutant R240H From Streptomyces Griseoflavus


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 Two-Domain Laccase Mutant R240H From Streptomyces Griseoflavus within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg409 b:49.1 occ:1.00 O B:HOH558 2.5 36.1 1.0 O A:HOH559 2.5 44.8 1.0 O C:HOH535 2.5 41.4 1.0 O B:HOH666 3.0 36.8 1.0 O A:HOH644 3.1 34.3 1.0 O C:HOH648 3.1 36.1 1.0 O B:HOH663 3.6 44.1 1.0 O C:HOH570 3.7 30.1 1.0 O C:HOH625 3.7 47.7 1.0 O B:HOH591 3.8 29.8 1.0 O A:HOH543 4.0 39.4 1.0 O A:HOH542 4.1 47.9 1.0 OD2 C:ASP243 4.4 26.4 1.0 O A:HOH528 4.5 39.5 1.0 OD2 B:ASP243 4.5 25.7 1.0 OD2 A:ASP243 4.6 24.2 1.0 NZ C:LYS262 4.7 25.4 1.0 NZ B:LYS262 4.8 23.9 1.0 NZ A:LYS262 5.0 24.9 1.0

Magnesium binding site 2 out of 3 in the Crystal Structure of Two-Domain Laccase Mutant R240H From Streptomyces Griseoflavus


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 Two-Domain Laccase Mutant R240H From Streptomyces Griseoflavus within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg407 b:50.0 occ:1.00 O B:HOH628 2.3 38.8 1.0 O C:HOH560 2.4 40.9 1.0 O B:HOH607 2.5 29.9 1.0 O A:HOH625 2.5 35.4 1.0 O A:HOH533 2.6 40.3 1.0 O C:HOH643 2.6 31.8 1.0 O B:HOH663 3.5 44.1 1.0 O B:HOH633 3.6 29.8 1.0 O C:HOH605 3.6 33.6 1.0 O A:HOH608 3.9 25.6 1.0 O A:ASP243 4.4 25.7 1.0 O C:ASP243 4.4 24.8 1.0 O B:ASP243 4.4 21.5 1.0 OG B:SER256 4.6 23.7 1.0 O C:HOH625 4.7 47.7 1.0 OG A:SER256 4.9 24.9 1.0 OG C:SER256 4.9 28.8 1.0 CB C:SER256 5.0 25.5 1.0 CA C:SER256 5.0 24.9 1.0

Magnesium binding site 3 out of 3 in the Crystal Structure of Two-Domain Laccase Mutant R240H From Streptomyces Griseoflavus


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 Two-Domain Laccase Mutant R240H From Streptomyces Griseoflavus within 5.0Å range: probe atom residue distance (Å) B Occ D:Mg406 b:47.4 occ:1.00 O F:HOH582 2.4 30.8 1.0 O D:HOH523 2.4 40.7 1.0 O E:HOH530 2.5 38.6 1.0 O E:HOH559 2.6 34.2 1.0 O D:HOH619 2.6 34.4 1.0 O F:HOH625 2.6 28.9 1.0 O F:HOH653 3.5 42.2 1.0 O D:HOH563 3.7 32.9 1.0 O F:HOH611 3.8 31.1 1.0 O E:HOH616 3.8 26.0 1.0 O F:ASP243 4.4 23.1 1.0 O E:ASP243 4.4 25.2 1.0 O D:ASP243 4.4 22.5 1.0 OG E:SER256 4.7 23.5 1.0 OG F:SER256 4.7 27.2 1.0 OG D:SER256 4.8 22.7 1.0

A.Gabdulkhakov, I.Kolyadenko, P.Oliveira, P.Tamagnini, A.Mikhaylina, S.Tishchenko. The Role of Positive Charged Residue in the Proton-Transfer Mechanism of Two-Domain Laccase From Streptomyces Griseoflavus Ac-993. J.Biomol.Struct.Dyn. 1 2021.
ISSN: ESSN 1538-0254
PubMed: 33870857
DOI: 10.1080/07391102.2021.1911852