Magnesium in PDB 3cbg: Functional and Structural Characterization of A Cationdependent O- Methyltransferase From the Cyanobacterium Synechocystis Sp. Strain Pcc 6803

The structure of Functional and Structural Characterization of A Cationdependent O- Methyltransferase From the Cyanobacterium Synechocystis Sp. Strain Pcc 6803, PDB code: 3cbg was solved by J.G.Kopycki, P.Neumann, M.T.Stubbs, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.81 / 2.00
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	57.622, 57.622, 119.834, 90.00, 90.00, 120.00
R / Rfree (%)	15.2 / 21.6

The binding sites of Magnesium atom in the Functional and Structural Characterization of A Cationdependent O- Methyltransferase From the Cyanobacterium Synechocystis Sp. Strain Pcc 6803 (pdb code 3cbg). 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 Functional and Structural Characterization of A Cationdependent O- Methyltransferase From the Cyanobacterium Synechocystis Sp. Strain Pcc 6803, PDB code: 3cbg:

Magnesium binding site 1 out of 1 in the Functional and Structural Characterization of A Cationdependent O- Methyltransferase From the Cyanobacterium Synechocystis Sp. Strain Pcc 6803


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Functional and Structural Characterization of A Cationdependent O- Methyltransferase From the Cyanobacterium Synechocystis Sp. Strain Pcc 6803 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg401 b:25.4 occ:1.00 O3 A:4FE502 2.2 31.3 0.5 OD1 A:ASN170 2.2 24.7 1.0 O4 A:4FE502 2.3 29.9 0.5 OD1 A:ASP143 2.4 19.0 1.0 OD2 A:ASP169 2.4 20.6 1.0 O A:HOH1128 2.4 19.9 1.0 O4 A:FER501 2.4 56.3 0.5 C8 A:4FE502 2.9 28.4 0.5 C5 A:FER501 3.0 58.0 0.5 C1 A:4FE502 3.0 32.7 0.5 C5 A:4FE502 3.1 31.3 0.5 CG A:ASN170 3.1 21.9 1.0 C4 A:FER501 3.1 56.9 0.5 ND2 A:ASN170 3.3 20.2 1.0 CG A:ASP143 3.3 17.2 1.0 OD2 A:ASP143 3.5 16.5 1.0 CG A:ASP169 3.5 21.4 1.0 O A:MET42 3.7 23.7 1.0 NZ A:LYS146 3.9 12.4 1.0 CB A:ASP169 4.0 21.6 1.0 NZ A:LYS3 4.1 35.8 1.0 O A:HOH1129 4.1 18.4 1.0 C6 A:FER501 4.3 58.4 0.5 C3 A:4FE502 4.4 33.1 0.5 C6 A:4FE502 4.4 31.9 0.5 C3 A:FER501 4.4 56.5 0.5 CB A:ASN170 4.5 19.7 1.0 OD1 A:ASP169 4.5 23.8 1.0 CB A:ASP143 4.7 17.8 1.0 N A:ASN170 4.8 21.4 1.0 C A:ASP169 4.8 22.0 1.0 C A:MET42 4.8 23.6 1.0 CE A:LYS146 4.9 13.9 1.0 CG2 A:ILE44 4.9 17.7 1.0 O A:ASP143 5.0 19.8 1.0

J.G.Kopycki, M.T.Stubbs, W.Brandt, M.Hagemann, A.Porzel, J.Schmidt, W.Schliemann, M.H.Zenk, T.Vogt. Functional and Structural Characterization of A Cation-Dependent O-Methyltransferase From the Cyanobacterium Synechocystis Sp. Strain Pcc 6803 J.Biol.Chem. V. 283 20888 2008.
ISSN: ISSN 0021-9258
PubMed: 18502765
DOI: 10.1074/JBC.M801943200