Magnesium in PDB 4z3y: Active Site Complex Bambc of Benzoyl Coenzyme A Reductase in Complex with Benzoyl-Coa

The structure of Active Site Complex Bambc of Benzoyl Coenzyme A Reductase in Complex with Benzoyl-Coa, PDB code: 4z3y was solved by T.Weinert, J.W.Kung, S.Weidenweber, S.G.Huwiler, M.Boll, U.Ermler, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	79.80 / 2.36
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	125.767, 116.256, 143.973, 90.00, 110.43, 90.00
R / Rfree (%)	24.2 / 27.5

The structure of Active Site Complex Bambc of Benzoyl Coenzyme A Reductase in Complex with Benzoyl-Coa also contains other interesting chemical elements:

Tungsten	(W)	4 atoms
Iron	(Fe)	64 atoms

The binding sites of Magnesium atom in the Active Site Complex Bambc of Benzoyl Coenzyme A Reductase in Complex with Benzoyl-Coa (pdb code 4z3y). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Active Site Complex Bambc of Benzoyl Coenzyme A Reductase in Complex with Benzoyl-Coa, PDB code: 4z3y:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in the Active Site Complex Bambc of Benzoyl Coenzyme A Reductase in Complex with Benzoyl-Coa


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Active Site Complex Bambc of Benzoyl Coenzyme A Reductase in Complex with Benzoyl-Coa within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg705 b:42.9 occ:1.00 O2P A:MTE703 1.9 55.4 1.0 O3P A:MTE702 2.1 48.2 1.0 O A:SER183 2.1 55.5 1.0 O A:MET94 2.4 50.7 1.0 P A:MTE703 3.1 41.6 1.0 C4' A:MTE703 3.2 50.2 1.0 C A:SER183 3.3 48.9 1.0 P A:MTE702 3.4 47.1 1.0 O3P A:MTE703 3.5 41.7 1.0 O4' A:MTE703 3.5 50.2 1.0 C A:MET94 3.6 51.3 1.0 O1P A:MTE702 3.8 40.3 1.0 OG A:SER185 3.8 48.6 1.0 C4' A:MTE702 4.1 46.0 1.0 N A:SER185 4.1 47.0 1.0 O4' A:MTE702 4.2 56.7 1.0 N A:ALA184 4.2 46.4 1.0 CA A:ALA184 4.2 42.5 1.0 O1P A:MTE703 4.4 60.8 1.0 CA A:SER183 4.4 47.2 1.0 N A:MET95 4.4 40.3 1.0 CA A:MET95 4.4 45.3 1.0 O2P A:MTE702 4.5 39.9 1.0 CB A:SER185 4.5 41.6 1.0 CA A:MET94 4.6 41.1 1.0 N A:SER183 4.6 51.1 1.0 C3' A:MTE703 4.6 51.9 1.0 N A:MET94 4.7 41.4 1.0 C A:ALA184 4.7 45.2 1.0 CB A:SER183 4.7 42.8 1.0 O3' A:MTE703 4.8 42.5 1.0 OG A:SER93 4.9 57.5 1.0 CB A:MET94 4.9 41.5 1.0

Magnesium binding site 2 out of 4 in the Active Site Complex Bambc of Benzoyl Coenzyme A Reductase in Complex with Benzoyl-Coa


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Active Site Complex Bambc of Benzoyl Coenzyme A Reductase in Complex with Benzoyl-Coa within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg706 b:62.3 occ:1.00 O3P B:MTE702 1.9 86.0 1.0 O B:SER183 2.1 94.8 1.0 O B:MET94 2.2 95.5 1.0 O1P B:MTE703 2.3 0.6 1.0 P B:MTE702 3.1 81.4 1.0 O1P B:MTE702 3.2 83.0 1.0 C B:MET94 3.3 91.2 1.0 C B:SER183 3.3 97.0 1.0 P B:MTE703 3.4 99.1 1.0 O2P B:MTE703 3.5 97.9 1.0 C4' B:MTE703 3.5 0.8 1.0 O4' B:MTE702 3.8 35.6 1.0 C4' B:MTE702 3.9 45.3 1.0 O4' B:MTE703 3.9 0.7 1.0 OG B:SER185 4.1 0.5 1.0 N B:ALA184 4.1 96.0 1.0 CA B:ALA184 4.1 97.4 1.0 N B:MET95 4.1 86.8 1.0 CA B:MET95 4.2 86.0 1.0 N B:SER185 4.2 0.6 1.0 O2P B:MTE702 4.3 80.2 1.0 CA B:MET94 4.3 93.2 1.0 CA B:SER183 4.4 96.0 1.0 N B:MET94 4.5 0.7 1.0 N B:SER183 4.6 93.8 1.0 O3P B:MTE703 4.7 0.2 1.0 CB B:MET94 4.7 87.0 1.0 C3' B:MTE703 4.7 0.3 1.0 C B:ALA184 4.7 0.2 1.0 O3' B:MTE703 4.8 0.2 1.0 CB B:SER185 4.8 0.4 1.0 OG B:SER93 4.8 0.2 1.0 CB B:SER183 4.9 97.8 1.0

Magnesium binding site 3 out of 4 in the Active Site Complex Bambc of Benzoyl Coenzyme A Reductase in Complex with Benzoyl-Coa


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Active Site Complex Bambc of Benzoyl Coenzyme A Reductase in Complex with Benzoyl-Coa within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg704 b:47.1 occ:1.00 O3P C:MTE702 1.9 49.7 1.0 O2P C:MTE703 2.0 41.3 1.0 O C:SER183 2.0 47.3 1.0 O C:MET94 2.2 47.5 1.0 P C:MTE702 3.2 40.0 1.0 C C:SER183 3.2 49.5 1.0 P C:MTE703 3.4 53.5 1.0 C C:MET94 3.4 44.0 1.0 O2P C:MTE702 3.5 48.0 1.0 O1P C:MTE703 3.7 50.6 1.0 OG C:SER185 3.8 54.2 1.0 C4' C:MTE703 3.9 53.1 1.0 CA C:ALA184 4.0 41.9 1.0 N C:ALA184 4.0 48.7 1.0 N C:SER185 4.0 43.3 1.0 O1P C:MTE702 4.1 37.0 1.0 CA C:MET95 4.1 45.4 1.0 O4' C:MTE703 4.2 60.5 1.0 N C:MET95 4.2 43.4 1.0 O4' C:MTE702 4.2 26.5 1.0 CA C:SER183 4.4 45.5 1.0 C4' C:MTE702 4.4 26.0 1.0 O3P C:MTE703 4.4 56.0 1.0 N C:SER183 4.5 41.3 1.0 CB C:SER185 4.5 48.8 1.0 OG C:SER183 4.5 50.2 1.0 C C:ALA184 4.5 43.4 1.0 CA C:MET94 4.5 45.1 1.0 N C:MET94 4.6 49.8 1.0 OG C:SER93 4.7 46.8 1.0 CB C:MET95 4.9 44.9 1.0 CA C:SER185 4.9 47.0 1.0 CB C:MET94 5.0 41.4 1.0 CB C:SER183 5.0 47.9 1.0

Magnesium binding site 4 out of 4 in the Active Site Complex Bambc of Benzoyl Coenzyme A Reductase in Complex with Benzoyl-Coa


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Active Site Complex Bambc of Benzoyl Coenzyme A Reductase in Complex with Benzoyl-Coa within 5.0Å range: probe atom residue distance (Å) B Occ D:Mg706 b:44.2 occ:1.00 O2P D:MTE704 1.9 56.7 1.0 O D:SER183 2.1 70.7 1.0 O3P D:MTE703 2.2 40.2 1.0 O D:MET94 2.3 55.9 1.0 P D:MTE704 3.1 43.5 1.0 C4' D:MTE704 3.3 52.2 1.0 C D:SER183 3.3 55.7 1.0 P D:MTE703 3.4 40.3 1.0 C D:MET94 3.5 54.3 1.0 O1P D:MTE704 3.6 61.3 1.0 O4' D:MTE704 3.6 54.1 1.0 O2P D:MTE703 3.7 31.9 1.0 OG D:SER185 3.9 45.6 1.0 N D:SER185 4.1 44.1 1.0 C4' D:MTE703 4.1 39.1 1.0 CA D:ALA184 4.1 58.7 1.0 N D:ALA184 4.2 55.5 1.0 O4' D:MTE703 4.2 49.2 1.0 N D:MET95 4.3 52.9 1.0 O3P D:MTE704 4.4 50.7 1.0 CA D:MET94 4.4 53.8 1.0 CA D:SER183 4.4 50.9 1.0 CA D:MET95 4.4 50.5 1.0 N D:MET94 4.5 52.5 1.0 O1P D:MTE703 4.6 42.4 1.0 CB D:SER185 4.6 43.6 1.0 N D:SER183 4.6 55.9 1.0 C D:ALA184 4.7 44.4 1.0 C3' D:MTE704 4.7 55.0 1.0 OG D:SER93 4.7 63.2 1.0 CB D:SER183 4.8 44.3 1.0 CB D:MET94 4.8 52.4 1.0 O3' D:MTE704 4.9 49.5 1.0 OG D:SER183 5.0 43.7 1.0

T.Weinert, S.G.Huwiler, J.W.Kung, S.Weidenweber, P.Hellwig, H.J.Stark, T.Biskup, S.Weber, J.J.Cotelesage, G.N.George, U.Ermler, M.Boll. Structural Basis of Enzymatic Benzene Ring Reduction. Nat.Chem.Biol. V. 11 586 2015.
ISSN: ESSN 1552-4469
PubMed: 26120796
DOI: 10.1038/NCHEMBIO.1849