Magnesium in PDB 4z40: Active Site Complex Bambc of Benzoyl Coenzyme A Reductase As Isolated

The structure of Active Site Complex Bambc of Benzoyl Coenzyme A Reductase As Isolated, PDB code: 4z40 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)	49.50 / 2.35
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	125.190, 116.820, 143.600, 90.00, 110.39, 90.00
R / Rfree (%)	21.2 / 23.8

The structure of Active Site Complex Bambc of Benzoyl Coenzyme A Reductase As Isolated also contains other interesting chemical elements:

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

The binding sites of Magnesium atom in the Active Site Complex Bambc of Benzoyl Coenzyme A Reductase As Isolated (pdb code 4z40). 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 As Isolated, PDB code: 4z40:
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 As Isolated


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 As Isolated within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg706 b:86.1 occ:1.00 O1P A:MTE704 1.9 0.1 1.0 O A:MET94 2.0 0.8 1.0 O3P A:MTE703 2.0 0.9 1.0 O A:SER183 2.2 0.1 1.0 C A:MET94 3.1 0.8 1.0 P A:MTE703 3.2 0.4 1.0 P A:MTE704 3.2 0.7 1.0 C A:SER183 3.4 0.3 1.0 O3P A:MTE704 3.4 0.7 1.0 O4' A:MTE703 3.7 89.8 1.0 O1P A:MTE703 3.7 0.9 1.0 C4' A:MTE703 3.8 92.9 1.0 N A:MET95 4.0 0.2 1.0 CA A:MET95 4.1 0.6 1.0 CA A:MET94 4.2 0.6 1.0 OG A:SER185 4.2 0.8 1.0 O2P A:MTE704 4.2 1.0 1.0 O4' A:MTE704 4.2 0.5 1.0 N A:ALA184 4.2 0.5 1.0 CA A:ALA184 4.2 0.3 1.0 N A:SER185 4.4 0.1 1.0 N A:MET94 4.4 0.4 1.0 C4' A:MTE704 4.4 1.0 1.0 O2P A:MTE703 4.4 0.6 1.0 CA A:SER183 4.5 0.6 1.0 CB A:MET94 4.5 0.7 1.0 O3' A:MTE703 4.6 0.4 1.0 N A:SER183 4.6 0.6 1.0 C3' A:MTE703 4.8 97.4 1.0 CB A:SER183 4.8 0.7 1.0 C A:ALA184 4.8 0.7 1.0 S2' A:MTE704 4.8 0.8 1.0 CB A:SER185 4.9 1.0 1.0 CB A:MET95 4.9 0.1 1.0 OG A:SER93 5.0 0.6 1.0

Magnesium binding site 2 out of 4 in the Active Site Complex Bambc of Benzoyl Coenzyme A Reductase As Isolated


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 As Isolated within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg706 b:59.1 occ:1.00 O2P B:MTE704 2.0 59.8 1.0 O3P B:MTE703 2.1 56.3 1.0 O B:SER183 2.2 63.4 1.0 O B:MET94 2.3 59.6 1.0 P B:MTE703 3.2 54.6 1.0 P B:MTE704 3.2 67.7 1.0 O2P B:MTE703 3.4 63.7 1.0 C B:SER183 3.4 63.2 1.0 C B:MET94 3.5 59.6 1.0 C4' B:MTE704 3.5 60.9 1.0 O1P B:MTE704 3.6 67.1 1.0 O4' B:MTE704 3.8 59.6 1.0 C4' B:MTE703 3.9 44.4 1.0 OG B:SER185 4.0 61.1 1.0 O4' B:MTE703 4.0 41.2 1.0 N B:SER185 4.3 58.3 1.0 N B:ALA184 4.3 62.0 1.0 CA B:ALA184 4.3 60.9 1.0 N B:MET95 4.3 59.1 1.0 O1P B:MTE703 4.4 53.0 1.0 CA B:MET95 4.4 57.8 1.0 CA B:SER183 4.4 63.3 1.0 O3P B:MTE704 4.5 69.3 1.0 CA B:MET94 4.5 59.2 1.0 N B:SER183 4.6 65.0 1.0 CB B:SER185 4.6 61.5 1.0 N B:MET94 4.6 58.8 1.0 CB B:SER183 4.6 63.0 1.0 C B:ALA184 4.8 57.8 1.0 CB B:MET94 4.8 61.0 1.0 C3' B:MTE704 4.8 63.1 1.0 C3' B:MTE703 5.0 50.4 1.0

Magnesium binding site 3 out of 4 in the Active Site Complex Bambc of Benzoyl Coenzyme A Reductase As Isolated


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 As Isolated within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg706 b:49.4 occ:1.00 O2P C:MTE704 1.9 0.3 1.0 O C:SER183 2.1 69.2 1.0 O3P C:MTE703 2.1 60.3 1.0 O C:MET94 2.6 56.8 1.0 P C:MTE703 3.2 57.5 1.0 O2P C:MTE703 3.2 54.9 1.0 P C:MTE704 3.2 0.8 1.0 C4' C:MTE704 3.3 58.0 1.0 C C:SER183 3.3 68.4 1.0 OG C:SER185 3.5 58.2 1.0 O4' C:MTE704 3.7 58.9 1.0 O1P C:MTE704 3.7 0.7 1.0 C C:MET94 3.8 62.7 1.0 C4' C:MTE703 3.9 57.8 1.0 O4' C:MTE703 4.0 57.9 1.0 N C:SER185 4.1 62.2 1.0 N C:ALA184 4.3 67.6 1.0 CA C:SER183 4.3 68.5 1.0 CA C:ALA184 4.3 66.7 1.0 CB C:SER185 4.3 59.9 1.0 CB C:SER183 4.4 66.6 1.0 O1P C:MTE703 4.4 58.8 1.0 O3P C:MTE704 4.4 0.3 1.0 N C:SER183 4.5 69.7 1.0 C3' C:MTE704 4.6 56.6 1.0 CA C:MET95 4.6 60.7 1.0 N C:MET95 4.7 60.9 1.0 C C:ALA184 4.7 63.7 1.0 OG C:SER183 4.8 66.9 1.0 O3' C:MTE704 4.8 57.6 1.0 CA C:MET94 4.8 62.6 1.0 CA C:SER185 4.9 62.3 1.0 N C:MET94 4.9 64.3 1.0 N5 C:MTE704 5.0 62.2 1.0

Magnesium binding site 4 out of 4 in the Active Site Complex Bambc of Benzoyl Coenzyme A Reductase As Isolated


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 As Isolated within 5.0Å range: probe atom residue distance (Å) B Occ D:Mg706 b:47.5 occ:1.00 O2P D:MTE704 1.9 97.1 1.0 O D:SER183 2.3 59.8 1.0 O3P D:MTE703 2.3 66.6 1.0 O D:MET94 2.6 59.6 1.0 P D:MTE704 3.1 50.1 1.0 P D:MTE703 3.3 66.0 1.0 C4' D:MTE704 3.3 48.0 1.0 O1P D:MTE703 3.4 34.8 1.0 C D:SER183 3.5 59.8 1.0 O3P D:MTE704 3.6 44.6 1.0 O4' D:MTE704 3.6 48.3 1.0 OG D:SER185 3.7 61.5 1.0 C D:MET94 3.8 59.6 1.0 C4' D:MTE703 4.0 55.9 1.0 O4' D:MTE703 4.1 58.9 1.0 O D:HOH811 4.1 57.2 1.0 N D:SER185 4.2 58.6 1.0 N D:ALA184 4.4 59.1 1.0 O1P D:MTE704 4.4 53.4 1.0 CB D:SER185 4.4 61.0 1.0 CA D:ALA184 4.4 59.5 1.0 CA D:SER183 4.4 62.1 1.0 C3' D:MTE704 4.5 47.8 1.0 O2P D:MTE703 4.6 66.2 1.0 CB D:SER183 4.6 62.9 1.0 N D:MET95 4.6 59.4 1.0 N D:SER183 4.6 64.2 1.0 CA D:MET95 4.7 57.9 1.0 O3' D:MTE704 4.7 46.6 1.0 CA D:MET94 4.7 59.8 1.0 C D:ALA184 4.8 58.8 1.0 N D:MET94 4.8 60.9 1.0 OG D:SER183 5.0 62.5 1.0 CA D:SER185 5.0 59.0 1.0 N5 D:MTE704 5.0 58.4 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