Manganese in PDB 5zis: Crystal Structure of Mn-Protoporphyrinix-Reconstituted P450BM3

All present enzymatic activity of Crystal Structure of Mn-Protoporphyrinix-Reconstituted P450BM3:
1.14.14.1; 1.6.2.4;

The structure of Crystal Structure of Mn-Protoporphyrinix-Reconstituted P450BM3, PDB code: 5zis was solved by K.Omura, Y.Aiba, H.Onoda, H.Sugimoto, O.Shoji, Y.Watanabe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.93 / 3.10
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	104.760, 155.320, 208.980, 90.00, 90.00, 90.00
R / Rfree (%)	25.8 / 29

The binding sites of Manganese atom in the Crystal Structure of Mn-Protoporphyrinix-Reconstituted P450BM3 (pdb code 5zis). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 4 binding sites of Manganese where determined in the Crystal Structure of Mn-Protoporphyrinix-Reconstituted P450BM3, PDB code: 5zis:
Jump to Manganese binding site number: 1; 2; 3; 4;

Manganese binding site 1 out of 4 in the Crystal Structure of Mn-Protoporphyrinix-Reconstituted P450BM3


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of Mn-Protoporphyrinix-Reconstituted P450BM3 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn500 b:63.5 occ:1.00 MN A:MNH500 0.0 63.5 1.0 NA A:MNH500 2.1 60.0 1.0 NB A:MNH500 2.1 62.6 1.0 ND A:MNH500 2.1 69.9 1.0 NC A:MNH500 2.1 66.6 1.0 SG A:CYS400 2.3 82.2 1.0 C4A A:MNH500 3.0 58.4 1.0 C4B A:MNH500 3.1 60.4 1.0 C1C A:MNH500 3.1 64.5 1.0 C1A A:MNH500 3.1 61.8 1.0 C4D A:MNH500 3.1 74.4 1.0 C1D A:MNH500 3.1 69.1 1.0 C4C A:MNH500 3.1 65.1 1.0 C1B A:MNH500 3.2 61.0 1.0 CHB A:MNH500 3.4 59.1 1.0 CHC A:MNH500 3.5 63.4 1.0 CHA A:MNH500 3.5 69.5 1.0 CHD A:MNH500 3.5 64.8 1.0 CB A:CYS400 3.5 87.8 1.0 CA A:CYS400 4.1 92.9 1.0 C3A A:MNH500 4.2 56.6 1.0 CE2 A:PHE87 4.3 90.9 1.0 C2D A:MNH500 4.3 71.5 1.0 C2A A:MNH500 4.3 60.5 1.0 C2C A:MNH500 4.3 61.1 1.0 C3D A:MNH500 4.3 77.3 1.0 C3C A:MNH500 4.3 64.7 1.0 C3B A:MNH500 4.3 58.2 1.0 C2B A:MNH500 4.4 63.3 1.0 CD2 A:PHE87 4.5 90.8 1.0 O A:ALA264 4.7 76.9 1.0 OG1 A:THR268 4.9 73.6 1.0 CB A:ALA264 5.0 85.7 1.0

Manganese binding site 2 out of 4 in the Crystal Structure of Mn-Protoporphyrinix-Reconstituted P450BM3


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Crystal Structure of Mn-Protoporphyrinix-Reconstituted P450BM3 within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn500 b:81.8 occ:1.00 MN B:MNH500 0.0 81.8 1.0 NA B:MNH500 2.1 82.9 1.0 NC B:MNH500 2.1 79.6 1.0 ND B:MNH500 2.1 77.6 1.0 NB B:MNH500 2.1 78.3 1.0 SG B:CYS400 2.4 85.0 1.0 C4A B:MNH500 3.0 79.2 1.0 C1D B:MNH500 3.1 77.0 1.0 C1C B:MNH500 3.1 76.8 1.0 C4C B:MNH500 3.1 77.5 1.0 C4B B:MNH500 3.1 78.7 1.0 C4D B:MNH500 3.1 76.9 1.0 C1A B:MNH500 3.1 79.4 1.0 C1B B:MNH500 3.2 76.6 1.0 CB B:CYS400 3.2 85.4 1.0 CHB B:MNH500 3.4 77.2 1.0 CHC B:MNH500 3.5 78.3 1.0 CHD B:MNH500 3.5 80.4 1.0 CHA B:MNH500 3.5 76.1 1.0 CA B:CYS400 4.1 84.7 1.0 C3A B:MNH500 4.3 74.0 1.0 C2D B:MNH500 4.3 76.8 1.0 C2C B:MNH500 4.3 75.5 1.0 C3C B:MNH500 4.3 75.2 1.0 C3D B:MNH500 4.3 79.6 1.0 C2A B:MNH500 4.3 74.6 1.0 C3B B:MNH500 4.3 79.4 1.0 C2B B:MNH500 4.4 74.0 1.0 CE2 B:PHE87 4.5 71.6 1.0 O B:ALA264 4.8 87.6 1.0 OG1 B:THR268 4.8 84.7 1.0 CB B:ALA264 4.8 78.7 1.0 C B:CYS400 4.9 87.6 1.0

Manganese binding site 3 out of 4 in the Crystal Structure of Mn-Protoporphyrinix-Reconstituted P450BM3


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Crystal Structure of Mn-Protoporphyrinix-Reconstituted P450BM3 within 5.0Å range: probe atom residue distance (Å) B Occ C:Mn500 b:53.8 occ:1.00 MN C:MNH500 0.0 53.8 1.0 NA C:MNH500 2.1 49.2 1.0 NB C:MNH500 2.1 53.7 1.0 NC C:MNH500 2.1 49.9 1.0 ND C:MNH500 2.1 51.3 1.0 SG C:CYS400 2.3 69.7 1.0 C4A C:MNH500 3.1 49.4 1.0 C4C C:MNH500 3.1 46.7 1.0 C4B C:MNH500 3.1 53.5 1.0 C1C C:MNH500 3.1 47.8 1.0 C1D C:MNH500 3.1 48.8 1.0 C1A C:MNH500 3.1 48.7 1.0 C4D C:MNH500 3.1 50.3 1.0 C1B C:MNH500 3.2 52.9 1.0 CB C:CYS400 3.4 72.9 1.0 CHB C:MNH500 3.4 48.3 1.0 CHC C:MNH500 3.5 50.1 1.0 CHD C:MNH500 3.5 45.9 1.0 CHA C:MNH500 3.5 51.4 1.0 CA C:CYS400 4.2 76.2 1.0 C3A C:MNH500 4.3 51.2 1.0 C2D C:MNH500 4.3 51.7 1.0 C2C C:MNH500 4.3 47.1 1.0 C3C C:MNH500 4.3 48.8 1.0 C2A C:MNH500 4.3 49.6 1.0 C3D C:MNH500 4.3 51.6 1.0 C3B C:MNH500 4.3 54.2 1.0 C2B C:MNH500 4.4 55.2 1.0 CE2 C:PHE87 4.5 64.5 1.0 O C:ALA264 4.7 62.9 1.0

Manganese binding site 4 out of 4 in the Crystal Structure of Mn-Protoporphyrinix-Reconstituted P450BM3


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 4 of Crystal Structure of Mn-Protoporphyrinix-Reconstituted P450BM3 within 5.0Å range: probe atom residue distance (Å) B Occ D:Mn500 b:54.0 occ:1.00 MN D:MNH500 0.0 54.0 1.0 NA D:MNH500 2.1 50.0 1.0 NC D:MNH500 2.1 55.8 1.0 ND D:MNH500 2.1 54.7 1.0 NB D:MNH500 2.1 60.2 1.0 SG D:CYS400 2.3 79.8 1.0 C4A D:MNH500 3.1 48.7 1.0 C1C D:MNH500 3.1 55.4 1.0 C4C D:MNH500 3.1 53.5 1.0 C4D D:MNH500 3.1 51.7 1.0 C1A D:MNH500 3.1 49.3 1.0 C1D D:MNH500 3.1 53.2 1.0 C4B D:MNH500 3.1 60.8 1.0 C1B D:MNH500 3.2 60.8 1.0 CB D:CYS400 3.3 82.6 1.0 CHB D:MNH500 3.5 55.3 1.0 CHC D:MNH500 3.5 57.1 1.0 CHD D:MNH500 3.5 54.3 1.0 CHA D:MNH500 3.5 47.3 1.0 CA D:CYS400 4.2 83.3 1.0 C3A D:MNH500 4.3 48.6 1.0 C2D D:MNH500 4.3 53.8 1.0 C2A D:MNH500 4.3 56.1 1.0 C2C D:MNH500 4.3 58.5 1.0 C3D D:MNH500 4.3 55.0 1.0 C3C D:MNH500 4.3 54.8 1.0 C3B D:MNH500 4.3 60.1 1.0 C2B D:MNH500 4.4 59.0 1.0 O D:ALA264 4.4 74.3 1.0 N D:GLY402 4.7 88.6 1.0 C D:CYS400 4.9 85.4 1.0 OG1 D:THR268 4.9 65.3 1.0

K.Omura, Y.Aiba, H.Onoda, J.K.Stanfield, S.Ariyasu, H.Sugimoto, Y.Shiro, O.Shoji, Y.Watanabe. Reconstitution of Full-Length P450BM3 with An Artificial Metal Complex By Utilising the Transpeptidase Sortase A. Chem. Commun. (Camb.) V. 54 7892 2018.
ISSN: ESSN 1364-548X
PubMed: 29845154
DOI: 10.1039/C8CC02760A