Manganese in PDB 5zlh: 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: 5zlh 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 / 3.40
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 (%)	31 / 34.6

The binding sites of Manganese atom in the Crystal Structure of Mn-Protoporphyrinix-Reconstituted P450BM3 (pdb code 5zlh). 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: 5zlh:
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:26.8 occ:1.00 MN A:MNH500 0.0 26.8 1.0 NA A:MNH500 2.1 18.6 1.0 NB A:MNH500 2.1 18.6 1.0 ND A:MNH500 2.1 27.2 1.0 NC A:MNH500 2.1 17.5 1.0 SG A:CYS400 2.5 35.8 1.0 C4A A:MNH500 3.0 18.2 1.0 C4B A:MNH500 3.1 13.6 1.0 C1C A:MNH500 3.1 12.3 1.0 C1A A:MNH500 3.1 18.8 1.0 C4D A:MNH500 3.1 28.3 1.0 C1D A:MNH500 3.1 21.9 1.0 C4C A:MNH500 3.1 19.6 1.0 C1B A:MNH500 3.2 19.9 1.0 CHB A:MNH500 3.4 19.1 1.0 CB A:CYS400 3.4 20.1 1.0 CHC A:MNH500 3.5 11.9 1.0 CHA A:MNH500 3.5 26.7 1.0 CHD A:MNH500 3.5 15.6 1.0 CA A:CYS400 3.9 23.2 1.0 CE2 A:PHE87 3.9 33.0 1.0 CD2 A:PHE87 4.1 26.3 1.0 C3A A:MNH500 4.2 14.0 1.0 C2D A:MNH500 4.3 26.6 1.0 C2A A:MNH500 4.3 17.2 1.0 C2C A:MNH500 4.3 12.2 1.0 C3D A:MNH500 4.3 34.8 1.0 C3C A:MNH500 4.3 18.3 1.0 C3B A:MNH500 4.3 12.8 1.0 C2B A:MNH500 4.4 17.9 1.0 N A:CYS400 4.7 18.7 1.0 CB A:ALA264 5.0 31.2 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:32.9 occ:1.00 MN B:MNH500 0.0 32.9 1.0 NA B:MNH500 2.1 21.9 1.0 NC B:MNH500 2.1 17.7 1.0 ND B:MNH500 2.1 10.9 1.0 NB B:MNH500 2.1 14.8 1.0 SG B:CYS400 2.5 14.5 1.0 C4A B:MNH500 3.0 18.2 1.0 C1D B:MNH500 3.1 12.2 1.0 C1C B:MNH500 3.1 15.2 1.0 C4C B:MNH500 3.1 20.7 1.0 C4B B:MNH500 3.1 18.3 1.0 C4D B:MNH500 3.1 10.5 1.0 C1A B:MNH500 3.1 18.5 1.0 C1B B:MNH500 3.2 17.9 1.0 CB B:CYS400 3.3 19.2 1.0 CHB B:MNH500 3.4 23.4 1.0 CHC B:MNH500 3.5 21.1 1.0 CHD B:MNH500 3.5 20.0 1.0 CHA B:MNH500 3.5 16.6 1.0 CA B:CYS400 4.2 20.4 1.0 C3A B:MNH500 4.3 13.8 1.0 C2D B:MNH500 4.3 11.1 1.0 C2C B:MNH500 4.3 16.5 1.0 C3C B:MNH500 4.3 16.7 1.0 C3D B:MNH500 4.3 11.1 1.0 C2A B:MNH500 4.3 16.9 1.0 C3B B:MNH500 4.3 20.6 1.0 C2B B:MNH500 4.4 17.5 1.0 CE2 B:PHE87 4.5 12.2 1.0 O B:ALA264 4.7 16.5 1.0 OG1 B:THR268 4.7 26.9 1.0 CB B:ALA264 4.8 7.2 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:40.7 occ:1.00 MN C:MNH500 0.0 40.7 1.0 NA C:MNH500 2.1 24.5 1.0 NB C:MNH500 2.1 27.7 1.0 NC C:MNH500 2.1 14.4 1.0 ND C:MNH500 2.1 19.0 1.0 SG C:CYS400 2.3 22.1 1.0 C4A C:MNH500 3.1 26.6 1.0 C4C C:MNH500 3.1 9.2 1.0 C4B C:MNH500 3.1 27.9 1.0 C1C C:MNH500 3.1 15.9 1.0 C1D C:MNH500 3.1 17.4 1.0 C1A C:MNH500 3.1 18.3 1.0 C4D C:MNH500 3.1 17.2 1.0 C1B C:MNH500 3.2 25.5 1.0 CB C:CYS400 3.2 21.4 1.0 CHB C:MNH500 3.4 28.1 1.0 CHC C:MNH500 3.5 24.0 1.0 CHD C:MNH500 3.5 8.8 1.0 CHA C:MNH500 3.5 22.4 1.0 CA C:CYS400 3.9 16.1 1.0 C3A C:MNH500 4.3 27.3 1.0 C2D C:MNH500 4.3 13.0 1.0 C2C C:MNH500 4.3 14.8 1.0 C3C C:MNH500 4.3 11.4 1.0 C2A C:MNH500 4.3 21.8 1.0 C3D C:MNH500 4.3 12.5 1.0 C3B C:MNH500 4.3 27.9 1.0 C2B C:MNH500 4.4 24.6 1.0 CE2 C:PHE87 4.5 14.8 1.0 C C:CYS400 4.9 14.0 1.0 CD2 C:PHE393 5.0 30.6 1.0 N C:CYS400 5.0 21.0 1.0 N C:ILE401 5.0 10.9 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:19.9 occ:1.00 MN D:MNH500 0.0 19.9 1.0 NA D:MNH500 2.1 18.6 1.0 NC D:MNH500 2.1 16.3 1.0 ND D:MNH500 2.1 14.6 1.0 NB D:MNH500 2.1 20.9 1.0 SG D:CYS400 2.5 22.2 1.0 C4A D:MNH500 3.1 20.4 1.0 C1C D:MNH500 3.1 19.5 1.0 C4C D:MNH500 3.1 13.2 1.0 C4D D:MNH500 3.1 20.0 1.0 C1A D:MNH500 3.1 20.2 1.0 C1D D:MNH500 3.1 14.2 1.0 C4B D:MNH500 3.1 13.5 1.0 C1B D:MNH500 3.2 16.8 1.0 CB D:CYS400 3.3 30.9 1.0 CHB D:MNH500 3.5 18.9 1.0 CHC D:MNH500 3.5 13.4 1.0 CHD D:MNH500 3.5 13.0 1.0 CHA D:MNH500 3.5 22.4 1.0 C3A D:MNH500 4.3 19.5 1.0 C2D D:MNH500 4.3 12.8 1.0 C2A D:MNH500 4.3 26.1 1.0 C2C D:MNH500 4.3 19.3 1.0 C3D D:MNH500 4.3 14.8 1.0 C3C D:MNH500 4.3 15.8 1.0 CA D:CYS400 4.3 29.1 1.0 C3B D:MNH500 4.3 14.8 1.0 C2B D:MNH500 4.4 13.0 1.0 O D:ALA264 4.4 16.4 1.0 OG1 D:THR268 4.8 13.2 1.0 N D:GLY402 5.0 31.3 1.0 CE2 D:PHE87 5.0 21.6 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