Iron in PDB 7y9j: Crystal Structure of P450 BM3-Tmk From Bacillus Megaterium in Complex with 5-Nitro-1,2-Benzisoxazole

All present enzymatic activity of Crystal Structure of P450 BM3-Tmk From Bacillus Megaterium in Complex with 5-Nitro-1,2-Benzisoxazole:
1.14.14.1; 1.6.2.4;

The structure of Crystal Structure of P450 BM3-Tmk From Bacillus Megaterium in Complex with 5-Nitro-1,2-Benzisoxazole, PDB code: 7y9j was solved by Q.Wang, L.L.Zhang, W.D.Liu, J.-W.Huang, Y.Yang, C.-C.Chen, R.-T.Guo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	24.73 / 1.83
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	58.767, 146.73, 63.587, 90, 97.71, 90
R / Rfree (%)	19.6 / 23.2

The binding sites of Iron atom in the Crystal Structure of P450 BM3-Tmk From Bacillus Megaterium in Complex with 5-Nitro-1,2-Benzisoxazole (pdb code 7y9j). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Crystal Structure of P450 BM3-Tmk From Bacillus Megaterium in Complex with 5-Nitro-1,2-Benzisoxazole, PDB code: 7y9j:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of P450 BM3-Tmk From Bacillus Megaterium in Complex with 5-Nitro-1,2-Benzisoxazole


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure of P450 BM3-Tmk From Bacillus Megaterium in Complex with 5-Nitro-1,2-Benzisoxazole within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:28.2 occ:1.00 FE A:HEM501 0.0 28.2 1.0 NB A:HEM501 2.0 20.7 1.0 NC A:HEM501 2.1 26.2 1.0 NA A:HEM501 2.1 29.3 1.0 ND A:HEM501 2.1 21.4 1.0 O A:HOH635 2.4 36.2 1.0 SG A:CYS401 2.5 27.3 1.0 C4B A:HEM501 3.0 28.6 1.0 C1B A:HEM501 3.0 27.9 1.0 C1C A:HEM501 3.1 30.3 1.0 C4A A:HEM501 3.1 26.2 1.0 C1D A:HEM501 3.1 28.3 1.0 C4C A:HEM501 3.1 30.0 1.0 C4D A:HEM501 3.1 29.0 1.0 C1A A:HEM501 3.1 26.4 1.0 CB A:CYS401 3.4 24.9 1.0 CHC A:HEM501 3.4 27.8 1.0 CHD A:HEM501 3.4 30.4 1.0 CHB A:HEM501 3.4 27.0 1.0 CHA A:HEM501 3.5 29.3 1.0 CA A:CYS401 4.0 26.2 1.0 O A:ALA265 4.2 38.6 1.0 C3B A:HEM501 4.3 23.1 1.0 C2B A:HEM501 4.3 23.2 1.0 C2C A:HEM501 4.3 29.5 1.0 C3A A:HEM501 4.3 25.7 1.0 C3C A:HEM501 4.3 30.3 1.0 C2D A:HEM501 4.3 25.4 1.0 C2A A:HEM501 4.3 27.4 1.0 C3D A:HEM501 4.3 27.8 1.0 O A:HOH840 4.5 57.9 1.0 CB A:ALA265 4.7 30.3 1.0 C A:CYS401 4.8 28.7 1.0 C A:ALA265 4.9 36.1 1.0 N A:GLY403 4.9 27.9 1.0

Iron binding site 2 out of 2 in the Crystal Structure of P450 BM3-Tmk From Bacillus Megaterium in Complex with 5-Nitro-1,2-Benzisoxazole


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structure of P450 BM3-Tmk From Bacillus Megaterium in Complex with 5-Nitro-1,2-Benzisoxazole within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe501 b:29.0 occ:1.00 FE B:HEM501 0.0 29.0 1.0 NB B:HEM501 2.0 21.0 1.0 ND B:HEM501 2.1 19.9 1.0 NA B:HEM501 2.1 27.9 1.0 NC B:HEM501 2.1 27.4 1.0 SG B:CYS401 2.5 26.4 1.0 OAA B:H5J502 2.5 35.8 1.0 C1B B:HEM501 3.0 28.3 1.0 C4B B:HEM501 3.0 28.8 1.0 C1D B:HEM501 3.1 25.6 1.0 C4A B:HEM501 3.1 26.9 1.0 C1C B:HEM501 3.1 25.5 1.0 C4C B:HEM501 3.1 27.5 1.0 C4D B:HEM501 3.1 28.2 1.0 C1A B:HEM501 3.1 27.8 1.0 CB B:CYS401 3.3 28.2 1.0 CHC B:HEM501 3.4 27.1 1.0 CHD B:HEM501 3.4 25.6 1.0 CHB B:HEM501 3.4 27.1 1.0 CHA B:HEM501 3.5 27.6 1.0 NAL B:H5J502 3.9 47.4 1.0 CA B:CYS401 4.1 24.7 1.0 C2B B:HEM501 4.2 25.2 1.0 C3B B:HEM501 4.2 23.4 1.0 O B:ALA265 4.2 33.5 1.0 C2C B:HEM501 4.3 27.6 1.0 C2D B:HEM501 4.3 27.3 1.0 C3C B:HEM501 4.3 27.6 1.0 C3A B:HEM501 4.3 25.7 1.0 C3D B:HEM501 4.3 26.2 1.0 C2A B:HEM501 4.3 27.1 1.0 CB B:ALA265 4.7 33.0 1.0 OAB B:H5J502 4.7 49.0 1.0 CAI B:H5J502 4.8 50.3 1.0 CAC B:H5J502 4.8 47.6 1.0 C B:CYS401 4.9 25.4 1.0 C B:ALA265 4.9 35.4 1.0 N B:GLY403 4.9 25.7 1.0

A.Li, Q.Wang, X.Song, X.Zhang, J.W.Huang, C.C.Chen, R.T.Guo, B.Wang, M.T.Reetz. Engineering of A P450-Based Kemp Eliminase with A New Mechanism Chinese J Catal V. 47 191 2023.
DOI: 10.1016/S1872-2067(23)64389-X