Iron in PDB 8jc3: Crystal Structure of the P450 BM3 Heme Domain Mutant F87A-T268V in Complex with Pyd-N-C4-Phe and Hydroxylamine

All present enzymatic activity of Crystal Structure of the P450 BM3 Heme Domain Mutant F87A-T268V in Complex with Pyd-N-C4-Phe and Hydroxylamine:
1.14.14.1; 1.6.2.4;

The structure of Crystal Structure of the P450 BM3 Heme Domain Mutant F87A-T268V in Complex with Pyd-N-C4-Phe and Hydroxylamine, PDB code: 8jc3 was solved by Y.Jiang, S.Dong, Y.Feng, Z.Cong, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.42 / 1.82
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	58.556, 147.58, 64.598, 90, 100.21, 90
R / Rfree (%)	19 / 21.2

The binding sites of Iron atom in the Crystal Structure of the P450 BM3 Heme Domain Mutant F87A-T268V in Complex with Pyd-N-C4-Phe and Hydroxylamine (pdb code 8jc3). 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 the P450 BM3 Heme Domain Mutant F87A-T268V in Complex with Pyd-N-C4-Phe and Hydroxylamine, PDB code: 8jc3:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of the P450 BM3 Heme Domain Mutant F87A-T268V in Complex with Pyd-N-C4-Phe and Hydroxylamine


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 the P450 BM3 Heme Domain Mutant F87A-T268V in Complex with Pyd-N-C4-Phe and Hydroxylamine within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe501 b:14.9 occ:1.00 FE B:HEM501 0.0 14.9 1.0 NB B:HEM501 2.0 12.0 1.0 NA B:HEM501 2.0 12.6 1.0 ND B:HEM501 2.0 12.5 1.0 NC B:HEM501 2.1 15.0 1.0 N B:HOA502 2.4 20.6 1.0 O B:HOA502 2.5 27.3 1.0 SG B:CYS400 2.5 15.9 1.0 C1B B:HEM501 3.0 15.6 1.0 C4B B:HEM501 3.0 13.6 1.0 C4A B:HEM501 3.0 12.4 1.0 C1D B:HEM501 3.1 15.5 1.0 C4C B:HEM501 3.1 13.7 1.0 C1C B:HEM501 3.1 13.4 1.0 C4D B:HEM501 3.1 15.1 1.0 C1A B:HEM501 3.1 16.9 1.0 CB B:CYS400 3.4 12.6 1.0 CHB B:HEM501 3.4 14.6 1.0 CHC B:HEM501 3.4 15.1 1.0 CHD B:HEM501 3.4 15.3 1.0 CHA B:HEM501 3.5 14.2 1.0 CA B:CYS400 4.1 12.0 1.0 C2B B:HEM501 4.3 12.2 1.0 C3B B:HEM501 4.3 15.2 1.0 C3A B:HEM501 4.3 11.6 1.0 C2D B:HEM501 4.3 14.7 1.0 C3D B:HEM501 4.3 12.5 1.0 C2C B:HEM501 4.3 15.4 1.0 C2A B:HEM501 4.3 15.8 1.0 C3C B:HEM501 4.3 14.8 1.0 O B:ALA264 4.4 21.7 1.0 N32 B:LXO503 4.5 13.2 0.5 N B:GLY402 4.8 17.2 1.0 C B:CYS400 4.9 15.3 1.0 C33 B:LXO503 4.9 16.3 0.5

Iron binding site 2 out of 2 in the Crystal Structure of the P450 BM3 Heme Domain Mutant F87A-T268V in Complex with Pyd-N-C4-Phe and Hydroxylamine


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 the P450 BM3 Heme Domain Mutant F87A-T268V in Complex with Pyd-N-C4-Phe and Hydroxylamine within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:15.4 occ:1.00 FE A:HEM501 0.0 15.4 1.0 ND A:HEM501 2.0 11.5 1.0 NB A:HEM501 2.0 11.0 1.0 NC A:HEM501 2.0 16.3 1.0 NA A:HEM501 2.1 12.2 1.0 O A:HOA502 2.4 27.2 1.0 N A:HOA502 2.4 23.0 1.0 SG A:CYS400 2.6 15.7 1.0 C1D A:HEM501 3.0 17.8 1.0 C1B A:HEM501 3.0 15.3 1.0 C4C A:HEM501 3.0 16.9 1.0 C4A A:HEM501 3.1 15.1 1.0 C4D A:HEM501 3.1 17.4 1.0 C4B A:HEM501 3.1 15.1 1.0 C1C A:HEM501 3.1 14.6 1.0 C1A A:HEM501 3.1 15.2 1.0 CHD A:HEM501 3.4 18.7 1.0 CHB A:HEM501 3.4 14.4 1.0 CB A:CYS400 3.4 14.1 1.0 CHC A:HEM501 3.5 14.9 1.0 CHA A:HEM501 3.5 12.8 1.0 CA A:CYS400 4.1 14.9 1.0 C2D A:HEM501 4.3 14.4 1.0 C2B A:HEM501 4.3 13.0 1.0 C3C A:HEM501 4.3 14.0 1.0 C3D A:HEM501 4.3 14.0 1.0 C2C A:HEM501 4.3 16.4 1.0 C3B A:HEM501 4.3 16.1 1.0 C3A A:HEM501 4.3 11.0 1.0 C2A A:HEM501 4.3 12.0 1.0 O A:ALA264 4.4 28.5 1.0 N32 A:LXO503 4.5 17.9 0.5 N A:GLY402 4.8 14.1 1.0 C A:CYS400 4.9 16.3 1.0 C33 A:LXO503 5.0 18.8 0.5 C A:ALA264 5.0 27.2 1.0

X.Qin, Y.Jiang, J.Chen, F.Yao, L.Jin, Z.Cong. C(SP3)-H Hydroxylation of Broad-Spectrum Alkanes Catalyzed By An Artificial P450 Peroxygenase Driven By Omega-Pyridyl Fatty Acyl Amino Acids. Mol Catal V. 550 2023.
ISSN: ESSN 2468-8231
DOI: 10.1016/J.MCAT.2023.113618