Iron in PDB 8jc4: Crystal Structure of the P450 BM3 Heme Domain Mutant F87A-T268V in Complex with Pyd-Pid-Phe and Hydroxylamine

All present enzymatic activity of Crystal Structure of the P450 BM3 Heme Domain Mutant F87A-T268V in Complex with Pyd-Pid-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-Pid-Phe and Hydroxylamine, PDB code: 8jc4 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)	19.89 / 2.64
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	58.839, 148.287, 64.925, 90, 100.38, 90
R / Rfree (%)	24.5 / 28

The binding sites of Iron atom in the Crystal Structure of the P450 BM3 Heme Domain Mutant F87A-T268V in Complex with Pyd-Pid-Phe and Hydroxylamine (pdb code 8jc4). 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-Pid-Phe and Hydroxylamine, PDB code: 8jc4:
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-Pid-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-Pid-Phe and Hydroxylamine within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe502 b:26.5 occ:1.00 FE A:HEM502 0.0 26.5 1.0 ND A:HEM502 2.0 30.6 1.0 NB A:HEM502 2.1 24.8 1.0 NA A:HEM502 2.1 25.7 1.0 NC A:HEM502 2.1 32.6 1.0 N A:HOA501 2.6 34.4 1.0 SG A:CYS400 2.9 20.9 1.0 O A:HOA501 3.0 24.4 1.0 C1D A:HEM502 3.1 31.6 1.0 C1C A:HEM502 3.1 26.4 1.0 C4C A:HEM502 3.1 27.7 1.0 C1B A:HEM502 3.1 24.1 1.0 C4D A:HEM502 3.1 26.6 1.0 C4A A:HEM502 3.1 27.1 1.0 C4B A:HEM502 3.1 25.1 1.0 C1A A:HEM502 3.1 27.2 1.0 CHD A:HEM502 3.4 30.9 1.0 CB A:CYS400 3.4 24.0 1.0 CHB A:HEM502 3.4 28.1 1.0 CHC A:HEM502 3.4 22.6 1.0 CHA A:HEM502 3.4 24.6 1.0 CA A:CYS400 4.2 21.8 1.0 C2C A:HEM502 4.3 33.5 1.0 C2D A:HEM502 4.3 29.3 1.0 C3C A:HEM502 4.3 29.8 1.0 C3D A:HEM502 4.3 26.0 1.0 C3A A:HEM502 4.3 24.3 1.0 C2B A:HEM502 4.3 28.9 1.0 C2A A:HEM502 4.3 22.7 1.0 C3B A:HEM502 4.3 24.9 1.0 O A:ALA264 4.4 37.9 1.0 CB A:ALA264 4.6 31.8 1.0 N24 A:UCH503 4.8 21.5 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-Pid-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-Pid-Phe and Hydroxylamine within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe502 b:24.9 occ:1.00 FE B:HEM502 0.0 24.9 1.0 ND B:HEM502 2.0 31.5 1.0 NA B:HEM502 2.0 26.3 1.0 NB B:HEM502 2.1 25.4 1.0 NC B:HEM502 2.1 30.2 1.0 N B:HOA501 2.7 25.9 1.0 O B:HOA501 2.8 29.7 1.0 SG B:CYS400 3.0 32.5 1.0 C4D B:HEM502 3.1 27.1 1.0 C1C B:HEM502 3.1 27.5 1.0 C1D B:HEM502 3.1 27.4 1.0 C1A B:HEM502 3.1 28.6 1.0 C4A B:HEM502 3.1 31.2 1.0 C4B B:HEM502 3.1 24.0 1.0 C1B B:HEM502 3.1 20.7 1.0 C4C B:HEM502 3.1 27.3 1.0 CHA B:HEM502 3.4 22.5 1.0 CHC B:HEM502 3.4 21.7 1.0 CHD B:HEM502 3.4 32.5 1.0 CHB B:HEM502 3.4 30.9 1.0 CB B:CYS400 3.5 26.4 1.0 CA B:CYS400 4.2 22.1 1.0 C2C B:HEM502 4.3 32.4 1.0 C3D B:HEM502 4.3 24.9 1.0 C2D B:HEM502 4.3 26.3 1.0 C2A B:HEM502 4.3 26.3 1.0 C3A B:HEM502 4.3 24.3 1.0 C3C B:HEM502 4.3 28.2 1.0 C2B B:HEM502 4.3 27.8 1.0 C3B B:HEM502 4.3 27.9 1.0 CB B:ALA264 4.5 28.6 1.0 N24 B:UCH503 4.9 31.1 0.6

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