Iron in PDB 7ydd: Crystal Structure of the P450 BM3 Heme Domain Mutant F87A/T268P/V78I in Complex with N-Imidazolyl-Pentanoyl-L-Phenylalanine,Propylbenzene and Hydroxylamine

The structure of Crystal Structure of the P450 BM3 Heme Domain Mutant F87A/T268P/V78I in Complex with N-Imidazolyl-Pentanoyl-L-Phenylalanine,Propylbenzene and Hydroxylamine, PDB code: 7ydd was solved by S.Dong, J.Chen, Y.Jiang, Z.Cong, Y.Feng, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	37.51 / 1.66
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	58.443, 148.259, 63.899, 90, 99.71, 90
R / Rfree (%)	15.6 / 19.3

The binding sites of Iron atom in the Crystal Structure of the P450 BM3 Heme Domain Mutant F87A/T268P/V78I in Complex with N-Imidazolyl-Pentanoyl-L-Phenylalanine,Propylbenzene and Hydroxylamine (pdb code 7ydd). 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/T268P/V78I in Complex with N-Imidazolyl-Pentanoyl-L-Phenylalanine,Propylbenzene and Hydroxylamine, PDB code: 7ydd:
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/T268P/V78I in Complex with N-Imidazolyl-Pentanoyl-L-Phenylalanine,Propylbenzene 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/T268P/V78I in Complex with N-Imidazolyl-Pentanoyl-L-Phenylalanine,Propylbenzene and Hydroxylamine within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe502 b:18.4 occ:1.00 FE A:HEM502 0.0 18.4 1.0 NB A:HEM502 2.0 16.0 1.0 NA A:HEM502 2.0 16.7 1.0 ND A:HEM502 2.0 15.5 1.0 NC A:HEM502 2.1 16.6 1.0 N A:HOA501 2.1 21.1 1.0 SG A:CYS400 2.3 19.6 1.0 C1A A:HEM502 3.0 16.2 1.0 C1B A:HEM502 3.0 17.2 1.0 C1D A:HEM502 3.0 17.5 1.0 C4B A:HEM502 3.0 17.2 1.0 C4A A:HEM502 3.0 17.1 1.0 O A:HOA501 3.0 27.3 1.0 C1C A:HEM502 3.1 18.9 1.0 C4C A:HEM502 3.1 19.2 1.0 C4D A:HEM502 3.1 20.6 1.0 CB A:CYS400 3.4 15.0 1.0 CHD A:HEM502 3.4 20.3 1.0 CHA A:HEM502 3.4 22.1 1.0 CHC A:HEM502 3.4 17.1 1.0 CHB A:HEM502 3.5 17.9 1.0 CA A:CYS400 4.1 16.5 1.0 C3B A:HEM502 4.2 17.1 1.0 C2D A:HEM502 4.3 21.2 1.0 C2B A:HEM502 4.3 18.9 1.0 C2C A:HEM502 4.3 19.8 1.0 C3C A:HEM502 4.3 19.7 1.0 C3A A:HEM502 4.3 15.8 1.0 C3D A:HEM502 4.3 17.9 1.0 C2A A:HEM502 4.3 18.2 1.0 CAG A:3H0503 4.6 86.1 1.0 CAA A:3H0503 4.7 79.0 1.0 C A:CYS400 4.9 20.2 1.0 CB A:ALA264 4.9 26.1 1.0 O A:ALA264 4.9 25.0 1.0 N A:GLY402 4.9 21.2 1.0

Iron binding site 2 out of 2 in the Crystal Structure of the P450 BM3 Heme Domain Mutant F87A/T268P/V78I in Complex with N-Imidazolyl-Pentanoyl-L-Phenylalanine,Propylbenzene 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/T268P/V78I in Complex with N-Imidazolyl-Pentanoyl-L-Phenylalanine,Propylbenzene and Hydroxylamine within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe503 b:18.9 occ:1.00 FE B:HEM503 0.0 18.9 1.0 NB B:HEM503 2.0 18.0 1.0 NC B:HEM503 2.0 16.8 1.0 NA B:HEM503 2.0 16.8 1.0 ND B:HEM503 2.0 17.1 1.0 N B:HOA502 2.1 19.5 1.0 SG B:CYS400 2.3 18.0 1.0 C1B B:HEM503 3.0 17.6 1.0 C4A B:HEM503 3.0 14.8 1.0 C4C B:HEM503 3.0 15.4 1.0 C1C B:HEM503 3.0 16.9 1.0 C1A B:HEM503 3.0 16.8 1.0 C4D B:HEM503 3.0 17.6 1.0 C4B B:HEM503 3.1 16.1 1.0 C1D B:HEM503 3.1 17.5 1.0 O B:HOA502 3.1 26.1 1.0 CB B:CYS400 3.3 17.2 1.0 CHB B:HEM503 3.4 17.4 1.0 CHA B:HEM503 3.4 19.6 1.0 CHD B:HEM503 3.5 14.9 1.0 CHC B:HEM503 3.5 17.4 1.0 CA B:CYS400 4.0 16.4 1.0 C2B B:HEM503 4.2 15.9 1.0 C3A B:HEM503 4.2 18.0 1.0 C2C B:HEM503 4.2 20.4 1.0 C3C B:HEM503 4.2 17.6 1.0 C2A B:HEM503 4.3 16.3 1.0 C2D B:HEM503 4.3 19.9 1.0 C3B B:HEM503 4.3 16.6 1.0 C3D B:HEM503 4.3 17.4 1.0 CAG B:3H0501 4.5 104.2 1.0 C B:CYS400 4.8 21.5 1.0 CB B:ALA264 4.9 23.3 1.0 O B:ALA264 4.9 24.8 1.0 CAA B:3H0501 5.0 101.2 1.0 N B:GLY402 5.0 17.8 1.0 N22 B:IRV504 5.0 31.4 0.6

J.Chen, S.Dong, W.Fang, Y.Jiang, Z.Chen, X.Qin, C.Wang, H.Zhou, L.Jin, Y.Feng, B.Wang, Z.Cong. Regiodivergent and Enantioselective Hydroxylation of C-H Bonds By Synergistic Use of Protein Engineering and Exogenous Dual-Functional Small Molecules. Angew.Chem.Int.Ed.Engl. V. 62 15088 2023.
ISSN: ESSN 1521-3773
PubMed: 36417593
DOI: 10.1002/ANIE.202215088