Iron in PDB 7egn: Crystal Structure of the P450 BM3 Heme Domain Mutant F87A in Complex with N-Imidazolyl-Hexanoyl-L-Phenylalanine and Hydroxylamine

All present enzymatic activity of Crystal Structure of the P450 BM3 Heme Domain Mutant F87A in Complex with N-Imidazolyl-Hexanoyl-L-Phenylalanine and Hydroxylamine:
1.14.14.1; 1.6.2.4;

The structure of Crystal Structure of the P450 BM3 Heme Domain Mutant F87A in Complex with N-Imidazolyl-Hexanoyl-L-Phenylalanine and Hydroxylamine, PDB code: 7egn 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)	39.43 / 2.70
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	58.67, 147.557, 64.324, 90, 99.98, 90
R / Rfree (%)	20 / 24.5

The binding sites of Iron atom in the Crystal Structure of the P450 BM3 Heme Domain Mutant F87A in Complex with N-Imidazolyl-Hexanoyl-L-Phenylalanine and Hydroxylamine (pdb code 7egn). 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 in Complex with N-Imidazolyl-Hexanoyl-L-Phenylalanine and Hydroxylamine, PDB code: 7egn:
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 in Complex with N-Imidazolyl-Hexanoyl-L-Phenylalanine 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 in Complex with N-Imidazolyl-Hexanoyl-L-Phenylalanine and Hydroxylamine within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:33.2 occ:1.00 FE A:HEM501 0.0 33.2 1.0 ND A:HEM501 1.9 34.5 1.0 NA A:HEM501 2.0 42.6 1.0 NC A:HEM501 2.1 40.2 1.0 NB A:HEM501 2.1 37.0 1.0 SG A:CYS400 2.4 29.7 1.0 N A:HOA503 2.6 35.9 1.0 C4D A:HEM501 2.9 32.2 1.0 C1D A:HEM501 2.9 34.8 1.0 C1A A:HEM501 3.0 34.1 1.0 C4C A:HEM501 3.0 37.2 1.0 C4A A:HEM501 3.0 39.0 1.0 C1B A:HEM501 3.1 39.8 1.0 C4B A:HEM501 3.1 37.3 1.0 C1C A:HEM501 3.1 36.1 1.0 O A:HOA503 3.2 32.9 1.0 CHA A:HEM501 3.3 35.0 1.0 CHD A:HEM501 3.4 35.7 1.0 CB A:CYS400 3.4 34.8 1.0 CHB A:HEM501 3.5 39.6 1.0 CHC A:HEM501 3.5 40.4 1.0 CA A:CYS400 4.1 30.9 1.0 C3D A:HEM501 4.1 30.1 1.0 C2D A:HEM501 4.1 36.6 1.0 C2A A:HEM501 4.2 33.2 1.0 C3A A:HEM501 4.2 34.4 1.0 C3C A:HEM501 4.3 39.8 1.0 C2C A:HEM501 4.3 42.7 1.0 C2B A:HEM501 4.3 40.1 1.0 C3B A:HEM501 4.3 35.2 1.0 O A:ALA264 4.5 47.2 1.0 CB A:ALA264 4.7 41.1 1.0 C A:CYS400 4.9 29.0 1.0

Iron binding site 2 out of 2 in the Crystal Structure of the P450 BM3 Heme Domain Mutant F87A in Complex with N-Imidazolyl-Hexanoyl-L-Phenylalanine 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 in Complex with N-Imidazolyl-Hexanoyl-L-Phenylalanine and Hydroxylamine within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe501 b:30.6 occ:1.00 FE B:HEM501 0.0 30.6 1.0 ND B:HEM501 1.9 37.0 1.0 NA B:HEM501 2.0 40.4 1.0 NC B:HEM501 2.1 37.5 1.0 NB B:HEM501 2.1 38.2 1.0 N B:HOA503 2.2 40.2 1.0 O B:HOA503 2.7 40.6 1.0 SG B:CYS400 2.7 36.0 1.0 C4D B:HEM501 2.9 36.9 1.0 C1D B:HEM501 2.9 32.7 1.0 C1A B:HEM501 3.0 36.9 1.0 C4C B:HEM501 3.0 34.5 1.0 C4A B:HEM501 3.1 36.9 1.0 C1B B:HEM501 3.1 33.1 1.0 C4B B:HEM501 3.1 39.6 1.0 C1C B:HEM501 3.1 34.8 1.0 CHA B:HEM501 3.3 34.4 1.0 CB B:CYS400 3.3 34.7 1.0 CHD B:HEM501 3.4 36.3 1.0 CHB B:HEM501 3.5 32.5 1.0 CHC B:HEM501 3.5 37.9 1.0 CA B:CYS400 4.1 33.9 1.0 C3D B:HEM501 4.1 34.2 1.0 C2D B:HEM501 4.1 29.6 1.0 C2A B:HEM501 4.2 36.6 1.0 C3A B:HEM501 4.2 33.8 1.0 C3C B:HEM501 4.3 28.8 1.0 C2C B:HEM501 4.3 35.6 1.0 C2B B:HEM501 4.3 33.2 1.0 O B:ALA264 4.3 51.4 1.0 C3B B:HEM501 4.3 35.3 1.0 N2 B:IC6502 4.5 54.5 1.0 CB B:ALA264 4.9 45.6 1.0 C B:CYS400 4.9 29.4 1.0 N B:ILE401 4.9 29.2 1.0 C3 B:IC6502 5.0 55.9 1.0

X.Zhang, Y.Jiang, Q.Chen, S.Dong, Y.Feng, Z.Cong, S.Shaik, B.Wang. H-Bonding Networks Dictate the Molecular Mechanism of H2O2 Activation By P450 Acs Catalysis V. 11 8774 2021.
ISSN: ESSN 2155-5435
DOI: 10.1021/ACSCATAL.1C02068