Iron in PDB 9ist: Crystal Structure of Cytochrome P450BM3 VI-18A12 Mutant Heme Domain with N-Decanoyl-L-Homoserine Lactone

All present enzymatic activity of Crystal Structure of Cytochrome P450BM3 VI-18A12 Mutant Heme Domain with N-Decanoyl-L-Homoserine Lactone:
1.14.14.1; 1.6.2.4;

The structure of Crystal Structure of Cytochrome P450BM3 VI-18A12 Mutant Heme Domain with N-Decanoyl-L-Homoserine Lactone, PDB code: 9ist was solved by Y.Yokoyama, H.Sugimoto, O.Shoji, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.00 / 2.27
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	58.482, 148.785, 61.374, 90, 98.91, 90
R / Rfree (%)	18.9 / 25.9

The binding sites of Iron atom in the Crystal Structure of Cytochrome P450BM3 VI-18A12 Mutant Heme Domain with N-Decanoyl-L-Homoserine Lactone (pdb code 9ist). 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 Cytochrome P450BM3 VI-18A12 Mutant Heme Domain with N-Decanoyl-L-Homoserine Lactone, PDB code: 9ist:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of Cytochrome P450BM3 VI-18A12 Mutant Heme Domain with N-Decanoyl-L-Homoserine Lactone


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 Cytochrome P450BM3 VI-18A12 Mutant Heme Domain with N-Decanoyl-L-Homoserine Lactone within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:15.9 occ:1.00 FE A:HEM501 0.0 15.9 1.0 ND A:HEM501 1.9 17.9 1.0 NA A:HEM501 2.0 17.0 1.0 NC A:HEM501 2.1 18.6 1.0 NB A:HEM501 2.1 18.2 1.0 SG A:CYS400 2.3 15.1 1.0 S A:DMS503 2.4 25.3 1.0 O A:DMS503 2.7 24.6 1.0 C4D A:HEM501 2.9 18.6 1.0 C1D A:HEM501 2.9 18.1 1.0 C1A A:HEM501 2.9 18.2 1.0 C4B A:HEM501 3.0 18.4 1.0 C4A A:HEM501 3.0 17.2 1.0 C4C A:HEM501 3.1 19.5 1.0 C1B A:HEM501 3.1 18.1 1.0 C1C A:HEM501 3.1 19.9 1.0 CHA A:HEM501 3.4 19.4 1.0 CB A:CYS400 3.4 15.7 1.0 CHD A:HEM501 3.4 19.0 1.0 CHB A:HEM501 3.5 17.9 1.0 CHC A:HEM501 3.5 19.4 1.0 C1 A:DMS503 3.6 25.7 1.0 C2 A:DMS503 3.8 24.9 1.0 CA A:CYS400 4.1 16.4 1.0 C2A A:HEM501 4.2 18.0 1.0 C3A A:HEM501 4.2 18.2 1.0 C2D A:HEM501 4.2 18.1 1.0 C3D A:HEM501 4.2 19.5 1.0 C3B A:HEM501 4.3 18.8 1.0 C2B A:HEM501 4.3 18.6 1.0 C3C A:HEM501 4.3 20.8 1.0 C2C A:HEM501 4.3 21.3 1.0 C A:CYS400 5.0 16.9 1.0

Iron binding site 2 out of 2 in the Crystal Structure of Cytochrome P450BM3 VI-18A12 Mutant Heme Domain with N-Decanoyl-L-Homoserine Lactone


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 Cytochrome P450BM3 VI-18A12 Mutant Heme Domain with N-Decanoyl-L-Homoserine Lactone within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe501 b:14.4 occ:1.00 FE B:HEM501 0.0 14.4 1.0 ND B:HEM501 1.9 16.5 1.0 NA B:HEM501 2.0 15.7 1.0 NC B:HEM501 2.1 15.7 1.0 NB B:HEM501 2.1 15.6 1.0 SG B:CYS400 2.4 16.1 1.0 S B:DMS503 2.5 27.2 1.0 O B:DMS503 2.7 25.9 1.0 C1D B:HEM501 2.9 17.5 1.0 C4D B:HEM501 2.9 15.9 1.0 C4A B:HEM501 3.0 15.7 1.0 C1A B:HEM501 3.0 16.0 1.0 C4C B:HEM501 3.0 17.3 1.0 C1B B:HEM501 3.1 15.8 1.0 C4B B:HEM501 3.1 16.0 1.0 C1C B:HEM501 3.1 16.4 1.0 CB B:CYS400 3.4 17.1 1.0 CHD B:HEM501 3.4 17.7 1.0 CHB B:HEM501 3.4 16.2 1.0 CHA B:HEM501 3.4 16.1 1.0 CHC B:HEM501 3.5 16.3 1.0 C2 B:DMS503 3.6 28.9 1.0 C1 B:DMS503 4.0 26.4 1.0 CA B:CYS400 4.1 16.8 1.0 C2D B:HEM501 4.1 18.8 1.0 C3D B:HEM501 4.2 17.0 1.0 C3A B:HEM501 4.2 16.2 1.0 C2A B:HEM501 4.2 16.3 1.0 C3C B:HEM501 4.3 17.7 1.0 C2C B:HEM501 4.3 17.2 1.0 C2B B:HEM501 4.3 16.7 1.0 C3B B:HEM501 4.3 16.9 1.0 CB B:ALA264 4.9 22.3 1.0 C B:CYS400 5.0 17.6 1.0

Y.Yokoyama, S.Ariyasu, M.Karasawa, C.Kasai, Y.Aiba, H.Sugimoto, O.Shoji. Bacterial Acyl Homoserine Lactones Triggered Non-Native Substrate Hydroxylation Catalyzed By Directed-Evolution-Derived Cytochrome P450BM3 Mutants Chemcatchem 2024.
ISSN: ESSN 1867-3899
DOI: 10.1002/CCTC.202401641