Iron in PDB 3qi8: Evolved Variant of Cytochrome P450 (BM3, CYP102A1)

All present enzymatic activity of Evolved Variant of Cytochrome P450 (BM3, CYP102A1):
1.14.14.1;

The structure of Evolved Variant of Cytochrome P450 (BM3, CYP102A1), PDB code: 3qi8 was solved by A.Rentmeister, T.R.Brown, C.D.Snow, M.N.Carbone, F.H.Arnold, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.38 / 3.20
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	82.350, 83.770, 143.020, 90.00, 90.00, 90.00
R / Rfree (%)	20.8 / 27.4

The binding sites of Iron atom in the Evolved Variant of Cytochrome P450 (BM3, CYP102A1) (pdb code 3qi8). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Evolved Variant of Cytochrome P450 (BM3, CYP102A1), PDB code: 3qi8:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Evolved Variant of Cytochrome P450 (BM3, CYP102A1)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Evolved Variant of Cytochrome P450 (BM3, CYP102A1) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe472 b:62.0 occ:1.00 FE A:HEM472 0.0 62.0 1.0 ND A:HEM472 2.0 53.3 1.0 NA A:HEM472 2.1 63.3 1.0 NB A:HEM472 2.1 55.2 1.0 NC A:HEM472 2.1 61.6 1.0 SG A:CYS400 2.5 59.8 1.0 C1D A:HEM472 3.0 56.2 1.0 C4D A:HEM472 3.0 60.3 1.0 C4A A:HEM472 3.1 54.5 1.0 C4B A:HEM472 3.1 49.7 1.0 C1B A:HEM472 3.1 52.8 1.0 C1A A:HEM472 3.1 61.5 1.0 C4C A:HEM472 3.1 55.8 1.0 C1C A:HEM472 3.2 59.2 1.0 CHD A:HEM472 3.4 53.8 1.0 CHA A:HEM472 3.4 58.8 1.0 CHB A:HEM472 3.5 50.3 1.0 CB A:CYS400 3.5 65.7 1.0 CHC A:HEM472 3.5 51.6 1.0 C2D A:HEM472 4.2 62.1 1.0 C3D A:HEM472 4.2 64.8 1.0 CA A:CYS400 4.3 65.1 1.0 C3A A:HEM472 4.3 49.3 1.0 C3B A:HEM472 4.3 43.5 1.0 C2B A:HEM472 4.3 56.0 1.0 C2A A:HEM472 4.3 58.4 1.0 C3C A:HEM472 4.4 56.4 1.0 C2C A:HEM472 4.4 61.6 1.0 OG1 A:THR268 4.5 59.4 1.0 O A:ALA264 4.9 76.8 1.0

Iron binding site 2 out of 2 in the Evolved Variant of Cytochrome P450 (BM3, CYP102A1)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Evolved Variant of Cytochrome P450 (BM3, CYP102A1) within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe472 b:44.3 occ:1.00 FE B:HEM472 0.0 44.3 1.0 NA B:HEM472 2.0 64.8 1.0 ND B:HEM472 2.0 59.9 1.0 NB B:HEM472 2.1 55.4 1.0 NC B:HEM472 2.1 46.5 1.0 SG B:CYS400 2.3 47.9 1.0 C4A B:HEM472 3.0 68.2 1.0 C1A B:HEM472 3.0 68.3 1.0 C1D B:HEM472 3.1 52.6 1.0 C1B B:HEM472 3.1 61.7 1.0 C4D B:HEM472 3.1 64.6 1.0 C4C B:HEM472 3.1 47.7 1.0 C4B B:HEM472 3.1 53.4 1.0 C1C B:HEM472 3.2 42.9 1.0 CHB B:HEM472 3.4 68.2 1.0 CB B:CYS400 3.4 64.6 1.0 CHA B:HEM472 3.4 71.0 1.0 CHD B:HEM472 3.4 52.9 1.0 CHC B:HEM472 3.5 50.5 1.0 CA B:CYS400 4.1 61.3 1.0 C2A B:HEM472 4.2 69.5 1.0 C3A B:HEM472 4.2 66.8 1.0 C2D B:HEM472 4.3 49.8 1.0 C2B B:HEM472 4.3 62.9 1.0 C3B B:HEM472 4.3 55.9 1.0 C3D B:HEM472 4.3 55.9 1.0 C3C B:HEM472 4.4 46.0 1.0 C2C B:HEM472 4.4 40.1 1.0 OG1 B:THR268 4.7 58.9 1.0 C B:CYS400 4.8 61.3 1.0 N B:GLY402 4.9 63.4 1.0 N B:ILE401 4.9 64.8 1.0

A.Rentmeister, T.R.Brown, C.D.Snow, M.N.Carbone, F.H.Arnold. Engineered Bacterial Mimics of Human Drug Metabolizing Enzyme CYP2C9 Chemcatchem 2011.
ISSN: ESSN 1867-3899
DOI: 10.1002/CCTC.201000452