Iron in PDB 4duf: Cytochrome P450 BM3H-2G9 Mri Sensor Bound to Serotonin

All present enzymatic activity of Cytochrome P450 BM3H-2G9 Mri Sensor Bound to Serotonin:
1.14.14.1;

The structure of Cytochrome P450 BM3H-2G9 Mri Sensor Bound to Serotonin, PDB code: 4duf was solved by E.M.Brustad, V.S.Lelyveld, C.D.Snow, N.Crook, F.M.Martinez, T.J.Scholl, A.Jasanoff, F.H.Arnold, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.44 / 1.80
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	79.691, 150.492, 87.707, 90.00, 90.32, 90.00
R / Rfree (%)	16.3 / 20.3

The binding sites of Iron atom in the Cytochrome P450 BM3H-2G9 Mri Sensor Bound to Serotonin (pdb code 4duf). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Cytochrome P450 BM3H-2G9 Mri Sensor Bound to Serotonin, PDB code: 4duf:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Cytochrome P450 BM3H-2G9 Mri Sensor Bound to Serotonin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Cytochrome P450 BM3H-2G9 Mri Sensor Bound to Serotonin within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe500 b:12.3 occ:1.00 FE A:HEM500 0.0 12.3 1.0 NB A:HEM500 2.0 10.5 1.0 NC A:HEM500 2.0 12.6 1.0 NA A:HEM500 2.0 14.2 1.0 ND A:HEM500 2.1 11.4 1.0 NZ A:SRO501 2.2 14.2 1.0 SG A:CYS400 2.2 13.2 1.0 C4B A:HEM500 3.0 10.6 1.0 C1B A:HEM500 3.0 10.4 1.0 C1C A:HEM500 3.1 8.8 1.0 C4C A:HEM500 3.1 9.8 1.0 C4A A:HEM500 3.1 11.2 1.0 C1A A:HEM500 3.1 8.7 1.0 C4D A:HEM500 3.1 12.1 1.0 C1D A:HEM500 3.1 11.1 1.0 CA A:SRO501 3.2 26.0 1.0 CB A:CYS400 3.3 8.9 1.0 CHD A:HEM500 3.4 11.2 1.0 CHC A:HEM500 3.4 9.8 1.0 CHB A:HEM500 3.4 9.6 1.0 CHA A:HEM500 3.4 9.1 1.0 CA A:CYS400 4.0 9.5 1.0 O A:ALA264 4.1 15.5 1.0 C3B A:HEM500 4.2 9.8 1.0 C2B A:HEM500 4.3 8.9 1.0 C3C A:HEM500 4.3 12.4 1.0 C3A A:HEM500 4.3 8.8 1.0 C2C A:HEM500 4.3 12.5 1.0 C2D A:HEM500 4.3 9.7 1.0 C3D A:HEM500 4.3 8.0 1.0 C2A A:HEM500 4.3 12.6 1.0 CB A:SRO501 4.5 27.6 1.0 C A:CYS400 4.7 9.4 1.0 N A:GLY402 4.7 12.1 1.0 CB A:ALA264 4.8 14.5 1.0 C A:ALA264 4.9 15.3 1.0 N A:ILE401 4.9 10.6 1.0 CD1 A:SRO501 4.9 31.9 1.0

Iron binding site 2 out of 4 in the Cytochrome P450 BM3H-2G9 Mri Sensor Bound to Serotonin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Cytochrome P450 BM3H-2G9 Mri Sensor Bound to Serotonin within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe500 b:11.4 occ:1.00 FE B:HEM500 0.0 11.4 1.0 NA B:HEM500 2.0 12.3 1.0 NB B:HEM500 2.0 7.7 1.0 NC B:HEM500 2.1 11.8 1.0 ND B:HEM500 2.1 8.2 1.0 NZ B:SRO501 2.3 13.1 1.0 SG B:CYS400 2.3 11.6 1.0 C4B B:HEM500 3.0 8.4 1.0 C4D B:HEM500 3.0 10.5 1.0 C4A B:HEM500 3.1 9.7 1.0 C1B B:HEM500 3.1 10.7 1.0 C1D B:HEM500 3.1 11.5 1.0 C1A B:HEM500 3.1 7.2 1.0 C4C B:HEM500 3.1 9.0 1.0 C1C B:HEM500 3.1 9.6 1.0 CA B:SRO501 3.2 28.0 1.0 CB B:CYS400 3.3 8.2 1.0 CHC B:HEM500 3.5 11.7 1.0 CHA B:HEM500 3.5 8.2 1.0 CHB B:HEM500 3.5 9.5 1.0 CHD B:HEM500 3.5 9.7 1.0 CA B:CYS400 4.0 8.5 1.0 O B:ALA264 4.1 14.1 1.0 C3B B:HEM500 4.3 9.3 1.0 C3A B:HEM500 4.3 9.1 1.0 C2D B:HEM500 4.3 8.7 1.0 C3D B:HEM500 4.3 6.5 1.0 C2B B:HEM500 4.3 9.4 1.0 C2A B:HEM500 4.3 7.5 1.0 C3C B:HEM500 4.3 11.7 1.0 C2C B:HEM500 4.3 11.2 1.0 CB B:SRO501 4.5 26.4 1.0 CB B:ALA264 4.7 15.1 1.0 C B:CYS400 4.7 9.5 1.0 N B:GLY402 4.8 9.2 1.0 CD1 B:SRO501 4.9 31.3 1.0 C B:ALA264 4.9 16.5 1.0 N B:ILE401 4.9 10.1 1.0

Iron binding site 3 out of 4 in the Cytochrome P450 BM3H-2G9 Mri Sensor Bound to Serotonin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Cytochrome P450 BM3H-2G9 Mri Sensor Bound to Serotonin within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe500 b:12.3 occ:1.00 FE C:HEM500 0.0 12.3 1.0 NA C:HEM500 2.0 10.9 1.0 NB C:HEM500 2.1 13.1 1.0 ND C:HEM500 2.1 11.1 1.0 NC C:HEM500 2.1 11.7 1.0 NZ C:SRO501 2.2 17.1 1.0 SG C:CYS400 2.3 12.8 1.0 C4A C:HEM500 3.0 10.7 1.0 C1A C:HEM500 3.0 10.8 1.0 C4B C:HEM500 3.0 13.8 1.0 C1B C:HEM500 3.1 10.9 1.0 C1D C:HEM500 3.1 13.5 1.0 C4D C:HEM500 3.1 12.1 1.0 C4C C:HEM500 3.1 12.7 1.0 C1C C:HEM500 3.1 14.1 1.0 CA C:SRO501 3.1 31.8 1.0 CB C:CYS400 3.3 8.9 1.0 CHC C:HEM500 3.5 12.8 1.0 CHD C:HEM500 3.5 11.3 1.0 CHB C:HEM500 3.5 11.2 1.0 CHA C:HEM500 3.5 9.4 1.0 CA C:CYS400 4.0 12.0 1.0 O C:ALA264 4.2 21.9 1.0 C3A C:HEM500 4.2 10.9 1.0 C3B C:HEM500 4.2 10.9 1.0 C2A C:HEM500 4.2 7.5 1.0 C3C C:HEM500 4.3 9.2 1.0 C2B C:HEM500 4.3 9.9 1.0 C2C C:HEM500 4.3 13.5 1.0 C2D C:HEM500 4.3 7.8 1.0 C3D C:HEM500 4.3 9.8 1.0 CB C:SRO501 4.5 35.7 1.0 CD1 C:SRO501 4.8 41.8 1.0 N C:GLY402 4.8 10.7 1.0 CB C:ALA264 4.8 19.9 1.0 C C:CYS400 4.8 13.0 1.0 CG C:SRO501 4.9 39.4 1.0

Iron binding site 4 out of 4 in the Cytochrome P450 BM3H-2G9 Mri Sensor Bound to Serotonin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Cytochrome P450 BM3H-2G9 Mri Sensor Bound to Serotonin within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe500 b:14.3 occ:1.00 FE D:HEM500 0.0 14.3 1.0 ND D:HEM500 2.0 11.7 1.0 NB D:HEM500 2.1 15.4 1.0 NC D:HEM500 2.1 14.6 1.0 NA D:HEM500 2.1 16.2 1.0 SG D:CYS400 2.3 14.5 1.0 NZ D:SRO501 2.3 15.1 1.0 C4D D:HEM500 3.1 14.1 1.0 C4C D:HEM500 3.1 11.9 1.0 C4B D:HEM500 3.1 15.6 1.0 C1D D:HEM500 3.1 12.7 1.0 C4A D:HEM500 3.1 13.6 1.0 C1B D:HEM500 3.1 15.1 1.0 C1A D:HEM500 3.1 12.6 1.0 C1C D:HEM500 3.1 14.0 1.0 CA D:SRO501 3.2 31.4 1.0 CB D:CYS400 3.3 10.8 1.0 CHD D:HEM500 3.4 14.4 1.0 CHC D:HEM500 3.5 16.3 1.0 CHA D:HEM500 3.5 11.6 1.0 CHB D:HEM500 3.5 15.4 1.0 CA D:CYS400 3.9 12.5 1.0 O D:ALA264 4.1 14.1 1.0 C3D D:HEM500 4.3 11.4 1.0 C3B D:HEM500 4.3 13.4 1.0 C2B D:HEM500 4.3 11.9 1.0 C3A D:HEM500 4.3 13.9 1.0 C3C D:HEM500 4.3 12.2 1.0 C2D D:HEM500 4.3 10.4 1.0 C2A D:HEM500 4.3 13.1 1.0 C2C D:HEM500 4.3 13.8 1.0 CB D:SRO501 4.6 23.4 1.0 CB D:ALA264 4.7 12.8 1.0 C D:CYS400 4.8 14.8 1.0 N D:GLY402 4.8 12.0 1.0 C D:ALA264 4.9 14.4 1.0 N D:ILE401 5.0 13.6 1.0

E.M.Brustad, V.S.Lelyveld, C.D.Snow, N.Crook, S.T.Jung, F.M.Martinez, T.J.Scholl, A.Jasanoff, F.H.Arnold. Structure-Guided Directed Evolution of Highly Selective P450-Based Magnetic Resonance Imaging Sensors For Dopamine and Serotonin. J.Mol.Biol. V. 422 245 2012.
ISSN: ISSN 0022-2836
PubMed: 22659321
DOI: 10.1016/J.JMB.2012.05.029