Iron in PDB 3fwg: Ferric Camphor Bound Cytochrome P450CAM, ARG365LEU, GLU366GLN, Monoclinic Crystal Form

All present enzymatic activity of Ferric Camphor Bound Cytochrome P450CAM, ARG365LEU, GLU366GLN, Monoclinic Crystal Form:
1.14.15.1;

The structure of Ferric Camphor Bound Cytochrome P450CAM, ARG365LEU, GLU366GLN, Monoclinic Crystal Form, PDB code: 3fwg was solved by I.Schlichting, K.Von Koenig, C.Aldag, D.Hilvert, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.13 / 1.55
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	67.180, 62.795, 95.605, 90.00, 90.53, 90.00
R / Rfree (%)	18.5 / 21.7

The structure of Ferric Camphor Bound Cytochrome P450CAM, ARG365LEU, GLU366GLN, Monoclinic Crystal Form also contains other interesting chemical elements:

Potassium

(K)

3 atoms

The binding sites of Iron atom in the Ferric Camphor Bound Cytochrome P450CAM, ARG365LEU, GLU366GLN, Monoclinic Crystal Form (pdb code 3fwg). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Ferric Camphor Bound Cytochrome P450CAM, ARG365LEU, GLU366GLN, Monoclinic Crystal Form, PDB code: 3fwg:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Ferric Camphor Bound Cytochrome P450CAM, ARG365LEU, GLU366GLN, Monoclinic Crystal Form


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Ferric Camphor Bound Cytochrome P450CAM, ARG365LEU, GLU366GLN, Monoclinic Crystal Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe417 b:13.8 occ:1.00 FE A:HEM417 0.0 13.8 1.0 NC A:HEM417 2.0 12.8 1.0 NA A:HEM417 2.0 13.2 1.0 ND A:HEM417 2.1 12.1 1.0 NB A:HEM417 2.1 12.4 1.0 SG A:CYS357 2.4 14.6 1.0 C1C A:HEM417 3.0 13.9 1.0 C4B A:HEM417 3.1 14.5 1.0 C1D A:HEM417 3.1 13.8 1.0 C1A A:HEM417 3.1 14.2 1.0 C4A A:HEM417 3.1 14.0 1.0 C4C A:HEM417 3.1 14.0 1.0 C1B A:HEM417 3.1 13.0 1.0 C4D A:HEM417 3.1 14.0 1.0 CB A:CYS357 3.4 14.6 1.0 CHC A:HEM417 3.4 14.3 1.0 CHD A:HEM417 3.4 14.9 1.0 CHA A:HEM417 3.5 14.0 1.0 CHB A:HEM417 3.5 14.1 1.0 CA A:CYS357 4.0 15.5 1.0 C5 A:CAM420 4.1 19.1 1.0 C2C A:HEM417 4.3 14.9 1.0 C3B A:HEM417 4.3 14.6 1.0 C3A A:HEM417 4.3 14.5 1.0 C3C A:HEM417 4.3 15.8 1.0 C2B A:HEM417 4.3 13.7 1.0 C2A A:HEM417 4.3 14.4 1.0 C2D A:HEM417 4.3 15.2 1.0 C3D A:HEM417 4.3 15.5 1.0 N A:GLY359 4.5 15.7 1.0 C4 A:CAM420 4.6 19.4 1.0 N A:LEU358 4.6 15.5 1.0 C A:CYS357 4.7 15.7 1.0 C9 A:CAM420 4.7 17.6 1.0 CA A:GLY359 4.8 15.1 1.0

Iron binding site 2 out of 2 in the Ferric Camphor Bound Cytochrome P450CAM, ARG365LEU, GLU366GLN, Monoclinic Crystal Form


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Ferric Camphor Bound Cytochrome P450CAM, ARG365LEU, GLU366GLN, Monoclinic Crystal Form within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe417 b:10.5 occ:1.00 FE B:HEM417 0.0 10.5 1.0 NC B:HEM417 2.0 11.4 1.0 NA B:HEM417 2.1 10.3 1.0 NB B:HEM417 2.1 10.4 1.0 ND B:HEM417 2.1 8.7 1.0 SG B:CYS357 2.3 11.2 1.0 C1C B:HEM417 3.0 11.3 1.0 C4B B:HEM417 3.1 10.3 1.0 C1B B:HEM417 3.1 9.4 1.0 C4C B:HEM417 3.1 11.6 1.0 C4D B:HEM417 3.1 9.4 1.0 C1D B:HEM417 3.1 9.5 1.0 C1A B:HEM417 3.1 8.1 1.0 C4A B:HEM417 3.1 8.4 1.0 CHC B:HEM417 3.4 11.2 1.0 CB B:CYS357 3.4 11.5 1.0 CHB B:HEM417 3.4 10.6 1.0 CHA B:HEM417 3.4 9.0 1.0 CHD B:HEM417 3.5 12.8 1.0 CA B:CYS357 4.0 11.9 1.0 C5 B:CAM420 4.1 13.7 1.0 C2C B:HEM417 4.3 13.8 1.0 C3B B:HEM417 4.3 10.0 1.0 C2B B:HEM417 4.3 9.6 1.0 C3C B:HEM417 4.3 13.6 1.0 C3A B:HEM417 4.3 9.2 1.0 C3D B:HEM417 4.3 10.8 1.0 C2A B:HEM417 4.3 8.7 1.0 C2D B:HEM417 4.3 11.2 1.0 N B:GLY359 4.4 14.0 1.0 C4 B:CAM420 4.6 12.7 1.0 N B:LEU358 4.6 12.8 1.0 C B:CYS357 4.7 12.6 1.0 C9 B:CAM420 4.8 14.4 1.0 CA B:GLY359 4.8 14.9 1.0

C.Aldag, I.A.Gromov, I.Garcia-Rubio, K.Von Koenig, I.Schlichting, B.Jaun, D.Hilvert. Probing the Role of the Proximal Heme Ligand in Cytochrome P450CAM By Recombinant Incorporation of Selenocysteine. Proc.Natl.Acad.Sci.Usa V. 106 5481 2009.
ISSN: ISSN 0027-8424
PubMed: 19293375
DOI: 10.1073/PNAS.0810503106