Iron in PDB 3cxx: Crystal Structure of Cytochrome P450 CYP121 F338H From M. Tuberculosis

The structure of Crystal Structure of Cytochrome P450 CYP121 F338H From M. Tuberculosis, PDB code: 3cxx was solved by D.Leys, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	66.82 / 1.90
Space group	P 65 2 2
Cell size a, b, c (Å), α, β, γ (°)	77.226, 77.226, 263.253, 90.00, 90.00, 120.00
R / Rfree (%)	17.4 / 21.7

The binding sites of Iron atom in the Crystal Structure of Cytochrome P450 CYP121 F338H From M. Tuberculosis (pdb code 3cxx). 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 P450 CYP121 F338H From M. Tuberculosis, PDB code: 3cxx:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of Cytochrome P450 CYP121 F338H From M. Tuberculosis


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 P450 CYP121 F338H From M. Tuberculosis within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe462 b:20.9 occ:0.70 FE A:HEM462 0.0 20.9 0.7 FE A:HEM462 0.5 19.7 0.3 ND A:HEM462 1.6 20.0 0.3 NA A:HEM462 2.0 19.6 0.7 NB A:HEM462 2.1 19.3 0.7 ND A:HEM462 2.1 19.6 0.7 NC A:HEM462 2.1 18.2 0.7 NA A:HEM462 2.1 19.4 0.3 NC A:HEM462 2.1 19.1 0.3 SG A:CYS345 2.3 25.6 1.0 NB A:HEM462 2.5 19.9 0.3 O A:HOH945 2.5 31.4 1.0 C4D A:HEM462 2.6 18.6 0.3 C1D A:HEM462 2.7 19.0 0.3 C1A A:HEM462 2.9 19.8 0.3 C4C A:HEM462 3.0 18.4 0.3 C1B A:HEM462 3.0 18.5 0.7 C4A A:HEM462 3.0 19.1 0.7 C1A A:HEM462 3.0 19.5 0.7 C4D A:HEM462 3.1 21.3 0.7 C1D A:HEM462 3.1 20.6 0.7 CHA A:HEM462 3.1 19.0 0.3 C4C A:HEM462 3.1 20.2 0.7 C1C A:HEM462 3.1 18.1 0.7 C4B A:HEM462 3.1 17.4 0.7 CHD A:HEM462 3.2 18.7 0.3 C1C A:HEM462 3.3 17.7 0.3 C4A A:HEM462 3.3 19.7 0.3 CB A:CYS345 3.3 24.1 1.0 CHB A:HEM462 3.4 18.8 0.7 CHA A:HEM462 3.4 19.8 0.7 C4B A:HEM462 3.5 19.0 0.3 CHD A:HEM462 3.5 18.4 0.7 C1B A:HEM462 3.5 19.1 0.3 CHC A:HEM462 3.5 17.7 0.7 CHC A:HEM462 3.8 18.3 0.3 CHB A:HEM462 3.8 18.8 0.3 C3D A:HEM462 3.8 18.7 0.3 C2D A:HEM462 3.9 18.6 0.3 CA A:CYS345 4.1 24.9 1.0 O A:HOH1071 4.2 36.6 1.0 C2A A:HEM462 4.2 20.3 0.3 C3A A:HEM462 4.2 19.7 0.7 C2B A:HEM462 4.3 18.3 0.7 C2A A:HEM462 4.3 19.1 0.7 C3C A:HEM462 4.3 18.5 0.3 C3D A:HEM462 4.3 22.3 0.7 C2D A:HEM462 4.3 20.9 0.7 C2C A:HEM462 4.3 19.3 0.7 C3B A:HEM462 4.3 18.0 0.7 C3C A:HEM462 4.3 20.4 0.7 C3A A:HEM462 4.4 20.0 0.3 C2C A:HEM462 4.4 18.0 0.3 OG A:SER237 4.5 18.1 1.0 C3B A:HEM462 4.6 19.8 0.3 C2B A:HEM462 4.6 20.1 0.3 CB A:SER237 4.8 17.4 1.0 C A:CYS345 4.9 25.7 1.0 CD A:PRO346 4.9 27.0 1.0 N A:GLY347 4.9 26.6 1.0 CD2 A:HIS338 5.0 25.6 1.0

Iron binding site 2 out of 2 in the Crystal Structure of Cytochrome P450 CYP121 F338H From M. Tuberculosis


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 P450 CYP121 F338H From M. Tuberculosis within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe462 b:19.7 occ:0.30 FE A:HEM462 0.0 19.7 0.3 FE A:HEM462 0.5 20.9 0.7 NC A:HEM462 1.6 18.2 0.7 NB A:HEM462 2.0 19.9 0.3 NA A:HEM462 2.1 19.4 0.3 NC A:HEM462 2.1 19.1 0.3 ND A:HEM462 2.1 19.6 0.7 ND A:HEM462 2.1 20.0 0.3 NB A:HEM462 2.1 19.3 0.7 SG A:CYS345 2.4 25.6 1.0 NA A:HEM462 2.5 19.6 0.7 O A:HOH945 2.5 31.4 1.0 C4C A:HEM462 2.6 20.2 0.7 C1C A:HEM462 2.7 18.1 0.7 C1D A:HEM462 2.9 20.6 0.7 C4B A:HEM462 3.0 17.4 0.7 C4B A:HEM462 3.0 19.0 0.3 C1B A:HEM462 3.0 19.1 0.3 C1A A:HEM462 3.0 19.8 0.3 C4A A:HEM462 3.1 19.7 0.3 C1C A:HEM462 3.1 17.7 0.3 C4D A:HEM462 3.1 18.6 0.3 CHD A:HEM462 3.1 18.4 0.7 C4C A:HEM462 3.1 18.4 0.3 C1D A:HEM462 3.1 19.0 0.3 CHC A:HEM462 3.2 17.7 0.7 C1B A:HEM462 3.2 18.5 0.7 C4D A:HEM462 3.2 21.3 0.7 CHA A:HEM462 3.4 19.0 0.3 CHC A:HEM462 3.4 18.3 0.3 CHB A:HEM462 3.4 18.8 0.3 C4A A:HEM462 3.5 19.1 0.7 CHD A:HEM462 3.5 18.7 0.3 C1A A:HEM462 3.5 19.5 0.7 CB A:CYS345 3.6 24.1 1.0 CHB A:HEM462 3.7 18.8 0.7 CHA A:HEM462 3.8 19.8 0.7 C3C A:HEM462 3.8 20.4 0.7 C2C A:HEM462 3.9 19.3 0.7 C3B A:HEM462 4.2 19.8 0.3 C2B A:HEM462 4.2 20.1 0.3 C2D A:HEM462 4.2 20.9 0.7 C2A A:HEM462 4.3 20.3 0.3 C3A A:HEM462 4.3 20.0 0.3 C3B A:HEM462 4.3 18.0 0.7 C2C A:HEM462 4.3 18.0 0.3 C3D A:HEM462 4.3 18.7 0.3 C3C A:HEM462 4.3 18.5 0.3 C2D A:HEM462 4.3 18.6 0.3 C2B A:HEM462 4.4 18.3 0.7 OG A:SER237 4.4 18.1 1.0 CA A:CYS345 4.4 24.9 1.0 C3D A:HEM462 4.4 22.3 0.7 O A:HOH1071 4.4 36.6 1.0 CB A:SER237 4.6 17.4 1.0 C3A A:HEM462 4.7 19.7 0.7 C2A A:HEM462 4.7 19.1 0.7 N A:GLY347 4.8 26.6 1.0 CD A:PRO346 4.9 27.0 1.0

K.J.Mclean, P.Carrol, D.G.Lewis, A.J.Dunford, H.E.Seward, R.Neeli, S.T.Cole, D.Leys, T.Parish, A.W.Munro. Characterization of the Active Site Structure of CY121 To Be Published.