Iron in PDB 3cxv: Crystal Structure of the Cytochrome P450 CYP121 A233G Mutant From Mycobacterium Tuberculosis

The structure of Crystal Structure of the Cytochrome P450 CYP121 A233G Mutant From Mycobacterium Tuberculosis, PDB code: 3cxv 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 / 1.70
Space group	P 65 2 2
Cell size a, b, c (Å), α, β, γ (°)	77.129, 77.129, 263.340, 90.00, 90.00, 120.00
R / Rfree (%)	16.6 / 19.1

The binding sites of Iron atom in the Crystal Structure of the Cytochrome P450 CYP121 A233G Mutant From Mycobacterium Tuberculosis (pdb code 3cxv). 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 the Cytochrome P450 CYP121 A233G Mutant From Mycobacterium Tuberculosis, PDB code: 3cxv:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of the Cytochrome P450 CYP121 A233G Mutant From Mycobacterium 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 the Cytochrome P450 CYP121 A233G Mutant From Mycobacterium Tuberculosis within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe462 b:8.2 occ:0.70 FE A:HEM462 0.0 8.2 0.7 FE A:HEM462 0.1 8.1 0.3 NB A:HEM462 2.0 6.4 0.7 NB A:HEM462 2.0 7.0 0.3 NC A:HEM462 2.0 7.8 0.3 NC A:HEM462 2.0 7.6 0.7 ND A:HEM462 2.1 8.1 0.7 NA A:HEM462 2.1 6.9 0.7 NA A:HEM462 2.1 7.6 0.3 ND A:HEM462 2.1 7.3 0.3 SG A:CYS345 2.3 10.1 1.0 O A:HOH914 2.4 18.7 1.0 C1C A:HEM462 3.0 7.8 0.3 C4B A:HEM462 3.0 6.6 0.7 C4B A:HEM462 3.0 6.8 0.3 C1B A:HEM462 3.0 6.7 0.7 C1C A:HEM462 3.0 7.0 0.7 C4C A:HEM462 3.1 8.8 0.7 C1D A:HEM462 3.1 9.5 0.7 C1A A:HEM462 3.1 7.9 0.3 C4D A:HEM462 3.1 7.9 0.3 C4C A:HEM462 3.1 7.9 0.3 C1B A:HEM462 3.1 7.5 0.3 C4D A:HEM462 3.1 10.2 0.7 C1A A:HEM462 3.1 7.7 0.7 C4A A:HEM462 3.1 5.2 0.7 C1D A:HEM462 3.1 7.5 0.3 C4A A:HEM462 3.1 7.7 0.3 CHC A:HEM462 3.3 7.4 0.3 CHC A:HEM462 3.4 6.5 0.7 CHD A:HEM462 3.4 9.8 0.7 CHA A:HEM462 3.4 8.2 0.3 CB A:CYS345 3.4 9.8 1.0 CHB A:HEM462 3.4 5.3 0.7 CHA A:HEM462 3.4 8.0 0.7 CHD A:HEM462 3.5 7.4 0.3 CHB A:HEM462 3.5 8.0 0.3 O A:HOH1166 4.2 28.1 1.0 CA A:CYS345 4.2 9.8 1.0 C3B A:HEM462 4.2 5.5 0.7 C2B A:HEM462 4.2 6.4 0.7 C2C A:HEM462 4.2 7.6 0.3 C2C A:HEM462 4.2 8.7 0.7 C3B A:HEM462 4.2 7.3 0.3 C3C A:HEM462 4.2 8.3 0.7 C3C A:HEM462 4.3 7.8 0.3 C2B A:HEM462 4.3 7.0 0.3 C3D A:HEM462 4.3 7.8 0.3 C2D A:HEM462 4.3 10.3 0.7 C2A A:HEM462 4.3 7.6 0.3 C3D A:HEM462 4.3 10.1 0.7 C3A A:HEM462 4.3 7.4 0.7 C2A A:HEM462 4.3 6.0 0.7 C2D A:HEM462 4.3 8.4 0.3 C3A A:HEM462 4.3 8.1 0.3 O A:HOH998 4.4 22.0 1.0 OG A:SER237 4.5 6.9 1.0 CD A:PRO346 4.8 10.8 1.0 CB A:SER237 4.8 5.3 1.0 C A:CYS345 4.9 10.4 1.0 N A:GLY347 5.0 11.2 1.0

Iron binding site 2 out of 2 in the Crystal Structure of the Cytochrome P450 CYP121 A233G Mutant From Mycobacterium 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 the Cytochrome P450 CYP121 A233G Mutant From Mycobacterium Tuberculosis within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe462 b:8.1 occ:0.30 FE A:HEM462 0.0 8.1 0.3 FE A:HEM462 0.1 8.2 0.7 NA A:HEM462 2.0 6.9 0.7 NB A:HEM462 2.0 6.4 0.7 NC A:HEM462 2.0 7.8 0.3 ND A:HEM462 2.0 8.1 0.7 NA A:HEM462 2.1 7.6 0.3 ND A:HEM462 2.1 7.3 0.3 NB A:HEM462 2.1 7.0 0.3 NC A:HEM462 2.1 7.6 0.7 SG A:CYS345 2.3 10.1 1.0 O A:HOH914 2.4 18.7 1.0 C4D A:HEM462 3.0 7.9 0.3 C1B A:HEM462 3.0 6.7 0.7 C1A A:HEM462 3.0 7.7 0.7 C1C A:HEM462 3.0 7.8 0.3 C4B A:HEM462 3.0 6.6 0.7 C1A A:HEM462 3.0 7.9 0.3 C4A A:HEM462 3.0 5.2 0.7 C4D A:HEM462 3.0 10.2 0.7 C1D A:HEM462 3.1 9.5 0.7 C4B A:HEM462 3.1 6.8 0.3 C1D A:HEM462 3.1 7.5 0.3 C4C A:HEM462 3.1 7.9 0.3 C1C A:HEM462 3.1 7.0 0.7 C4C A:HEM462 3.1 8.8 0.7 C4A A:HEM462 3.1 7.7 0.3 C1B A:HEM462 3.1 7.5 0.3 CHC A:HEM462 3.4 7.4 0.3 CHA A:HEM462 3.4 8.2 0.3 CHA A:HEM462 3.4 8.0 0.7 CB A:CYS345 3.4 9.8 1.0 CHB A:HEM462 3.4 5.3 0.7 CHC A:HEM462 3.4 6.5 0.7 CHD A:HEM462 3.4 7.4 0.3 CHD A:HEM462 3.5 9.8 0.7 CHB A:HEM462 3.5 8.0 0.3 CA A:CYS345 4.2 9.8 1.0 O A:HOH1166 4.2 28.1 1.0 C3D A:HEM462 4.2 7.8 0.3 C2B A:HEM462 4.2 6.4 0.7 C3B A:HEM462 4.2 5.5 0.7 C2A A:HEM462 4.2 6.0 0.7 C3A A:HEM462 4.3 7.4 0.7 C2C A:HEM462 4.3 7.6 0.3 C2D A:HEM462 4.3 8.4 0.3 C2A A:HEM462 4.3 7.6 0.3 C3D A:HEM462 4.3 10.1 0.7 C3C A:HEM462 4.3 7.8 0.3 C2D A:HEM462 4.3 10.3 0.7 C2C A:HEM462 4.3 8.7 0.7 C3B A:HEM462 4.3 7.3 0.3 C3C A:HEM462 4.3 8.3 0.7 C3A A:HEM462 4.3 8.1 0.3 C2B A:HEM462 4.3 7.0 0.3 O A:HOH998 4.4 22.0 1.0 OG A:SER237 4.5 6.9 1.0 CD A:PRO346 4.8 10.8 1.0 CB A:SER237 4.9 5.3 1.0 C A:CYS345 4.9 10.4 1.0 N A:GLY347 5.0 11.2 1.0

K.J.Mclean, P.Carroll, D.G.Lewis, A.J.Dunford, H.E.Seward, R.Neeli, M.R.Cheesman, L.Marsollier, P.Douglas, W.E.Smith, I.Rosenkrands, S.T.Cole, D.Leys, T.Parish, A.W.Munro. Characterization of Active Site Structure in CYP121. A Cytochrome P450 Essential For Viability of Mycobacterium Tuberculosis H37RV. J.Biol.Chem. V. 283 33406 2008.
ISSN: ISSN 0021-9258
PubMed: 18818197
DOI: 10.1074/JBC.M802115200