Iron in PDB 1dt6: Structure of Mammalian Cytochrome P450 2C5

All present enzymatic activity of Structure of Mammalian Cytochrome P450 2C5:
1.14.14.1;

The structure of Structure of Mammalian Cytochrome P450 2C5, PDB code: 1dt6 was solved by P.A.Williams, J.Cosme, V.Sridhar, E.F.Johnson, D.E.Mcree, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	25.00 / 3.00
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	74.700, 132.000, 172.400, 90.00, 90.00, 90.00
R / Rfree (%)	23.8 / 31.3

The structure of Structure of Mammalian Cytochrome P450 2C5 also contains other interesting chemical elements:

Samarium

(Sm)

1 atom

The binding sites of Iron atom in the Structure of Mammalian Cytochrome P450 2C5 (pdb code 1dt6). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the Structure of Mammalian Cytochrome P450 2C5, PDB code: 1dt6:

Iron binding site 1 out of 1 in the Structure of Mammalian Cytochrome P450 2C5


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of Mammalian Cytochrome P450 2C5 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:33.7 occ:1.00 FE A:HEM501 0.0 33.7 1.0 NB A:HEM501 2.1 26.9 1.0 NA A:HEM501 2.1 32.3 1.0 NC A:HEM501 2.1 31.7 1.0 ND A:HEM501 2.1 35.1 1.0 SG A:CYS432 2.5 45.8 1.0 C1B A:HEM501 3.0 33.7 1.0 C4B A:HEM501 3.0 35.3 1.0 C4A A:HEM501 3.1 36.0 1.0 C1A A:HEM501 3.1 34.6 1.0 C1C A:HEM501 3.1 29.0 1.0 C4D A:HEM501 3.1 38.1 1.0 C1D A:HEM501 3.1 39.6 1.0 C4C A:HEM501 3.1 34.2 1.0 CHC A:HEM501 3.4 32.3 1.0 CHB A:HEM501 3.4 34.5 1.0 CHA A:HEM501 3.4 33.5 1.0 CHD A:HEM501 3.5 33.3 1.0 CB A:CYS432 3.8 41.1 1.0 C3A A:HEM501 4.3 35.3 1.0 C2A A:HEM501 4.3 35.5 1.0 C2B A:HEM501 4.3 30.6 1.0 C3B A:HEM501 4.3 33.2 1.0 C2C A:HEM501 4.3 33.5 1.0 C3D A:HEM501 4.3 44.3 1.0 C2D A:HEM501 4.3 44.8 1.0 C3C A:HEM501 4.3 38.1 1.0 CA A:CYS432 4.5 42.6 1.0 CB A:ALA294 4.6 42.0 1.0 O A:ALA294 4.6 47.5 1.0 OG1 A:THR298 4.7 48.0 1.0 N A:VAL433 4.9 39.5 1.0 C A:ALA294 4.9 50.8 1.0

P.A.Williams, J.Cosme, V.Sridhar, E.F.Johnson, D.E.Mcree. Mammalian Microsomal Cytochrome P450 Monooxygenase: Structural Adaptations For Membrane Binding and Functional Diversity. Mol.Cell V. 5 121 2000.
ISSN: ISSN 1097-2765
PubMed: 10678174
DOI: 10.1016/S1097-2765(00)80408-6