Iron in PDB 1z11: Crystal Structure of Human Microsomal P450 2A6 with Methoxsalen Bound

All present enzymatic activity of Crystal Structure of Human Microsomal P450 2A6 with Methoxsalen Bound:
1.14.14.1;

The structure of Crystal Structure of Human Microsomal P450 2A6 with Methoxsalen Bound, PDB code: 1z11 was solved by J.K.Yano, M.H.Hsu, K.J.Griffin, C.D.Stout, E.F.Johnson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.05
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	70.660, 159.030, 103.880, 90.00, 92.00, 90.00
R / Rfree (%)	21.9 / 26.1

The binding sites of Iron atom in the Crystal Structure of Human Microsomal P450 2A6 with Methoxsalen Bound (pdb code 1z11). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Crystal Structure of Human Microsomal P450 2A6 with Methoxsalen Bound, PDB code: 1z11:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Crystal Structure of Human Microsomal P450 2A6 with Methoxsalen Bound


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 Human Microsomal P450 2A6 with Methoxsalen Bound within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe500 b:34.6 occ:1.00 FE A:HEM500 0.0 34.6 1.0 NC A:HEM500 2.0 34.0 1.0 ND A:HEM500 2.0 34.9 1.0 NB A:HEM500 2.0 32.0 1.0 NA A:HEM500 2.1 35.0 1.0 SG A:CYS439 2.4 37.2 1.0 C1D A:HEM500 3.0 35.1 1.0 C1C A:HEM500 3.0 33.7 1.0 C4B A:HEM500 3.0 31.5 1.0 C4A A:HEM500 3.0 33.3 1.0 C4D A:HEM500 3.0 32.8 1.0 C4C A:HEM500 3.0 34.4 1.0 C1B A:HEM500 3.0 30.7 1.0 C1A A:HEM500 3.1 32.0 1.0 O2 A:8MO501 3.3 79.7 1.0 CB A:CYS439 3.3 36.5 1.0 CHC A:HEM500 3.3 32.8 1.0 CHB A:HEM500 3.3 31.5 1.0 CHD A:HEM500 3.3 31.1 1.0 CHA A:HEM500 3.4 34.3 1.0 C2 A:8MO501 3.7 80.4 1.0 CA A:CYS439 4.2 40.2 1.0 C2D A:HEM500 4.2 34.8 1.0 C2C A:HEM500 4.2 34.7 1.0 C3A A:HEM500 4.2 33.1 1.0 C3D A:HEM500 4.2 32.8 1.0 C2A A:HEM500 4.3 31.5 1.0 C3C A:HEM500 4.3 35.5 1.0 C3B A:HEM500 4.3 29.2 1.0 C2B A:HEM500 4.3 29.6 1.0 C10 A:8MO501 4.5 79.6 1.0 O3 A:8MO501 4.8 81.7 1.0 C A:CYS439 4.9 41.4 1.0 N A:GLY441 5.0 42.7 1.0

Iron binding site 2 out of 4 in the Crystal Structure of Human Microsomal P450 2A6 with Methoxsalen Bound


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 Human Microsomal P450 2A6 with Methoxsalen Bound within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe500 b:39.4 occ:1.00 FE B:HEM500 0.0 39.4 1.0 NB B:HEM500 2.0 33.7 1.0 ND B:HEM500 2.0 37.8 1.0 NA B:HEM500 2.0 36.1 1.0 NC B:HEM500 2.0 36.5 1.0 SG B:CYS439 2.4 40.5 1.0 C1D B:HEM500 3.0 37.0 1.0 C4B B:HEM500 3.0 35.7 1.0 C4D B:HEM500 3.0 36.0 1.0 C1C B:HEM500 3.0 37.2 1.0 C1B B:HEM500 3.0 36.1 1.0 C4A B:HEM500 3.0 37.5 1.0 C4C B:HEM500 3.0 37.6 1.0 C1A B:HEM500 3.0 35.2 1.0 O2 B:8MO501 3.2 80.2 1.0 CHC B:HEM500 3.3 36.0 1.0 CHD B:HEM500 3.3 38.4 1.0 CHB B:HEM500 3.3 34.5 1.0 CB B:CYS439 3.3 42.1 1.0 CHA B:HEM500 3.4 37.7 1.0 C2 B:8MO501 3.8 80.0 1.0 C2D B:HEM500 4.2 37.4 1.0 C3D B:HEM500 4.2 38.0 1.0 C2C B:HEM500 4.2 37.0 1.0 C3A B:HEM500 4.2 36.8 1.0 C3B B:HEM500 4.3 34.3 1.0 C3C B:HEM500 4.3 38.1 1.0 C2A B:HEM500 4.3 38.3 1.0 C2B B:HEM500 4.3 32.4 1.0 CA B:CYS439 4.3 44.0 1.0 C10 B:8MO501 4.5 81.4 1.0 O3 B:8MO501 4.5 85.2 1.0 N B:GLY441 4.9 46.4 1.0 C B:CYS439 5.0 44.2 1.0 C11 B:8MO501 5.0 82.5 1.0

Iron binding site 3 out of 4 in the Crystal Structure of Human Microsomal P450 2A6 with Methoxsalen Bound


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Crystal Structure of Human Microsomal P450 2A6 with Methoxsalen Bound within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe500 b:43.5 occ:1.00 FE C:HEM500 0.0 43.5 1.0 ND C:HEM500 2.0 42.6 1.0 NA C:HEM500 2.0 39.3 1.0 NC C:HEM500 2.1 41.4 1.0 NB C:HEM500 2.1 43.5 1.0 SG C:CYS439 2.3 45.0 1.0 C1D C:HEM500 3.0 43.0 1.0 C4D C:HEM500 3.0 39.8 1.0 C1C C:HEM500 3.0 42.6 1.0 C4B C:HEM500 3.0 42.5 1.0 C4A C:HEM500 3.0 41.0 1.0 C4C C:HEM500 3.0 40.7 1.0 C1B C:HEM500 3.1 42.4 1.0 C1A C:HEM500 3.1 39.7 1.0 CB C:CYS439 3.3 42.8 1.0 CHD C:HEM500 3.3 41.0 1.0 CHC C:HEM500 3.3 42.7 1.0 CHB C:HEM500 3.3 40.4 1.0 CHA C:HEM500 3.4 38.9 1.0 O2 C:8MO501 3.4 82.3 1.0 C2 C:8MO501 3.8 82.9 1.0 C2D C:HEM500 4.2 43.1 1.0 CA C:CYS439 4.2 45.7 1.0 C3D C:HEM500 4.2 40.7 1.0 C2C C:HEM500 4.2 42.4 1.0 C3C C:HEM500 4.3 41.0 1.0 C3B C:HEM500 4.3 42.1 1.0 C3A C:HEM500 4.3 38.8 1.0 C2A C:HEM500 4.3 39.1 1.0 C2B C:HEM500 4.3 41.5 1.0 C10 C:8MO501 4.7 82.9 1.0 N C:GLY441 4.9 51.3 1.0 C C:CYS439 5.0 45.1 1.0

Iron binding site 4 out of 4 in the Crystal Structure of Human Microsomal P450 2A6 with Methoxsalen Bound


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Crystal Structure of Human Microsomal P450 2A6 with Methoxsalen Bound within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe500 b:44.0 occ:1.00 FE D:HEM500 0.0 44.0 1.0 ND D:HEM500 2.0 41.5 1.0 NB D:HEM500 2.0 43.5 1.0 NA D:HEM500 2.1 41.5 1.0 NC D:HEM500 2.1 44.7 1.0 SG D:CYS439 2.4 44.0 1.0 C1D D:HEM500 3.0 42.7 1.0 C4B D:HEM500 3.0 42.8 1.0 C1C D:HEM500 3.0 44.2 1.0 C4D D:HEM500 3.0 42.2 1.0 C1B D:HEM500 3.0 43.5 1.0 C4C D:HEM500 3.0 42.3 1.0 C4A D:HEM500 3.0 41.0 1.0 C1A D:HEM500 3.1 40.9 1.0 CHD D:HEM500 3.3 44.6 1.0 CHC D:HEM500 3.3 43.1 1.0 CB D:CYS439 3.3 44.9 1.0 CHB D:HEM500 3.3 42.9 1.0 CHA D:HEM500 3.4 40.2 1.0 O2 D:8MO501 3.4 91.8 1.0 C2 D:8MO501 4.0 92.1 1.0 C2D D:HEM500 4.2 41.7 1.0 C2C D:HEM500 4.2 42.6 1.0 C3D D:HEM500 4.2 41.5 1.0 C3C D:HEM500 4.2 43.7 1.0 C3B D:HEM500 4.2 42.8 1.0 CA D:CYS439 4.3 45.4 1.0 C2B D:HEM500 4.3 42.8 1.0 C3A D:HEM500 4.3 40.0 1.0 C2A D:HEM500 4.3 40.8 1.0 C10 D:8MO501 4.7 92.4 1.0 O3 D:8MO501 4.8 94.2 1.0 N D:GLY441 5.0 47.8 1.0

J.K.Yano, M.H.Hsu, K.J.Griffin, C.D.Stout, E.F.Johnson. Structures of Human Microsomal Cytochrome P450 2A6 Complexed with Coumarin and Methoxsalen Nat.Struct.Mol.Biol. V. 12 822 2005.
ISSN: ISSN 1545-9993
PubMed: 16086027
DOI: 10.1038/NSMB971