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Iron in PDB 3tk3: Cytochrome P450 2B4 Mutant L437A in Complex with 4-(4-Chlorophenyl) Imidazole

Enzymatic activity of Cytochrome P450 2B4 Mutant L437A in Complex with 4-(4-Chlorophenyl) Imidazole

All present enzymatic activity of Cytochrome P450 2B4 Mutant L437A in Complex with 4-(4-Chlorophenyl) Imidazole:
1.14.14.1;

Protein crystallography data

The structure of Cytochrome P450 2B4 Mutant L437A in Complex with 4-(4-Chlorophenyl) Imidazole, PDB code: 3tk3 was solved by S.C.Gay, H.H.Jang, P.R.Wilderman, Q.Zhang, C.D.Stout, J.R.Halpert, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.43 / 2.80
Space group P 3
Cell size a, b, c (Å), α, β, γ (°) 232.910, 232.910, 56.960, 90.00, 90.00, 120.00
R / Rfree (%) 19.3 / 24.1

Other elements in 3tk3:

The structure of Cytochrome P450 2B4 Mutant L437A in Complex with 4-(4-Chlorophenyl) Imidazole also contains other interesting chemical elements:

Chlorine (Cl) 4 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Cytochrome P450 2B4 Mutant L437A in Complex with 4-(4-Chlorophenyl) Imidazole (pdb code 3tk3). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Cytochrome P450 2B4 Mutant L437A in Complex with 4-(4-Chlorophenyl) Imidazole, PDB code: 3tk3:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 3tk3

Go back to Iron Binding Sites List in 3tk3
Iron binding site 1 out of 4 in the Cytochrome P450 2B4 Mutant L437A in Complex with 4-(4-Chlorophenyl) Imidazole


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Cytochrome P450 2B4 Mutant L437A in Complex with 4-(4-Chlorophenyl) Imidazole within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe500

b:35.4
occ:1.00
 FE A:HEM500 0.0 35.4 1.0
N1 A:CPZ501 1.9 39.1 1.0
NC A:HEM500 2.0 39.9 1.0
NA A:HEM500 2.0 41.5 1.0
NB A:HEM500 2.1 41.9 1.0
ND A:HEM500 2.1 45.2 1.0
SG A:CYS436 2.3 34.9 1.0
C5 A:CPZ501 2.8 41.9 1.0
C4A A:HEM500 3.0 42.3 1.0
C4C A:HEM500 3.0 43.4 1.0
C1B A:HEM500 3.0 44.0 1.0
C2 A:CPZ501 3.0 41.4 1.0
C1C A:HEM500 3.1 43.3 1.0
C1A A:HEM500 3.1 43.3 1.0
C1D A:HEM500 3.1 41.5 1.0
C4B A:HEM500 3.1 37.4 1.0
C4D A:HEM500 3.2 44.5 1.0
CB A:CYS436 3.3 38.3 1.0
CHB A:HEM500 3.4 44.9 1.0
CHD A:HEM500 3.4 39.1 1.0
CHC A:HEM500 3.5 44.5 1.0
CHA A:HEM500 3.5 44.5 1.0
N3 A:CPZ501 4.1 44.5 1.0
C4 A:CPZ501 4.1 44.3 1.0
CA A:CYS436 4.2 42.0 1.0
C3A A:HEM500 4.2 42.8 1.0
C3C A:HEM500 4.2 44.3 1.0
C2B A:HEM500 4.3 40.4 1.0
C2C A:HEM500 4.3 37.4 1.0
C2A A:HEM500 4.3 40.8 1.0
C3B A:HEM500 4.3 42.0 1.0
C2D A:HEM500 4.4 37.8 1.0
C3D A:HEM500 4.4 42.4 1.0
CB A:ALA298 4.7 44.1 1.0
N A:GLY438 4.9 43.9 1.0
C A:CYS436 4.9 42.2 1.0

Iron binding site 2 out of 4 in 3tk3

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Iron binding site 2 out of 4 in the Cytochrome P450 2B4 Mutant L437A in Complex with 4-(4-Chlorophenyl) Imidazole


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Cytochrome P450 2B4 Mutant L437A in Complex with 4-(4-Chlorophenyl) Imidazole within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe500

b:36.5
occ:1.00
 FE B:HEM500 0.0 36.5 1.0
NA B:HEM500 2.0 38.4 1.0
N1 B:CPZ501 2.0 35.1 1.0
NC B:HEM500 2.0 42.6 1.0
NB B:HEM500 2.0 40.2 1.0
ND B:HEM500 2.1 43.1 1.0
SG B:CYS436 2.3 35.4 1.0
C2 B:CPZ501 3.0 38.0 1.0
C4A B:HEM500 3.0 39.6 1.0
C1A B:HEM500 3.0 39.7 1.0
C4C B:HEM500 3.0 45.0 1.0
C1B B:HEM500 3.0 41.1 1.0
C5 B:CPZ501 3.1 42.3 1.0
C1C B:HEM500 3.1 43.7 1.0
C4B B:HEM500 3.1 39.4 1.0
C4D B:HEM500 3.1 43.8 1.0
C1D B:HEM500 3.1 41.2 1.0
CB B:CYS436 3.2 37.4 1.0
CHB B:HEM500 3.4 44.2 1.0
CHA B:HEM500 3.4 39.9 1.0
CHD B:HEM500 3.4 40.4 1.0
CHC B:HEM500 3.5 39.8 1.0
CA B:CYS436 4.1 41.5 1.0
C4 B:CPZ501 4.2 38.5 1.0
N3 B:CPZ501 4.2 43.9 1.0
C3A B:HEM500 4.2 41.7 1.0
C2A B:HEM500 4.2 43.0 1.0
C3C B:HEM500 4.3 44.0 1.0
C2C B:HEM500 4.3 44.8 1.0
C2B B:HEM500 4.3 40.4 1.0
C3B B:HEM500 4.3 40.2 1.0
C3D B:HEM500 4.3 41.2 1.0
C2D B:HEM500 4.4 41.3 1.0
CB B:ALA298 4.5 37.1 1.0
N B:GLY438 4.9 42.0 1.0
C B:CYS436 4.9 43.5 1.0
N B:ALA437 4.9 40.6 1.0

Iron binding site 3 out of 4 in 3tk3

Go back to Iron Binding Sites List in 3tk3
Iron binding site 3 out of 4 in the Cytochrome P450 2B4 Mutant L437A in Complex with 4-(4-Chlorophenyl) Imidazole


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Cytochrome P450 2B4 Mutant L437A in Complex with 4-(4-Chlorophenyl) Imidazole within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe500

b:34.6
occ:1.00
 FE C:HEM500 0.0 34.6 1.0
NA C:HEM500 2.0 37.8 1.0
N1 C:CPZ501 2.0 35.5 1.0
NC C:HEM500 2.0 39.5 1.0
NB C:HEM500 2.1 36.2 1.0
ND C:HEM500 2.1 38.7 1.0
SG C:CYS436 2.2 34.5 1.0
C4A C:HEM500 3.0 37.2 1.0
C4C C:HEM500 3.0 41.8 1.0
C2 C:CPZ501 3.0 38.8 1.0
C1A C:HEM500 3.0 38.5 1.0
C5 C:CPZ501 3.0 41.5 1.0
C1C C:HEM500 3.1 44.1 1.0
C1B C:HEM500 3.1 36.0 1.0
C1D C:HEM500 3.1 37.8 1.0
C4D C:HEM500 3.1 40.2 1.0
C4B C:HEM500 3.1 34.5 1.0
CB C:CYS436 3.4 37.4 1.0
CHD C:HEM500 3.4 39.5 1.0
CHB C:HEM500 3.4 38.4 1.0
CHA C:HEM500 3.4 39.4 1.0
CHC C:HEM500 3.5 41.1 1.0
C4 C:CPZ501 4.2 41.3 1.0
CA C:CYS436 4.2 39.5 1.0
N3 C:CPZ501 4.2 41.1 1.0
C3A C:HEM500 4.2 36.1 1.0
C2A C:HEM500 4.2 40.2 1.0
C3C C:HEM500 4.2 44.8 1.0
C2C C:HEM500 4.3 40.8 1.0
C2B C:HEM500 4.3 39.2 1.0
C3B C:HEM500 4.3 39.2 1.0
C2D C:HEM500 4.3 41.0 1.0
C3D C:HEM500 4.3 39.8 1.0
CB C:ALA298 4.7 43.0 1.0
N C:GLY438 4.8 38.1 1.0
N C:ALA437 4.8 41.3 1.0
C C:CYS436 4.9 42.6 1.0

Iron binding site 4 out of 4 in 3tk3

Go back to Iron Binding Sites List in 3tk3
Iron binding site 4 out of 4 in the Cytochrome P450 2B4 Mutant L437A in Complex with 4-(4-Chlorophenyl) Imidazole


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Cytochrome P450 2B4 Mutant L437A in Complex with 4-(4-Chlorophenyl) Imidazole within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe500

b:39.9
occ:1.00
 FE D:HEM500 0.0 39.9 1.0
N1 D:CPZ501 1.9 38.7 1.0
NA D:HEM500 2.0 40.0 1.0
NB D:HEM500 2.0 42.2 1.0
NC D:HEM500 2.1 44.9 1.0
ND D:HEM500 2.2 45.9 1.0
SG D:CYS436 2.2 32.7 1.0
C5 D:CPZ501 2.9 42.2 1.0
C4A D:HEM500 3.0 39.7 1.0
C1B D:HEM500 3.0 39.9 1.0
C2 D:CPZ501 3.0 36.5 1.0
C1A D:HEM500 3.0 41.6 1.0
C4B D:HEM500 3.0 42.9 1.0
C1C D:HEM500 3.1 45.6 1.0
C4C D:HEM500 3.1 47.9 1.0
C4D D:HEM500 3.1 44.8 1.0
C1D D:HEM500 3.2 42.3 1.0
CB D:CYS436 3.3 37.0 1.0
CHB D:HEM500 3.4 39.7 1.0
CHC D:HEM500 3.4 45.8 1.0
CHA D:HEM500 3.4 42.6 1.0
CHD D:HEM500 3.5 43.3 1.0
N3 D:CPZ501 4.1 42.7 1.0
C4 D:CPZ501 4.1 40.1 1.0
C3A D:HEM500 4.2 40.1 1.0
CA D:CYS436 4.2 38.5 1.0
C2B D:HEM500 4.2 42.5 1.0
C2A D:HEM500 4.2 46.3 1.0
C3B D:HEM500 4.2 41.7 1.0
C2C D:HEM500 4.3 42.5 1.0
C3C D:HEM500 4.3 46.7 1.0
C3D D:HEM500 4.4 40.9 1.0
C2D D:HEM500 4.4 40.8 1.0
CB D:ALA298 4.6 46.3 1.0
N D:GLY438 4.8 43.7 1.0
C D:CYS436 4.9 42.5 1.0

Reference:

P.R.Wilderman, S.C.Gay, H.H.Jang, Q.Zhang, C.D.Stout, J.R.Halpert. Investigation By Site-Directed Mutagenesis of the Role of Cytochrome P450 2B4 Non-Active-Site Residues in Protein-Ligand Interactions Based on Crystal Structures of the Ligand-Bound Enzyme. Febs J. V. 279 1607 2012.
ISSN: ISSN 1742-464X
PubMed: 22051155
DOI: 10.1111/J.1742-4658.2011.08411.X
Page generated: Sun Dec 13 15:22:15 2020

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