Iron in PDB 5wk7: P450CAM Mutant R186A

All present enzymatic activity of P450CAM Mutant R186A:
1.14.15.1;

The structure of P450CAM Mutant R186A, PDB code: 5wk7 was solved by D.Batabyal, T.L.Poulos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.24 / 1.98
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	56.820, 58.420, 57.250, 90.00, 104.97, 90.00
R / Rfree (%)	16.3 / 21.5

The structure of P450CAM Mutant R186A also contains other interesting chemical elements:

Potassium

(K)

1 atom

The binding sites of Iron atom in the P450CAM Mutant R186A (pdb code 5wk7). 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 P450CAM Mutant R186A, PDB code: 5wk7:

Iron binding site 1 out of 1 in the P450CAM Mutant R186A


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of P450CAM Mutant R186A within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:23.9 occ:1.00 FE A:HEM501 0.0 23.9 1.0 NC A:HEM501 2.0 21.9 1.0 NA A:HEM501 2.0 18.8 1.0 NB A:HEM501 2.1 26.7 1.0 ND A:HEM501 2.1 20.5 1.0 SG A:CYS357 2.5 23.9 1.0 C1C A:HEM501 3.0 21.1 1.0 O5 A:CAH502 3.0 52.2 1.0 C4D A:HEM501 3.1 22.2 1.0 C1A A:HEM501 3.1 17.9 1.0 C4B A:HEM501 3.1 20.3 1.0 C4A A:HEM501 3.1 18.5 1.0 C1D A:HEM501 3.1 26.1 1.0 C1B A:HEM501 3.1 24.4 1.0 C4C A:HEM501 3.1 20.9 1.0 CHC A:HEM501 3.4 19.1 1.0 CHA A:HEM501 3.4 15.5 1.0 CB A:CYS357 3.4 22.0 1.0 CHB A:HEM501 3.5 20.3 1.0 CHD A:HEM501 3.5 19.2 1.0 CA A:CYS357 4.1 20.4 1.0 O A:HOH602 4.2 35.3 0.7 C2C A:HEM501 4.3 17.3 1.0 C5 A:CAH502 4.3 40.5 1.0 C3B A:HEM501 4.3 25.1 1.0 C3A A:HEM501 4.3 20.7 1.0 C2B A:HEM501 4.3 20.6 1.0 C3C A:HEM501 4.3 19.2 1.0 C2A A:HEM501 4.3 17.4 1.0 C3D A:HEM501 4.3 26.4 1.0 C2D A:HEM501 4.3 22.3 1.0 N A:GLY359 4.6 23.0 1.0 C4 A:CAH502 4.7 37.6 1.0 N A:LEU358 4.7 23.1 1.0 C A:CYS357 4.8 19.7 1.0 C9 A:CAH502 4.8 37.5 1.0

D.Batabyal, L.S.Richards, T.L.Poulos. Effect of Redox Partner Binding on Cytochrome P450 Conformational Dynamics. J. Am. Chem. Soc. V. 139 13193 2017.
ISSN: ESSN 1520-5126
PubMed: 28823160
DOI: 10.1021/JACS.7B07656