Iron in PDB 4l4a: Structure of L358A/K178G Mutant of P450CAM Bound to Camphor

All present enzymatic activity of Structure of L358A/K178G Mutant of P450CAM Bound to Camphor:
1.14.15.1;

The structure of Structure of L358A/K178G Mutant of P450CAM Bound to Camphor, PDB code: 4l4a was solved by D.Batabyal, H.Li, T.L.Poulos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.78 / 2.10
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	36.436, 103.401, 105.813, 90.00, 90.00, 90.00
R / Rfree (%)	17 / 23.1

The structure of Structure of L358A/K178G Mutant of P450CAM Bound to Camphor also contains other interesting chemical elements:

Potassium

(K)

2 atoms

The binding sites of Iron atom in the Structure of L358A/K178G Mutant of P450CAM Bound to Camphor (pdb code 4l4a). 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 L358A/K178G Mutant of P450CAM Bound to Camphor, PDB code: 4l4a:

Iron binding site 1 out of 1 in the Structure of L358A/K178G Mutant of P450CAM Bound to Camphor


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of L358A/K178G Mutant of P450CAM Bound to Camphor within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:17.4 occ:1.00 FE A:HEM501 0.0 17.4 1.0 NC A:HEM501 2.0 18.0 1.0 NA A:HEM501 2.1 8.9 1.0 NB A:HEM501 2.1 9.7 1.0 ND A:HEM501 2.1 10.7 1.0 SG A:CYS357 2.5 15.4 1.0 C1C A:HEM501 3.1 20.1 1.0 C4C A:HEM501 3.1 15.6 1.0 C4B A:HEM501 3.1 9.5 1.0 C1D A:HEM501 3.1 10.9 1.0 C4A A:HEM501 3.1 12.6 1.0 C1B A:HEM501 3.1 12.4 1.0 C1A A:HEM501 3.1 9.8 1.0 C4D A:HEM501 3.1 12.7 1.0 CB A:CYS357 3.4 23.4 1.0 CHC A:HEM501 3.4 13.8 1.0 CHD A:HEM501 3.4 17.8 1.0 CHA A:HEM501 3.5 9.5 1.0 CHB A:HEM501 3.5 10.8 1.0 C5 A:CAM502 4.0 17.8 1.0 CA A:CYS357 4.1 18.2 1.0 C2C A:HEM501 4.3 16.7 1.0 C3C A:HEM501 4.3 19.4 1.0 C3B A:HEM501 4.3 11.3 1.0 C2B A:HEM501 4.3 13.5 1.0 C3A A:HEM501 4.3 13.1 1.0 C2A A:HEM501 4.3 9.5 1.0 C2D A:HEM501 4.3 15.9 1.0 C3D A:HEM501 4.3 15.2 1.0 N A:GLY359 4.6 17.9 1.0 C4 A:CAM502 4.6 18.9 1.0 N A:ALA358 4.7 21.2 1.0 C A:CYS357 4.7 17.2 1.0 C9 A:CAM502 5.0 16.8 1.0

D.Batabyal, H.Li, T.L.Poulos. Synergistic Effects of Mutations in Cytochrome P450CAM Designed to Mimic CYP101D1. Biochemistry V. 52 5396 2013.
ISSN: ISSN 0006-2960
PubMed: 23865948
DOI: 10.1021/BI400676D