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Iron in PDB 4l4g: Structure of Cyanide and Camphor Bound P450CAM Mutant L358P/K178G

Enzymatic activity of Structure of Cyanide and Camphor Bound P450CAM Mutant L358P/K178G

All present enzymatic activity of Structure of Cyanide and Camphor Bound P450CAM Mutant L358P/K178G:
1.14.15.1;

Protein crystallography data

The structure of Structure of Cyanide and Camphor Bound P450CAM Mutant L358P/K178G, PDB code: 4l4g 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) 35.88 / 1.55
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 57.072, 58.790, 57.072, 90.00, 105.02, 90.00
R / Rfree (%) 17.3 / 21.2

Other elements in 4l4g:

The structure of Structure of Cyanide and Camphor Bound P450CAM Mutant L358P/K178G also contains other interesting chemical elements:

Potassium (K) 3 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Structure of Cyanide and Camphor Bound P450CAM Mutant L358P/K178G (pdb code 4l4g). 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 Cyanide and Camphor Bound P450CAM Mutant L358P/K178G, PDB code: 4l4g:

Iron binding site 1 out of 1 in 4l4g

Go back to Iron Binding Sites List in 4l4g
Iron binding site 1 out of 1 in the Structure of Cyanide and Camphor Bound P450CAM Mutant L358P/K178G


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of Cyanide and Camphor Bound P450CAM Mutant L358P/K178G within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:13.2
occ:1.00
 FE A:HEM501 0.0 13.2 1.0
C A:CYN502 2.0 14.4 1.0
NC A:HEM501 2.1 13.8 1.0
NA A:HEM501 2.1 13.2 1.0
NB A:HEM501 2.1 14.0 1.0
ND A:HEM501 2.1 13.3 1.0
SG A:CYS357 2.4 13.1 1.0
N A:CYN502 3.0 14.5 1.0
C1C A:HEM501 3.1 13.8 1.0
C4B A:HEM501 3.1 13.5 1.0
C4D A:HEM501 3.1 13.1 1.0
C1A A:HEM501 3.1 13.4 1.0
C4A A:HEM501 3.1 13.5 1.0
C1D A:HEM501 3.1 14.1 1.0
C1B A:HEM501 3.1 13.5 1.0
C4C A:HEM501 3.1 13.8 1.0
CB A:CYS357 3.4 14.1 1.0
CHC A:HEM501 3.4 13.8 1.0
CHA A:HEM501 3.5 12.9 1.0
CHD A:HEM501 3.5 13.8 1.0
CHB A:HEM501 3.5 13.6 1.0
C2C A:HEM501 4.3 14.3 1.0
C3C A:HEM501 4.3 14.5 1.0
C3D A:HEM501 4.3 13.9 1.0
C3B A:HEM501 4.3 14.2 1.0
C3A A:HEM501 4.3 13.5 1.0
C2B A:HEM501 4.3 14.3 1.0
C2A A:HEM501 4.3 13.4 1.0
CA A:CYS357 4.3 11.7 1.0
C2D A:HEM501 4.4 14.3 1.0
C5 A:CAM503 4.5 13.4 1.0
OG1 A:THR252 4.6 23.0 1.0
N A:GLY359 4.9 11.4 1.0
C9 A:CAM503 5.0 14.3 1.0
CD A:PRO358 5.0 13.2 1.0

Reference:

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
Page generated: Tue Aug 5 12:28:28 2025

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