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Iron in PDB 4l4b: Structure of L358A/K178G/D182N Mutant of P450CAM Bound to Camphor

Enzymatic activity of Structure of L358A/K178G/D182N Mutant of P450CAM Bound to Camphor

All present enzymatic activity of Structure of L358A/K178G/D182N Mutant of P450CAM Bound to Camphor:
1.14.15.1;

Protein crystallography data

The structure of Structure of L358A/K178G/D182N Mutant of P450CAM Bound to Camphor, PDB code: 4l4b 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) 34.51 / 2.10
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 36.503, 103.587, 105.843, 90.00, 90.00, 90.00
R / Rfree (%) 17.6 / 23.5

Other elements in 4l4b:

The structure of Structure of L358A/K178G/D182N Mutant of P450CAM Bound to Camphor also contains other interesting chemical elements:

Potassium (K) 2 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Structure of L358A/K178G/D182N Mutant of P450CAM Bound to Camphor (pdb code 4l4b). 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/D182N Mutant of P450CAM Bound to Camphor, PDB code: 4l4b:

Iron binding site 1 out of 1 in 4l4b

Go back to Iron Binding Sites List in 4l4b
Iron binding site 1 out of 1 in the Structure of L358A/K178G/D182N 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/D182N Mutant of P450CAM Bound to Camphor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:18.7
occ:1.00
 FE A:HEM501 0.0 18.7 1.0
NB A:HEM501 2.1 13.1 1.0
ND A:HEM501 2.1 16.8 1.0
NA A:HEM501 2.1 11.9 1.0
NC A:HEM501 2.1 19.3 1.0
SG A:CYS357 2.5 16.3 1.0
C1D A:HEM501 3.0 16.3 1.0
C1B A:HEM501 3.1 8.6 1.0
C4A A:HEM501 3.1 7.4 1.0
C4B A:HEM501 3.1 13.5 1.0
C4D A:HEM501 3.1 19.1 1.0
C4C A:HEM501 3.1 18.7 1.0
C1A A:HEM501 3.1 12.8 1.0
C1C A:HEM501 3.1 19.5 1.0
CB A:CYS357 3.4 15.1 1.0
CHD A:HEM501 3.4 16.3 1.0
CHB A:HEM501 3.4 5.6 1.0
CHA A:HEM501 3.5 17.9 1.0
CHC A:HEM501 3.5 16.5 1.0
C5 A:CAM502 3.9 19.1 1.0
CA A:CYS357 4.1 13.5 1.0
C2B A:HEM501 4.3 13.1 1.0
C2D A:HEM501 4.3 22.0 1.0
C3B A:HEM501 4.3 11.6 1.0
C3A A:HEM501 4.3 13.3 1.0
C3D A:HEM501 4.3 20.2 1.0
C2A A:HEM501 4.3 16.0 1.0
C3C A:HEM501 4.3 20.8 1.0
C2C A:HEM501 4.3 19.1 1.0
C4 A:CAM502 4.6 18.3 1.0
N A:GLY359 4.7 15.9 1.0
C A:CYS357 4.7 15.8 1.0
N A:ALA358 4.8 17.6 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: Sun Dec 13 15:40:46 2020

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