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Potassium 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:

Iron (Fe) 1 atom

Potassium Binding Sites:

The binding sites of Potassium 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 Potassium atom.
In total 3 binding sites of Potassium where determined in the Structure of Cyanide and Camphor Bound P450CAM Mutant L358P/K178G, PDB code: 4l4g:
Jump to Potassium binding site number: 1; 2; 3;

Potassium binding site 1 out of 3 in 4l4g

Go back to Potassium Binding Sites List in 4l4g
Potassium binding site 1 out of 3 in the Structure of Cyanide and Camphor Bound P450CAM Mutant L358P/K178G


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K 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:K504

b:17.0
occ:1.00
O A:GLU84 2.6 18.2 1.0
O A:TYR96 2.6 18.2 1.0
O A:GLY93 2.8 16.3 1.0
O A:HOH635 2.8 22.8 1.0
O A:HOH770 2.8 24.2 1.0
O A:GLU94 2.9 17.6 1.0
C A:GLU94 3.5 15.6 1.0
C A:TYR96 3.6 15.0 1.0
CA A:GLU94 3.7 14.8 1.0
C A:GLU84 3.8 20.0 1.0
C A:GLY93 3.9 13.7 1.0
N A:TYR96 3.9 14.5 1.0
CA A:TYR96 4.2 15.5 1.0
N A:GLU94 4.3 14.6 1.0
CG A:GLU84 4.3 27.8 1.0
CA A:CYS85 4.4 22.5 1.0
N A:ALA95 4.4 13.9 1.0
CB A:TYR96 4.5 14.6 1.0
N A:CYS85 4.5 18.2 1.0
C A:ALA95 4.5 16.1 1.0
N A:ASP97 4.6 15.0 1.0
CB A:CYS85 4.8 24.1 1.0
CA A:GLU84 4.8 17.7 1.0
CA A:ASP97 4.9 13.2 1.0
CA A:ALA95 4.9 18.9 1.0

Potassium binding site 2 out of 3 in 4l4g

Go back to Potassium Binding Sites List in 4l4g
Potassium binding site 2 out of 3 in the Structure of Cyanide and Camphor Bound P450CAM Mutant L358P/K178G


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Structure of Cyanide and Camphor Bound P450CAM Mutant L358P/K178G within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K505

b:30.5
occ:1.00
O A:VAL18 2.6 24.8 1.0
O A:HOH732 2.8 33.6 1.0
O A:PRO16 2.8 27.8 1.0
O A:PRO15 3.0 27.2 1.0
O A:HOH794 3.2 29.1 1.0
C A:PRO16 3.4 27.9 1.0
CD2 A:LEU14 3.6 28.2 1.0
C A:VAL18 3.6 28.8 1.0
CA A:PRO16 3.7 28.0 1.0
N A:VAL18 3.9 26.1 1.0
C A:PRO15 4.0 40.3 1.0
CG A:LEU14 4.0 34.5 1.0
CA A:VAL18 4.3 28.2 1.0
N A:PRO16 4.3 32.8 1.0
N A:HIS17 4.4 27.5 1.0
N A:PRO19 4.5 25.0 1.0
CA A:PRO19 4.6 26.8 1.0
C A:HIS17 4.6 21.6 1.0
CB A:LEU14 4.7 26.9 1.0
O A:LEU14 4.8 26.3 1.0
O A:HOH1028 4.9 44.7 1.0
N A:GLU20 4.9 26.5 1.0
CB A:VAL18 4.9 28.8 1.0
C A:PRO19 4.9 23.9 1.0
CA A:HIS17 4.9 42.9 1.0
C A:LEU14 5.0 29.7 1.0

Potassium binding site 3 out of 3 in 4l4g

Go back to Potassium Binding Sites List in 4l4g
Potassium binding site 3 out of 3 in the Structure of Cyanide and Camphor Bound P450CAM Mutant L358P/K178G


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 3 of Structure of Cyanide and Camphor Bound P450CAM Mutant L358P/K178G within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K506

b:24.5
occ:1.00
OG1 A:THR181 2.7 19.9 1.0
OD2 A:ASP182 2.7 20.3 1.0
OD2 A:ASP251 2.7 32.1 1.0
O A:HOH846 2.9 28.7 1.0
O A:LEU250 3.1 29.9 1.0
O A:GLY178 3.2 19.7 1.0
N A:ASP182 3.4 17.2 1.0
CG A:ASP182 3.6 23.7 1.0
CG A:ASP251 3.6 25.1 1.0
CB A:THR181 3.7 18.8 1.0
O A:HOH738 3.9 38.1 1.0
C A:THR181 3.9 15.1 1.0
CA A:ASP182 4.0 18.5 1.0
C A:LEU250 4.0 20.4 1.0
CB A:ASP251 4.0 17.8 1.0
C A:GLY178 4.1 17.3 1.0
CA A:GLY178 4.2 17.2 1.0
NH2 A:ARG186 4.2 17.4 1.0
CA A:ASP251 4.2 17.5 1.0
CA A:THR181 4.3 10.8 1.0
CB A:ASP182 4.4 17.5 1.0
O A:HOH749 4.4 27.6 1.0
OD1 A:ASP182 4.4 21.0 1.0
N A:ASP251 4.5 16.6 1.0
CB A:LEU250 4.5 15.8 1.0
O A:THR181 4.5 17.4 1.0
OD1 A:ASP251 4.6 27.9 1.0
O A:HOH699 4.9 23.0 1.0
N A:THR181 4.9 15.4 1.0
CA A:LEU250 4.9 15.4 1.0
CG2 A:THR181 5.0 13.9 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 23:39:59 2020

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