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Potassium in PDB 3fwg: Ferric Camphor Bound Cytochrome P450CAM, ARG365LEU, GLU366GLN, Monoclinic Crystal Form

Enzymatic activity of Ferric Camphor Bound Cytochrome P450CAM, ARG365LEU, GLU366GLN, Monoclinic Crystal Form

All present enzymatic activity of Ferric Camphor Bound Cytochrome P450CAM, ARG365LEU, GLU366GLN, Monoclinic Crystal Form:
1.14.15.1;

Protein crystallography data

The structure of Ferric Camphor Bound Cytochrome P450CAM, ARG365LEU, GLU366GLN, Monoclinic Crystal Form, PDB code: 3fwg was solved by I.Schlichting, K.Von Koenig, C.Aldag, D.Hilvert, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 39.13 / 1.55
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 67.180, 62.795, 95.605, 90.00, 90.53, 90.00
R / Rfree (%) 18.5 / 21.7

Other elements in 3fwg:

The structure of Ferric Camphor Bound Cytochrome P450CAM, ARG365LEU, GLU366GLN, Monoclinic Crystal Form also contains other interesting chemical elements:

Iron (Fe) 2 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the Ferric Camphor Bound Cytochrome P450CAM, ARG365LEU, GLU366GLN, Monoclinic Crystal Form (pdb code 3fwg). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 3 binding sites of Potassium where determined in the Ferric Camphor Bound Cytochrome P450CAM, ARG365LEU, GLU366GLN, Monoclinic Crystal Form, PDB code: 3fwg:
Jump to Potassium binding site number: 1; 2; 3;

Potassium binding site 1 out of 3 in 3fwg

Go back to Potassium Binding Sites List in 3fwg
Potassium binding site 1 out of 3 in the Ferric Camphor Bound Cytochrome P450CAM, ARG365LEU, GLU366GLN, Monoclinic Crystal Form


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Ferric Camphor Bound Cytochrome P450CAM, ARG365LEU, GLU366GLN, Monoclinic Crystal Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K515

b:21.3
occ:1.00
 O A:GLU84 2.6 22.1 1.0
O A:TYR96 2.6 19.7 1.0
O A:HOH478 2.7 67.3 1.0
O A:GLY93 2.8 22.3 1.0
O A:HOH427 2.9 37.1 1.0
O A:GLU94 3.0 22.5 1.0
C A:GLU94 3.6 21.9 1.0
C A:TYR96 3.7 19.2 1.0
C A:GLU84 3.8 22.8 1.0
CA A:GLU94 3.8 22.6 1.0
C A:GLY93 3.9 22.8 1.0
N A:TYR96 4.2 20.4 1.0
N A:GLU94 4.4 22.6 1.0
CA A:TYR96 4.4 19.6 1.0
CA A:CYS85 4.4 22.7 1.0
N A:ALA95 4.6 21.2 1.0
N A:CYS85 4.6 22.6 1.0
C A:ALA95 4.6 20.8 1.0
CB A:TYR96 4.6 19.5 1.0
CG A:GLU84 4.7 27.8 1.0
N A:ASP97 4.8 18.6 1.0
CA A:GLU84 4.8 22.9 1.0
CB A:CYS85 4.9 22.8 1.0
O A:ALA95 5.0 21.4 1.0
CD A:PRO86 5.0 22.1 1.0

Potassium binding site 2 out of 3 in 3fwg

Go back to Potassium Binding Sites List in 3fwg
Potassium binding site 2 out of 3 in the Ferric Camphor Bound Cytochrome P450CAM, ARG365LEU, GLU366GLN, Monoclinic Crystal Form


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Ferric Camphor Bound Cytochrome P450CAM, ARG365LEU, GLU366GLN, Monoclinic Crystal Form within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K515

b:12.8
occ:1.00
 O B:GLU84 2.6 13.3 1.0
O B:TYR96 2.6 11.6 1.0
O B:HOH474 2.7 37.3 1.0
O B:GLY93 2.8 12.1 1.0
O B:GLU94 2.8 13.2 1.0
O B:HOH535 2.8 19.3 1.0
C B:GLU94 3.5 12.1 1.0
CA B:GLU94 3.7 12.2 1.0
C B:TYR96 3.7 11.8 1.0
C B:GLU84 3.8 12.4 1.0
C B:GLY93 3.9 12.2 1.0
N B:TYR96 4.1 12.0 1.0
SG B:CYS85 4.2 23.2 0.5
N B:GLU94 4.3 12.1 1.0
CA B:TYR96 4.3 11.6 1.0
O B:HOH548 4.4 33.2 1.0
CA B:CYS85 4.4 10.9 0.5
CA B:CYS85 4.4 14.1 0.5
C B:ALA95 4.5 12.1 1.0
N B:ALA95 4.5 11.7 1.0
N B:CYS85 4.6 13.1 0.5
N B:CYS85 4.6 11.7 0.5
CG B:GLU84 4.6 20.9 1.0
CB B:TYR96 4.6 11.8 1.0
O B:HOH555 4.8 27.8 1.0
N B:ASP97 4.8 11.1 1.0
CB B:CYS85 4.9 10.6 0.5
CA B:GLU84 4.9 12.8 1.0
O B:ALA95 4.9 14.0 1.0
CB B:CYS85 4.9 14.5 0.5
CA B:ASP97 5.0 11.3 1.0
CB B:GLU94 5.0 13.0 1.0
CA B:ALA95 5.0 12.1 1.0

Potassium binding site 3 out of 3 in 3fwg

Go back to Potassium Binding Sites List in 3fwg
Potassium binding site 3 out of 3 in the Ferric Camphor Bound Cytochrome P450CAM, ARG365LEU, GLU366GLN, Monoclinic Crystal Form


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 3 of Ferric Camphor Bound Cytochrome P450CAM, ARG365LEU, GLU366GLN, Monoclinic Crystal Form within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K715

b:16.4
occ:1.00
 O B:VAL18 2.6 14.9 1.0
O B:PRO16 2.8 15.8 1.0
O B:HOH8 2.8 20.4 1.0
O B:PRO15 2.9 15.7 1.0
OE2 B:GLU20 2.9 20.1 1.0
C B:PRO16 3.4 15.7 1.0
C B:VAL18 3.6 14.9 1.0
CA B:PRO16 3.7 16.4 1.0
CD B:GLU20 3.7 18.4 1.0
N B:VAL18 3.8 14.1 1.0
C B:PRO15 3.9 16.2 1.0
CD2 B:LEU14 3.9 17.8 1.0
O B:HOH425 4.0 24.1 1.0
OE1 B:GLU20 4.1 17.4 1.0
CG B:LEU14 4.2 17.7 1.0
CA B:VAL18 4.3 14.0 1.0
N B:PRO16 4.3 16.8 1.0
N B:HIS17 4.3 15.0 1.0
O B:HOH769 4.4 36.0 1.0
C B:HIS17 4.5 14.4 1.0
N B:PRO19 4.6 15.5 1.0
CA B:PRO19 4.8 15.7 1.0
CG B:GLU20 4.8 18.5 1.0
O B:LEU14 4.8 17.0 1.0
CB B:VAL18 4.8 14.0 1.0
N B:GLU20 4.8 15.8 1.0
CA B:HIS17 4.9 14.8 1.0
CB B:LEU14 5.0 17.1 1.0

Reference:

C.Aldag, I.A.Gromov, I.Garcia-Rubio, K.Von Koenig, I.Schlichting, B.Jaun, D.Hilvert. Probing the Role of the Proximal Heme Ligand in Cytochrome P450CAM By Recombinant Incorporation of Selenocysteine. Proc.Natl.Acad.Sci.Usa V. 106 5481 2009.
ISSN: ISSN 0027-8424
PubMed: 19293375
DOI: 10.1073/PNAS.0810503106
Page generated: Mon Aug 12 08:20:37 2024

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