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Potassium in PDB 7nf2: Structure of T. Atroviride Fdc Variant Tafdcv in Complex with Prfmn Crotonic Acid Adduct

Enzymatic activity of Structure of T. Atroviride Fdc Variant Tafdcv in Complex with Prfmn Crotonic Acid Adduct

All present enzymatic activity of Structure of T. Atroviride Fdc Variant Tafdcv in Complex with Prfmn Crotonic Acid Adduct:
4.1.1.102;

Protein crystallography data

The structure of Structure of T. Atroviride Fdc Variant Tafdcv in Complex with Prfmn Crotonic Acid Adduct, PDB code: 7nf2 was solved by A.Saaret, D.Leys, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 115.12 / 1.33
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 74.54, 74.54, 345.36, 90, 90, 120
R / Rfree (%) 16.2 / 18.1

Other elements in 7nf2:

The structure of Structure of T. Atroviride Fdc Variant Tafdcv in Complex with Prfmn Crotonic Acid Adduct also contains other interesting chemical elements:

Manganese (Mn) 2 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the Structure of T. Atroviride Fdc Variant Tafdcv in Complex with Prfmn Crotonic Acid Adduct (pdb code 7nf2). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 4 binding sites of Potassium where determined in the Structure of T. Atroviride Fdc Variant Tafdcv in Complex with Prfmn Crotonic Acid Adduct, PDB code: 7nf2:
Jump to Potassium binding site number: 1; 2; 3; 4;

Potassium binding site 1 out of 4 in 7nf2

Go back to Potassium Binding Sites List in 7nf2
Potassium binding site 1 out of 4 in the Structure of T. Atroviride Fdc Variant Tafdcv in Complex with Prfmn Crotonic Acid Adduct


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Structure of T. Atroviride Fdc Variant Tafdcv in Complex with Prfmn Crotonic Acid Adduct within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K1206

b:11.8
occ:1.00
O A:LEU471 2.6 11.6 1.0
O A:ARG431 2.6 11.4 1.0
O A:ASP469 2.7 11.1 1.0
OD2 A:ASP437 2.8 12.6 1.0
O A:HOH1680 2.8 13.7 1.0
O A:HOH1347 3.2 13.7 1.0
OD2 A:ASP469 3.3 15.2 1.0
CG A:ASP437 3.4 12.4 1.0
C A:LEU471 3.6 10.7 1.0
CG A:ASP469 3.7 12.6 1.0
C A:ASP469 3.8 11.0 1.0
C A:ARG431 3.8 10.4 1.0
CB A:ASP437 3.9 12.3 1.0
OD1 A:ASP469 4.0 13.7 1.0
OD1 B:ASN457 4.0 15.1 1.0
N A:LEU471 4.1 11.1 1.0
OD1 A:ASP437 4.1 13.4 1.0
CA A:CYS432 4.2 10.7 1.0
O A:HOH1425 4.2 13.6 1.0
CB A:ASP469 4.3 11.3 1.0
CA A:LEU472 4.4 11.6 1.0
N A:LEU472 4.4 12.3 1.0
CA A:ALA470 4.4 10.9 1.0
N A:CYS432 4.5 10.7 1.0
N A:ALA470 4.5 10.6 1.0
CA A:LEU471 4.5 12.6 1.0
C A:ALA470 4.5 11.5 1.0
CA A:ASP469 4.7 10.9 1.0
N A:ARG433 4.7 11.2 1.0
C A:LEU472 4.9 12.1 1.0
CA A:ARG431 4.9 10.3 1.0

Potassium binding site 2 out of 4 in 7nf2

Go back to Potassium Binding Sites List in 7nf2
Potassium binding site 2 out of 4 in the Structure of T. Atroviride Fdc Variant Tafdcv in Complex with Prfmn Crotonic Acid Adduct


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Structure of T. Atroviride Fdc Variant Tafdcv in Complex with Prfmn Crotonic Acid Adduct within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K1207

b:13.4
occ:1.00
OE2 A:GLU243 2.8 9.7 1.0
O A:MET235 2.8 11.9 1.0
O7 A:JRH1205 2.8 10.3 1.0
O A:ALA232 2.9 10.6 1.0
O6 A:JRH1205 3.0 9.6 1.0
O A:TRP179 3.0 9.4 1.0
O A:SER233 3.1 11.5 1.0
O A:HOH1374 3.4 10.2 1.0
P1 A:JRH1205 3.4 9.9 1.0
C A:SER233 3.5 10.6 1.0
CD A:GLU243 3.6 9.4 1.0
MN A:MN1208 3.7 14.7 1.0
O9 A:JRH1205 3.7 10.8 1.0
CA A:SER233 3.7 9.9 1.0
CG A:GLU243 3.8 10.1 1.0
C A:MET235 3.9 10.5 1.0
C A:ALA232 3.9 10.3 1.0
N A:MET235 4.1 10.7 1.0
O4 A:JRH1205 4.2 11.6 1.0
C22 A:JRH1205 4.2 10.4 1.0
C21 A:JRH1205 4.2 10.0 1.0
C A:TRP179 4.2 9.4 1.0
N A:SER233 4.3 9.7 1.0
CB A:SER180 4.3 10.3 1.0
N A:SER234 4.4 10.0 1.0
CA A:SER180 4.4 9.3 1.0
CA A:MET235 4.6 11.7 1.0
OE1 A:GLU243 4.7 10.3 1.0
C A:SER234 4.8 10.6 1.0
OD1 A:ASN178 4.8 12.4 1.0
N A:SER180 4.8 9.2 1.0
CG1 A:ILE237 4.9 12.1 1.0
O8 A:JRH1205 4.9 10.9 1.0
N A:PRO236 4.9 9.9 1.0
N A:ILE237 4.9 11.7 1.0

Potassium binding site 3 out of 4 in 7nf2

Go back to Potassium Binding Sites List in 7nf2
Potassium binding site 3 out of 4 in the Structure of T. Atroviride Fdc Variant Tafdcv in Complex with Prfmn Crotonic Acid Adduct


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 3 of Structure of T. Atroviride Fdc Variant Tafdcv in Complex with Prfmn Crotonic Acid Adduct within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K904

b:12.7
occ:1.00
O B:ARG431 2.6 12.2 1.0
O B:LEU471 2.6 12.7 1.0
O B:ASP469 2.7 12.9 1.0
OD2 B:ASP437 2.7 12.2 1.0
O B:HOH1333 2.8 12.5 1.0
O B:HOH1118 3.2 13.5 1.0
OD2 B:ASP469 3.3 14.6 1.0
CG B:ASP437 3.4 12.8 1.0
CG B:ASP469 3.6 13.5 1.0
C B:LEU471 3.6 11.8 1.0
C B:ASP469 3.8 12.0 1.0
C B:ARG431 3.8 11.7 1.0
CB B:ASP437 3.9 12.4 1.0
OD1 B:ASP469 4.0 14.1 1.0
OD1 A:ASN457 4.0 17.2 1.0
OD1 B:ASP437 4.1 14.2 1.0
N B:LEU471 4.1 12.2 1.0
CA B:CYS432 4.2 10.9 1.0
O B:HOH1098 4.2 12.8 1.0
CB B:ASP469 4.3 12.3 1.0
N B:LEU472 4.4 11.8 1.0
N B:CYS432 4.4 10.4 1.0
CA B:LEU472 4.4 12.0 1.0
CA B:ALA470 4.5 11.3 1.0
N B:ALA470 4.5 12.1 1.0
CA B:LEU471 4.5 12.0 1.0
C B:ALA470 4.6 11.5 1.0
N B:ARG433 4.7 10.3 1.0
CA B:ASP469 4.7 12.6 1.0
CA B:ARG431 4.9 11.1 1.0
C B:LEU472 4.9 13.3 1.0

Potassium binding site 4 out of 4 in 7nf2

Go back to Potassium Binding Sites List in 7nf2
Potassium binding site 4 out of 4 in the Structure of T. Atroviride Fdc Variant Tafdcv in Complex with Prfmn Crotonic Acid Adduct


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 4 of Structure of T. Atroviride Fdc Variant Tafdcv in Complex with Prfmn Crotonic Acid Adduct within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K905

b:17.8
occ:1.00
OE2 B:GLU243 2.8 16.1 1.0
O B:MET235 2.8 15.6 1.0
O8 B:JRH903 2.9 13.7 1.0
O B:ALA232 2.9 16.9 1.0
O6 B:JRH903 3.0 14.0 1.0
O B:TRP179 3.0 13.3 1.0
O B:SER233 3.2 14.3 1.0
O B:HOH1062 3.4 14.3 1.0
P1 B:JRH903 3.5 14.2 1.0
C B:SER233 3.5 13.4 1.0
CD B:GLU243 3.6 15.6 1.0
MN B:MN906 3.7 19.6 1.0
O7 B:JRH903 3.7 14.9 1.0
CG B:GLU243 3.7 14.6 1.0
CA B:SER233 3.8 14.6 1.0
C B:MET235 3.9 16.7 1.0
C B:ALA232 4.0 15.6 1.0
N B:MET235 4.1 17.8 1.0
O4 B:JRH903 4.1 16.8 1.0
C B:TRP179 4.2 13.7 1.0
C22 B:JRH903 4.2 14.3 1.0
C21 B:JRH903 4.2 14.1 1.0
N B:SER233 4.3 14.9 1.0
CB B:SER180 4.3 13.1 1.0
CA B:SER180 4.4 13.4 1.0
N B:SER234 4.4 14.7 1.0
CA B:MET235 4.6 17.3 1.0
OE1 B:GLU243 4.6 14.3 1.0
C B:SER234 4.8 17.8 1.0
OD1 B:ASN178 4.8 18.5 1.0
N B:SER180 4.8 13.3 1.0
O9 B:JRH903 4.9 13.7 1.0
N B:PRO236 4.9 17.7 1.0
CG1 B:ILE237 4.9 17.9 1.0
N B:ILE237 5.0 16.0 1.0

Reference:

A.Saaret, B.Villiers, F.Stricher, M.Anissimova, M.Cadillon, R.Spiess, S.Hay, D.Leys. Directed Evolution of Prenylated Fmn-Dependent Fdc Supports Efficient in Vivo Isobutene Production Nat Commun 2021.
ISSN: ESSN 2041-1723
Page generated: Mon Aug 12 19:31:46 2024

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