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Potassium in PDB 4yb5: Adenosine Triphosphate Phosphoribosyltransferase From Campylobacter Jejuni in Complex with the Allosteric Inhibitor Histidine

Enzymatic activity of Adenosine Triphosphate Phosphoribosyltransferase From Campylobacter Jejuni in Complex with the Allosteric Inhibitor Histidine

All present enzymatic activity of Adenosine Triphosphate Phosphoribosyltransferase From Campylobacter Jejuni in Complex with the Allosteric Inhibitor Histidine:
2.4.2.17;

Protein crystallography data

The structure of Adenosine Triphosphate Phosphoribosyltransferase From Campylobacter Jejuni in Complex with the Allosteric Inhibitor Histidine, PDB code: 4yb5 was solved by G.Mittelstaedt, G.-J.Moggre, E.J.Parker, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.04 / 2.24
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 91.137, 123.216, 95.701, 90.00, 110.66, 90.00
R / Rfree (%) 20.9 / 23.9

Potassium Binding Sites:

The binding sites of Potassium atom in the Adenosine Triphosphate Phosphoribosyltransferase From Campylobacter Jejuni in Complex with the Allosteric Inhibitor Histidine (pdb code 4yb5). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 5 binding sites of Potassium where determined in the Adenosine Triphosphate Phosphoribosyltransferase From Campylobacter Jejuni in Complex with the Allosteric Inhibitor Histidine, PDB code: 4yb5:
Jump to Potassium binding site number: 1; 2; 3; 4; 5;

Potassium binding site 1 out of 5 in 4yb5

Go back to Potassium Binding Sites List in 4yb5
Potassium binding site 1 out of 5 in the Adenosine Triphosphate Phosphoribosyltransferase From Campylobacter Jejuni in Complex with the Allosteric Inhibitor Histidine


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Adenosine Triphosphate Phosphoribosyltransferase From Campylobacter Jejuni in Complex with the Allosteric Inhibitor Histidine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K303

b:77.6
occ:1.00
 OD1 A:ASN181 2.7 52.3 1.0
O A:GLN178 2.8 61.8 1.0
O F:ARG160 2.9 51.2 1.0
C A:GLN178 3.8 60.3 1.0
CG A:ASN181 3.9 54.4 1.0
C F:ARG160 4.0 50.3 1.0
OE1 A:GLN112 4.3 83.9 1.0
CA A:ALA179 4.4 57.3 1.0
N A:ASN181 4.4 55.7 1.0
CA A:ASN181 4.5 57.0 1.0
N A:ALA179 4.6 58.0 1.0
CA F:ARG160 4.6 49.6 1.0
CB F:ASN162 4.6 58.8 1.0
NE2 A:GLN112 4.7 77.0 1.0
N F:ASN162 4.8 54.5 1.0
ND2 A:ASN181 4.8 51.1 1.0
C A:ALA179 4.8 54.6 1.0
CA A:GLN178 4.9 59.7 1.0
CB A:ASN181 4.9 53.2 1.0
O F:PRO159 4.9 42.4 1.0
CD A:GLN112 5.0 83.3 1.0

Potassium binding site 2 out of 5 in 4yb5

Go back to Potassium Binding Sites List in 4yb5
Potassium binding site 2 out of 5 in the Adenosine Triphosphate Phosphoribosyltransferase From Campylobacter Jejuni in Complex with the Allosteric Inhibitor Histidine


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Adenosine Triphosphate Phosphoribosyltransferase From Campylobacter Jejuni in Complex with the Allosteric Inhibitor Histidine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K305

b:70.5
occ:1.00
 OD1 F:ASN181 2.7 60.4 1.0
O A:ARG160 2.9 51.7 1.0
O F:GLN178 3.0 50.2 1.0
CG F:ASN181 3.9 70.0 1.0
C A:ARG160 4.0 51.1 1.0
C F:GLN178 4.1 57.6 1.0
OE1 F:GLN112 4.2 92.4 1.0
CA A:ARG160 4.5 49.9 1.0
CB A:ASN162 4.6 67.4 1.0
N F:ASN181 4.6 62.7 1.0
CA F:ASN181 4.6 66.1 1.0
CA F:ALA179 4.7 63.0 1.0
N A:ASN162 4.7 60.9 1.0
NE2 F:GLN112 4.7 77.2 1.0
O A:PRO159 4.8 50.7 1.0
N F:ALA179 4.8 57.9 1.0
ND2 F:ASN181 4.8 63.7 1.0
CB F:ASN181 4.9 68.3 1.0
CD F:GLN112 4.9 84.5 1.0
CG F:GLN178 4.9 80.3 1.0
N A:ALA161 5.0 48.7 1.0

Potassium binding site 3 out of 5 in 4yb5

Go back to Potassium Binding Sites List in 4yb5
Potassium binding site 3 out of 5 in the Adenosine Triphosphate Phosphoribosyltransferase From Campylobacter Jejuni in Complex with the Allosteric Inhibitor Histidine


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 3 of Adenosine Triphosphate Phosphoribosyltransferase From Campylobacter Jejuni in Complex with the Allosteric Inhibitor Histidine within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K302

b:80.1
occ:1.00
 OD1 B:ASN181 2.7 65.4 1.0
O D:ARG160 2.7 55.9 1.0
O B:GLN178 2.8 65.9 1.0
C D:ARG160 3.8 55.5 1.0
CG B:ASN181 3.9 59.7 1.0
C B:GLN178 3.9 67.4 1.0
CA D:ARG160 4.4 58.4 1.0
CB D:ASN162 4.4 64.7 1.0
N D:ASN162 4.5 55.5 1.0
N B:ASN181 4.5 59.1 1.0
CA B:ASN181 4.5 63.2 1.0
O D:PRO159 4.5 56.9 1.0
CA B:ALA179 4.7 65.4 1.0
N B:ALA179 4.7 64.6 1.0
N D:ALA161 4.8 51.7 1.0
ND2 B:ASN181 4.8 59.9 1.0
CB B:ASN181 4.8 59.0 1.0
C D:ALA161 4.9 53.3 1.0
CA B:GLN178 4.9 69.8 1.0
CA D:ASN162 4.9 58.8 1.0

Potassium binding site 4 out of 5 in 4yb5

Go back to Potassium Binding Sites List in 4yb5
Potassium binding site 4 out of 5 in the Adenosine Triphosphate Phosphoribosyltransferase From Campylobacter Jejuni in Complex with the Allosteric Inhibitor Histidine


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 4 of Adenosine Triphosphate Phosphoribosyltransferase From Campylobacter Jejuni in Complex with the Allosteric Inhibitor Histidine within 5.0Å range:
probe atom residue distance (Å) B Occ
C:K303

b:63.7
occ:1.00
 O C:GLN178 2.6 50.3 1.0
OD1 C:ASN181 2.6 43.4 1.0
O E:ARG160 2.8 39.6 1.0
C C:GLN178 3.7 49.5 1.0
CG C:ASN181 3.8 49.6 1.0
C E:ARG160 3.9 42.6 1.0
OE1 C:GLN112 4.0 82.1 1.0
N C:ASN181 4.3 53.2 1.0
CA C:ASN181 4.3 52.7 1.0
CA C:ALA179 4.4 51.6 1.0
NE2 C:GLN112 4.5 73.4 1.0
N C:ALA179 4.5 51.9 1.0
CA E:ARG160 4.5 44.4 1.0
CD C:GLN112 4.7 74.0 1.0
CA C:GLN178 4.7 54.1 1.0
CB C:ASN181 4.7 49.4 1.0
CB E:ASN162 4.7 60.0 1.0
ND2 C:ASN181 4.8 47.3 1.0
N E:ASN162 4.8 54.5 1.0
C C:ALA179 4.8 49.9 1.0
O E:PRO159 4.9 44.4 1.0
N E:ALA161 5.0 45.5 1.0

Potassium binding site 5 out of 5 in 4yb5

Go back to Potassium Binding Sites List in 4yb5
Potassium binding site 5 out of 5 in the Adenosine Triphosphate Phosphoribosyltransferase From Campylobacter Jejuni in Complex with the Allosteric Inhibitor Histidine


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 5 of Adenosine Triphosphate Phosphoribosyltransferase From Campylobacter Jejuni in Complex with the Allosteric Inhibitor Histidine within 5.0Å range:
probe atom residue distance (Å) B Occ
C:K305

b:75.7
occ:1.00
 O C:ARG160 2.8 48.8 1.0
OD1 E:ASN181 2.9 49.8 1.0
O E:GLN178 2.9 65.5 1.0
C C:ARG160 3.9 48.8 1.0
C E:GLN178 4.0 57.1 1.0
CG E:ASN181 4.2 58.4 1.0
CB C:ASN162 4.4 56.2 1.0
CA E:ALA179 4.4 57.9 1.0
CA C:ARG160 4.5 50.5 1.0
N C:ASN162 4.6 50.4 1.0
N E:ALA179 4.7 54.4 1.0
O C:PRO159 4.7 49.3 1.0
N E:ASN181 4.7 51.4 1.0
CA E:ASN181 4.8 56.7 1.0
N C:ALA161 4.9 45.1 1.0
C E:ALA179 4.9 57.8 1.0
C C:ALA161 4.9 51.3 1.0

Reference:

G.Mittelstadt, G.J.Moggre, S.Panjikar, A.R.Nazmi, E.J.Parker. Campylobacter Jejuni Adenosine Triphosphate Phosphoribosyltransferase Is An Active Hexamer That Is Allosterically Controlled By the Twisting of A Regulatory Tail. Protein Sci. V. 25 1492 2016.
ISSN: ESSN 1469-896X
PubMed: 27191057
DOI: 10.1002/PRO.2948
Page generated: Mon Aug 12 12:44:07 2024

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