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Potassium in PDB 6b10: C. Jejuni Agmatine Deiminase

Protein crystallography data

The structure of C. Jejuni Agmatine Deiminase, PDB code: 6b10 was solved by R.Shek, K.A.Hicks, J.B.French, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.60 / 2.09
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 53.400, 80.296, 83.923, 90.00, 97.36, 90.00
R / Rfree (%) 20 / 25

Potassium Binding Sites:

The binding sites of Potassium atom in the C. Jejuni Agmatine Deiminase (pdb code 6b10). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the C. Jejuni Agmatine Deiminase, PDB code: 6b10:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in 6b10

Go back to Potassium Binding Sites List in 6b10
Potassium binding site 1 out of 2 in the C. Jejuni Agmatine Deiminase


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of C. Jejuni Agmatine Deiminase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K403

b:48.9
occ:1.00
O A:PHE99 2.5 47.0 1.0
OD1 A:ASP98 2.8 49.5 1.0
O A:PHE83 2.8 42.1 1.0
O A:HOH544 3.0 44.0 1.0
C A:PHE99 3.6 46.2 1.0
C A:PHE83 3.8 39.4 1.0
N A:PHE99 3.9 43.1 1.0
CA A:PHE83 4.0 40.1 1.0
CG A:ASP98 4.1 47.8 1.0
ND2 A:ASN117 4.1 62.6 1.0
CB A:PHE101 4.1 62.0 1.0
CB A:PHE83 4.3 40.3 1.0
CA A:PHE99 4.3 43.6 1.0
C A:ASP98 4.4 42.8 1.0
N A:PHE101 4.5 58.8 1.0
CA A:ASP98 4.6 42.8 1.0
O A:GLY84 4.7 37.6 1.0
N A:THR100 4.7 49.8 1.0
CB A:PHE99 4.8 41.4 1.0
C A:THR100 4.8 55.7 1.0
CA A:THR100 4.9 53.7 1.0
OD2 A:ASP98 4.9 51.1 1.0
CA A:PHE101 4.9 61.6 1.0
CB A:ASP98 5.0 45.7 1.0
N A:GLY84 5.0 38.5 1.0

Potassium binding site 2 out of 2 in 6b10

Go back to Potassium Binding Sites List in 6b10
Potassium binding site 2 out of 2 in the C. Jejuni Agmatine Deiminase


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of C. Jejuni Agmatine Deiminase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K403

b:35.7
occ:1.00
O B:PHE99 2.6 33.2 1.0
OD1 B:ASP98 2.8 38.2 1.0
O B:HOH587 2.8 38.6 1.0
O B:PHE83 2.8 32.1 1.0
O B:HOH565 2.9 26.6 1.0
C B:PHE99 3.7 34.1 1.0
C B:PHE83 3.7 31.1 1.0
N B:PHE99 3.8 32.2 1.0
ND2 B:ASN117 3.9 34.7 1.0
O B:HOH506 4.0 34.7 1.0
CG B:ASP98 4.0 37.9 1.0
CA B:PHE83 4.1 31.2 1.0
CB B:PHE101 4.1 39.5 1.0
CA B:PHE99 4.2 32.6 1.0
C B:ASP98 4.3 32.5 1.0
O B:GLY84 4.5 30.8 1.0
CA B:ASP98 4.5 33.0 1.0
N B:PHE101 4.5 38.9 1.0
CB B:PHE83 4.5 31.7 1.0
N B:THR100 4.7 35.1 1.0
CB B:PHE99 4.8 32.4 1.0
N B:GLY84 4.9 29.8 1.0
OD2 B:ASP98 4.9 42.0 1.0
C B:THR100 4.9 37.8 1.0
CB B:ASP98 4.9 35.4 1.0
C B:GLY84 4.9 30.5 1.0
CA B:PHE101 5.0 39.9 1.0

Reference:

R.Shek, D.A.Dattmore, D.P.Stives, A.L.Jackson, C.H.Chatfield, K.A.Hicks, J.B.French. Structural and Functional Basis For Targeting Campylobacter Jejuni Agmatine Deiminase to Overcome Antibiotic Resistance. Biochemistry V. 56 6734 2017.
ISSN: ISSN 1520-4995
PubMed: 29190068
DOI: 10.1021/ACS.BIOCHEM.7B00982
Page generated: Sat Aug 9 10:26:34 2025

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