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Potassium in PDB 7n7c: Crystal Structure of the N-Formyltransferase HCAN_0200 From Helicobacter Canadensis in Complex with Folinic Acid and Dtdp-3- Aminoquinovose

Protein crystallography data

The structure of Crystal Structure of the N-Formyltransferase HCAN_0200 From Helicobacter Canadensis in Complex with Folinic Acid and Dtdp-3- Aminoquinovose, PDB code: 7n7c was solved by C.J.Heisdorf, J.B.Thoden, H.M.Holden, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.20 / 2.00
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 126.997, 74.039, 82.328, 90, 115.04, 90
R / Rfree (%) 18.2 / 23.2

Potassium Binding Sites:

The binding sites of Potassium atom in the Crystal Structure of the N-Formyltransferase HCAN_0200 From Helicobacter Canadensis in Complex with Folinic Acid and Dtdp-3- Aminoquinovose (pdb code 7n7c). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Crystal Structure of the N-Formyltransferase HCAN_0200 From Helicobacter Canadensis in Complex with Folinic Acid and Dtdp-3- Aminoquinovose, PDB code: 7n7c:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in 7n7c

Go back to Potassium Binding Sites List in 7n7c
Potassium binding site 1 out of 2 in the Crystal Structure of the N-Formyltransferase HCAN_0200 From Helicobacter Canadensis in Complex with Folinic Acid and Dtdp-3- Aminoquinovose


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Crystal Structure of the N-Formyltransferase HCAN_0200 From Helicobacter Canadensis in Complex with Folinic Acid and Dtdp-3- Aminoquinovose within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K306

b:30.1
occ:1.00
ND1 A:HIS96 2.0 16.4 1.0
O3 A:FON301 2.5 25.1 1.0
N3Q A:T3Q302 2.6 33.1 1.0
O A:HOH442 2.6 24.1 1.0
OD1 A:ASP132 2.7 20.7 1.0
CE1 A:HIS96 2.9 14.7 1.0
O2Q A:T3Q302 3.0 29.3 1.0
CG A:HIS96 3.1 15.9 1.0
O A:HOH435 3.2 21.0 1.0
CB A:HIS96 3.5 14.4 1.0
C3Q A:T3Q302 3.6 33.1 1.0
CG A:ASP132 3.6 16.7 1.0
CP1 A:FON301 3.6 25.3 1.0
CA A:HIS96 3.7 15.2 1.0
C2Q A:T3Q302 3.7 30.2 1.0
OD2 A:ASP132 3.7 15.4 1.0
ND2 A:ASN94 3.9 16.5 1.0
O A:HOH546 4.0 27.2 1.0
NE2 A:HIS96 4.0 17.0 1.0
CD2 A:HIS96 4.2 16.1 1.0
O A:HOH420 4.2 32.9 1.0
O A:GLY105 4.4 16.9 1.0
N A:PHE97 4.5 14.6 1.0
C A:HIS96 4.6 14.9 1.0
O A:MET95 4.7 15.1 1.0
N10 A:FON301 4.7 25.0 1.0
N A:HIS96 4.8 15.8 1.0
N5 A:FON301 4.9 24.9 1.0
C4Q A:T3Q302 4.9 33.8 1.0
CB A:ASP132 4.9 16.2 1.0
CG A:ASN94 5.0 16.9 1.0

Potassium binding site 2 out of 2 in 7n7c

Go back to Potassium Binding Sites List in 7n7c
Potassium binding site 2 out of 2 in the Crystal Structure of the N-Formyltransferase HCAN_0200 From Helicobacter Canadensis in Complex with Folinic Acid and Dtdp-3- Aminoquinovose


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Crystal Structure of the N-Formyltransferase HCAN_0200 From Helicobacter Canadensis in Complex with Folinic Acid and Dtdp-3- Aminoquinovose within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K303

b:33.8
occ:1.00
ND1 B:HIS96 2.0 23.8 1.0
N3Q B:T3Q302 2.4 31.0 1.0
O3 B:FON301 2.6 52.2 1.0
O B:HOH419 2.7 35.2 1.0
CE1 B:HIS96 2.9 23.3 1.0
O B:HOH421 2.9 20.1 1.0
O2Q B:T3Q302 3.1 31.8 1.0
CG B:HIS96 3.2 21.4 1.0
OD1 B:ASP132 3.3 22.9 1.0
C3Q B:T3Q302 3.5 32.2 1.0
CB B:HIS96 3.6 19.5 1.0
C2Q B:T3Q302 3.7 32.7 1.0
CA B:HIS96 3.7 19.4 1.0
CP1 B:FON301 3.8 56.0 1.0
OD2 B:ASP132 3.8 21.9 1.0
CG B:ASP132 3.9 22.7 1.0
O B:HOH418 4.0 36.9 1.0
ND2 B:ASN94 4.0 21.8 1.0
O B:HOH473 4.0 34.0 1.0
NE2 B:HIS96 4.1 24.1 1.0
CD2 B:HIS96 4.2 23.6 1.0
N B:PHE97 4.4 16.9 1.0
O B:GLY105 4.4 19.3 1.0
N10 B:FON301 4.6 55.5 1.0
O B:MET95 4.6 22.8 1.0
C B:HIS96 4.6 18.6 1.0
N B:HIS96 4.8 19.8 1.0
C4Q B:T3Q302 4.8 31.1 1.0
OE2 B:GLU77 4.8 19.5 1.0
N5 B:FON301 5.0 53.0 1.0
CG B:ASN94 5.0 24.0 1.0

Reference:

C.J.Heisdorf, W.A.Griffiths, J.B.Thoden, H.M.Holden. Investigation of the Enzymes Required For the Biosynthesis of An Unusual Formylated Sugar in the Emerging Human Pathogen Helicobacter Canadensis To Be Published.
Page generated: Mon Aug 12 19:28:45 2024

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