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Potassium in PDB 8acw: X-Ray Structure of Na+-Nqr From Vibrio Cholerae at 3.4 A Resolution

Enzymatic activity of X-Ray Structure of Na+-Nqr From Vibrio Cholerae at 3.4 A Resolution

All present enzymatic activity of X-Ray Structure of Na+-Nqr From Vibrio Cholerae at 3.4 A Resolution:
7.2.1.1;

Protein crystallography data

The structure of X-Ray Structure of Na+-Nqr From Vibrio Cholerae at 3.4 A Resolution, PDB code: 8acw was solved by G.Fritz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.60 / 3.40
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 93.72, 142.94, 103.39, 90, 109.93, 90
R / Rfree (%) 27 / 30.6

Other elements in 8acw:

The structure of X-Ray Structure of Na+-Nqr From Vibrio Cholerae at 3.4 A Resolution also contains other interesting chemical elements:

Iron (Fe) 4 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the X-Ray Structure of Na+-Nqr From Vibrio Cholerae at 3.4 A Resolution (pdb code 8acw). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total only one binding site of Potassium was determined in the X-Ray Structure of Na+-Nqr From Vibrio Cholerae at 3.4 A Resolution, PDB code: 8acw:

Potassium binding site 1 out of 1 in 8acw

Go back to Potassium Binding Sites List in 8acw
Potassium binding site 1 out of 1 in the X-Ray Structure of Na+-Nqr From Vibrio Cholerae at 3.4 A Resolution


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of X-Ray Structure of Na+-Nqr From Vibrio Cholerae at 3.4 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K504

b:155.3
occ:1.00
 O B:ARG372 2.4 140.1 1.0
O B:TYR378 2.4 159.5 1.0
O B:ASN375 2.8 130.7 1.0
HA B:PRO379 2.9 173.9 1.0
HA B:ARG372 3.3 166.7 1.0
C B:ARG372 3.3 151.2 1.0
O B:ILE371 3.4 166.7 1.0
C B:TYR378 3.5 146.9 1.0
CA B:PRO379 3.7 144.6 1.0
HA B:PRO376 3.8 197.1 1.0
C B:ASN375 3.8 146.3 1.0
CA B:ARG372 3.9 138.6 1.0
HE2 B:MET322 4.0 204.7 1.0
N B:PRO379 4.0 93.5 1.0
O B:PRO379 4.1 174.4 1.0
C B:PRO379 4.1 175.8 1.0
H B:ASN375 4.1 197.4 1.0
HE1 B:MET322 4.2 204.7 1.0
H B:TYR378 4.2 183.0 1.0
O B:PRO376 4.3 172.2 1.0
N B:VAL373 4.4 168.4 1.0
C B:ILE371 4.4 156.1 1.0
CA B:PRO376 4.4 164.0 1.0
HB3 B:ASN375 4.4 186.6 1.0
HG3 B:MET322 4.5 200.7 1.0
C B:PRO376 4.5 187.9 1.0
CE B:MET322 4.5 170.3 1.0
N B:TYR378 4.6 152.3 1.0
HA B:VAL373 4.6 143.1 1.0
N B:PRO376 4.6 150.5 1.0
CA B:TYR378 4.6 144.0 1.0
HB2 B:ALA242 4.6 252.2 1.0
N B:ARG372 4.6 125.2 1.0
O B:VAL373 4.7 144.4 1.0
N B:ASN375 4.7 164.2 1.0
C B:VAL373 4.8 95.2 1.0
CA B:ASN375 4.8 155.3 1.0
HB2 B:TYR378 4.8 191.0 1.0
CA B:VAL373 4.8 119.0 1.0
HB3 B:PRO379 4.9 150.6 1.0
CB B:PRO379 4.9 125.2 1.0
HB3 B:ARG372 5.0 168.9 1.0

Reference:

G.Fritz, G.Fritz. N/A N/A.
ISSN: ESSN 1545-9985
Page generated: Mon Aug 12 22:00:18 2024

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