Sodium in PDB 8ad0: X-Ray Structure of Na+-Nqr From Vibrio Cholerae in Different Conformation at 3.1 A

Enzymatic activity of X-Ray Structure of Na+-Nqr From Vibrio Cholerae in Different Conformation at 3.1 A

All present enzymatic activity of X-Ray Structure of Na+-Nqr From Vibrio Cholerae in Different Conformation at 3.1 A:
7.2.1.1;

Protein crystallography data

The structure of X-Ray Structure of Na+-Nqr From Vibrio Cholerae in Different Conformation at 3.1 A, PDB code: 8ad0 was solved by G.Fritz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.12 / 3.11
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 89.31, 142.15, 105.93, 90, 109.83, 90
R / Rfree (%) 24.9 / 28.8

Other elements in 8ad0:

The structure of X-Ray Structure of Na+-Nqr From Vibrio Cholerae in Different Conformation at 3.1 A also contains other interesting chemical elements:

Bromine (Br) 1 atom
Iron (Fe) 4 atoms
Potassium (K) 1 atom

Sodium Binding Sites:

The binding sites of Sodium atom in the X-Ray Structure of Na+-Nqr From Vibrio Cholerae in Different Conformation at 3.1 A (pdb code 8ad0). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the X-Ray Structure of Na+-Nqr From Vibrio Cholerae in Different Conformation at 3.1 A, PDB code: 8ad0:

Sodium binding site 1 out of 1 in 8ad0

Go back to Sodium Binding Sites List in 8ad0
Sodium binding site 1 out of 1 in the X-Ray Structure of Na+-Nqr From Vibrio Cholerae in Different Conformation at 3.1 A


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of X-Ray Structure of Na+-Nqr From Vibrio Cholerae in Different Conformation at 3.1 A within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Na505

b:127.1
occ:1.00
 O B:VAL275 2.7 136.5 1.0
O B:VAL332 2.8 125.0 1.0
HD11 B:ILE268 2.9 161.6 1.0
HA B:VAL275 2.9 166.2 1.0
O B:GLU274 3.3 132.7 1.0
C B:VAL275 3.4 137.7 1.0
O B:HOH603 3.4 126.1 1.0
O B:ALA263 3.5 140.3 1.0
C B:VAL332 3.6 124.4 1.0
CA B:VAL275 3.6 137.8 1.0
O B:GLY334 3.6 123.1 1.0
HA B:LEU333 3.7 144.1 1.0
CD1 B:ILE268 3.8 134.0 1.0
HG3 B:GLU274 3.9 156.9 1.0
OG1 B:THR277 4.0 126.7 1.0
C B:GLU274 4.1 135.4 1.0
HD12 B:ILE268 4.1 161.6 1.0
H B:GLY334 4.2 141.0 1.0
HA B:VAL332 4.2 152.2 1.0
N B:LEU333 4.2 119.4 1.0
HB1 B:ALA263 4.2 160.5 1.0
CA B:LEU333 4.2 119.4 1.0
HD13 B:ILE268 4.3 161.6 1.0
N B:GLY334 4.3 116.9 1.0
H B:THR277 4.3 159.3 1.0
C B:LEU333 4.3 119.5 1.0
N B:VAL275 4.3 136.9 1.0
HG1 B:THR277 4.3 152.9 1.0
HA2 B:GLY266 4.5 211.7 1.0
CA B:VAL332 4.5 126.2 1.0
C B:ALA263 4.5 139.8 1.0
HB B:VAL332 4.5 162.9 1.0
HA B:ALA263 4.5 168.6 1.0
N B:SER276 4.6 141.0 1.0
HG13 B:ILE268 4.7 166.9 1.0
N B:THR277 4.7 132.1 1.0
C B:GLY334 4.7 121.3 1.0
CG1 B:ILE268 4.7 138.4 1.0
HG12 B:ILE268 4.7 166.9 1.0
HB B:VAL275 4.8 170.1 1.0
CB B:VAL275 4.8 141.1 1.0
H B:LEU333 4.9 144.1 1.0
CG B:GLU274 4.9 130.1 1.0
O B:LEU333 4.9 120.4 1.0
CA B:ALA263 4.9 139.8 1.0

Reference:

G.Fritz, G.Fritz. N/A N/A.
ISSN: ESSN 1545-9985
Page generated: Wed Oct 9 10:29:47 2024

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