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Bromine 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:

Iron (Fe) 4 atoms
Sodium (Na) 1 atom
Potassium (K) 1 atom

Bromine Binding Sites:

The binding sites of Bromine 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 Bromine atom.
In total only one binding site of Bromine was determined in the X-Ray Structure of Na+-Nqr From Vibrio Cholerae in Different Conformation at 3.1 A, PDB code: 8ad0:

Bromine binding site 1 out of 1 in 8ad0

Go back to Bromine Binding Sites List in 8ad0
Bromine 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 Bromine with other atoms in the Br 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
C:Br302

b:165.2
occ:1.00
HE2 C:HIS141 2.6 172.2 1.0
H C:ALA119 2.7 206.3 1.0
HA C:ARG118 3.1 208.3 1.0
HB2 C:ALA97 3.1 221.3 1.0
HG2 C:GLN93 3.2 206.3 1.0
HZ2 C:TRP238 3.3 174.5 1.0
HE21 C:GLN93 3.3 208.3 1.0
NE2 C:HIS141 3.4 142.8 1.0
N C:ALA119 3.5 171.3 1.0
HH2 C:TRP238 3.6 179.3 1.0
NE2 C:GLN93 3.7 172.9 1.0
HB2 C:ALA119 3.8 213.4 1.0
HB3 C:ALA119 3.8 213.4 1.0
CB C:ALA97 3.9 183.8 1.0
HB1 C:ALA97 3.9 221.3 1.0
HG2 C:ARG118 3.9 197.0 1.0
CA C:ARG118 4.0 172.9 1.0
CZ2 C:TRP238 4.0 144.8 1.0
CG C:GLN93 4.0 171.3 1.0
CD C:GLN93 4.0 169.4 1.0
HE22 C:GLN93 4.0 208.3 1.0
CB C:ALA119 4.1 177.2 1.0
CH2 C:TRP238 4.2 148.8 1.0
O C:ARG117 4.2 177.7 1.0
CE1 C:HIS141 4.2 143.2 1.0
HB3 C:ALA97 4.2 221.3 1.0
CD2 C:HIS141 4.2 139.0 1.0
C C:ARG118 4.3 173.7 1.0
HE1 C:HIS141 4.3 172.7 1.0
HD2 C:HIS141 4.3 167.6 1.0
HG3 C:ARG118 4.4 197.0 1.0
CA C:ALA119 4.4 174.3 1.0
HG3 C:GLN93 4.5 206.3 1.0
CG C:ARG118 4.5 163.5 1.0
HD12 C:ILE115 4.6 188.1 1.0
O C:GLN93 4.6 185.4 1.0
CB C:ARG118 4.8 168.4 1.0
N C:ARG118 4.9 178.3 1.0
OE1 C:GLN93 4.9 164.4 1.0
C C:ARG117 4.9 180.4 1.0
HE2 C:PHE78 4.9 199.3 1.0

Reference:

G.Fritz, G.Fritz. N/A N/A.
ISSN: ESSN 1545-9985
Page generated: Thu Jul 11 04:51:31 2024

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