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Bromine in PDB 4uqs: Structure of Bacillus Subtilis Nitric Oxide Synthase in Complex with 3-Bromo-7-Nitroindazole

Enzymatic activity of Structure of Bacillus Subtilis Nitric Oxide Synthase in Complex with 3-Bromo-7-Nitroindazole

All present enzymatic activity of Structure of Bacillus Subtilis Nitric Oxide Synthase in Complex with 3-Bromo-7-Nitroindazole:
1.14.13.165;

Protein crystallography data

The structure of Structure of Bacillus Subtilis Nitric Oxide Synthase in Complex with 3-Bromo-7-Nitroindazole, PDB code: 4uqs was solved by J.K.Holden, T.L.Poulos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 2.15
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 80.420, 94.530, 63.227, 90.00, 90.00, 90.00
R / Rfree (%) 22.863 / 28.306

Other elements in 4uqs:

The structure of Structure of Bacillus Subtilis Nitric Oxide Synthase in Complex with 3-Bromo-7-Nitroindazole also contains other interesting chemical elements:

Iron (Fe) 1 atom
Chlorine (Cl) 1 atom

Bromine Binding Sites:

The binding sites of Bromine atom in the Structure of Bacillus Subtilis Nitric Oxide Synthase in Complex with 3-Bromo-7-Nitroindazole (pdb code 4uqs). 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 Structure of Bacillus Subtilis Nitric Oxide Synthase in Complex with 3-Bromo-7-Nitroindazole, PDB code: 4uqs:

Bromine binding site 1 out of 1 in 4uqs

Go back to Bromine Binding Sites List in 4uqs
Bromine binding site 1 out of 1 in the Structure of Bacillus Subtilis Nitric Oxide Synthase in Complex with 3-Bromo-7-Nitroindazole


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Structure of Bacillus Subtilis Nitric Oxide Synthase in Complex with 3-Bromo-7-Nitroindazole within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br904

b:47.0
occ:1.00
 BR A:INE904 0.0 47.0 1.0
C3 A:INE904 1.9 43.3 1.0
N2 A:INE904 2.9 51.2 1.0
C9 A:INE904 3.0 51.3 1.0
CE1 A:PHE235 3.2 42.2 1.0
CD1 A:PHE235 3.3 42.8 1.0
C4 A:INE904 3.5 54.8 1.0
N A:GLY237 3.7 35.8 1.0
CA A:ASN236 3.7 37.2 1.0
C1C A:HEM901 3.7 34.4 1.0
O A:PHE235 3.8 39.4 1.0
C A:ASN236 3.9 38.7 1.0
C2C A:HEM901 3.9 37.1 1.0
CG1 A:ILE218 4.0 49.3 1.0
NC A:HEM901 4.0 43.7 1.0
O A:PRO216 4.1 36.7 1.0
N1 A:INE904 4.1 48.7 1.0
C8 A:INE904 4.1 49.1 1.0
C3C A:HEM901 4.2 37.8 1.0
C4C A:HEM901 4.2 36.4 1.0
CHC A:HEM901 4.2 36.1 1.0
C A:PHE235 4.2 41.9 1.0
N A:ASN236 4.3 37.6 1.0
CZ A:PHE235 4.4 43.5 1.0
CG A:PHE235 4.5 43.9 1.0
CMC A:HEM901 4.5 44.4 1.0
FE A:HEM901 4.6 41.7 1.0
CA A:GLY237 4.7 37.5 1.0
C4B A:HEM901 4.7 32.2 1.0
O A:ASN236 4.8 37.2 1.0
NB A:HEM901 4.8 33.8 1.0
CHD A:HEM901 4.8 44.6 1.0
CB A:ASN236 4.8 37.9 1.0
CB A:ILE218 4.9 45.5 1.0
N A:ILE218 4.9 36.7 1.0
C5 A:INE904 4.9 52.1 1.0
C A:PRO216 4.9 40.5 1.0
CD1 A:ILE218 5.0 49.8 1.0
ND A:HEM901 5.0 40.4 1.0
CAC A:HEM901 5.0 38.9 1.0

Reference:

J.K.Holden, N.Lim, T.L.Poulos. Identification of Redox Partners and Development of A Novel Chimeric Bacterial Nitric Oxide Synthase For Structure Activity Analyses. J.Biol.Chem. V. 289 29437 2014.
ISSN: ISSN 0021-9258
PubMed: 25194416
DOI: 10.1074/JBC.M114.595165
Page generated: Sat Dec 12 02:23:29 2020

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