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Atomistry » Bromine » PDB 4kvh-4my6 » 4lau » |
Bromine in PDB 4lau: Crystal Structure of Human Ar Complexed with Nadp+ and {2-[(4- Bromobenzyl)Carbamoyl]-5-Chlorophenoxy}Acetic AcidEnzymatic activity of Crystal Structure of Human Ar Complexed with Nadp+ and {2-[(4- Bromobenzyl)Carbamoyl]-5-Chlorophenoxy}Acetic Acid
All present enzymatic activity of Crystal Structure of Human Ar Complexed with Nadp+ and {2-[(4- Bromobenzyl)Carbamoyl]-5-Chlorophenoxy}Acetic Acid:
1.1.1.21; Protein crystallography data
The structure of Crystal Structure of Human Ar Complexed with Nadp+ and {2-[(4- Bromobenzyl)Carbamoyl]-5-Chlorophenoxy}Acetic Acid, PDB code: 4lau
was solved by
A.Cousido-Siah,
A.Mitschler,
F.X.Ruiz,
J.Fanfrlik,
M.Kolar,
P.Hobza,
A.Podjarny,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 4lau:
The structure of Crystal Structure of Human Ar Complexed with Nadp+ and {2-[(4- Bromobenzyl)Carbamoyl]-5-Chlorophenoxy}Acetic Acid also contains other interesting chemical elements:
Bromine Binding Sites:
The binding sites of Bromine atom in the Crystal Structure of Human Ar Complexed with Nadp+ and {2-[(4- Bromobenzyl)Carbamoyl]-5-Chlorophenoxy}Acetic Acid
(pdb code 4lau). 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 Crystal Structure of Human Ar Complexed with Nadp+ and {2-[(4- Bromobenzyl)Carbamoyl]-5-Chlorophenoxy}Acetic Acid, PDB code: 4lau: Bromine binding site 1 out of 1 in 4lauGo back to![]() ![]()
Bromine binding site 1 out
of 1 in the Crystal Structure of Human Ar Complexed with Nadp+ and {2-[(4- Bromobenzyl)Carbamoyl]-5-Chlorophenoxy}Acetic Acid
![]() Mono view ![]() Stereo pair view
Reference:
J.Fanfrlik,
M.Kolar,
M.Kamlar,
D.Hurny,
F.X.Ruiz,
A.Cousido-Siah,
A.Mitschler,
J.Rezac,
E.Munusamy,
M.Lepsik,
P.Matejicek,
J.Vesely,
A.Podjarny,
P.Hobza.
Modulation of Aldose Reductase Inhibition By Halogen Bond Tuning. Acs Chem.Biol. V. 8 2484 2013.
Page generated: Mon Jul 7 07:01:58 2025
ISSN: ISSN 1554-8929 PubMed: 23988122 DOI: 10.1021/CB400526N |
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