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Atomistry » Bromine » PDB 1uhj-1z5m » 1us0 » |
Bromine in PDB 1us0: Human Aldose Reductase in Complex with Nadp+ and the Inhibitor IDD594 at 0.66 AngstromEnzymatic activity of Human Aldose Reductase in Complex with Nadp+ and the Inhibitor IDD594 at 0.66 Angstrom
All present enzymatic activity of Human Aldose Reductase in Complex with Nadp+ and the Inhibitor IDD594 at 0.66 Angstrom:
1.1.1.21; Protein crystallography data
The structure of Human Aldose Reductase in Complex with Nadp+ and the Inhibitor IDD594 at 0.66 Angstrom, PDB code: 1us0
was solved by
E.I.Howard,
R.Sanishvili,
R.E.Cachau,
A.Mitschler,
B.Chevrier,
P.Barth,
V.Lamour,
M.Van Zandt,
E.Sibley,
C.Bon,
D.Moras,
T.R.Schneider,
A.Joachimiak,
A.Podjarny,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 1us0:
The structure of Human Aldose Reductase in Complex with Nadp+ and the Inhibitor IDD594 at 0.66 Angstrom also contains other interesting chemical elements:
Bromine Binding Sites:
The binding sites of Bromine atom in the Human Aldose Reductase in Complex with Nadp+ and the Inhibitor IDD594 at 0.66 Angstrom
(pdb code 1us0). 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 Human Aldose Reductase in Complex with Nadp+ and the Inhibitor IDD594 at 0.66 Angstrom, PDB code: 1us0: Bromine binding site 1 out of 1 in 1us0Go back to Bromine Binding Sites List in 1us0
Bromine binding site 1 out
of 1 in the Human Aldose Reductase in Complex with Nadp+ and the Inhibitor IDD594 at 0.66 Angstrom
Mono view Stereo pair view
Reference:
E.I.Howard,
R.Sanishvili,
R.E.Cachau,
A.Mitschler,
B.Chevrier,
P.Barth,
V.Lamour,
M.Van Zandt,
E.Sibley,
C.Bon,
D.Moras,
T.R.Schneider,
A.Joachimiak,
A.Podjarny.
Ultrahigh Resolution Drug Design I: Details of Interactions in Human Aldose Reductase-Inhibitor Complex at 0.66 A. Proteins V. 55 792 2004.
Page generated: Sat Dec 12 02:04:22 2020
ISSN: ISSN 0887-3585 PubMed: 15146478 DOI: 10.1002/PROT.20015 |
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