Bromine in PDB 1us0: Human Aldose Reductase in Complex with Nadp+ and the Inhibitor IDD594 at 0.66 Angstrom

Enzymatic 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:

*Resolution Low / High (Å)*	20.00 / 0.66
*Space group*	P 1 2₁ 1
*Cell size a, b, c (Å), α, β, γ (°)*	49.280, 66.590, 47.260, 90.00, 92.40, 90.00
*R / R_free (%)*	9.4 / 10.3

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:

Fluorine

(F)

2 atoms

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 1us0

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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

A full contact list of Bromine with other atoms in the Br binding site number 1 of Human Aldose Reductase in Complex with Nadp+ and the Inhibitor IDD594 at 0.66 Angstrom within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Br320 b:5.0 occ:0.94	BR8	A:LDT320	0.0	5.0	0.9
	C25	A:LDT320	1.9	4.5	1.0
	C29	A:LDT320	2.8	4.4	1.0
	C28	A:LDT320	2.8	4.5	1.0
	OG1	A:THR113	3.0	4.1	1.0
	CE3	A:TRP111	3.8	3.8	1.0
	CD2	A:TRP111	3.9	3.6	1.0
	CB	A:CYS303	3.9	5.7	1.0
	CG	A:TRP111	3.9	3.5	1.0
	CB	A:TRP111	3.9	3.3	1.0
	CZ	A:PHE115	3.9	4.8	1.0
	CG2	A:THR113	4.0	4.8	1.0
	SG	A:CYS303	4.1	6.2	1.0
	CB	A:THR113	4.1	3.9	1.0
	C27	A:LDT320	4.1	4.2	1.0
	C26	A:LDT320	4.1	4.2	1.0
	CE1	A:PHE115	4.3	4.7	1.0
	CD1	A:TYR309	4.4	5.3	1.0
	CE1	A:TYR309	4.6	5.5	1.0
	CZ3	A:TRP111	4.6	4.3	1.0
	C24	A:LDT320	4.7	4.0	1.0
	CE2	A:TRP111	4.8	4.1	1.0
	CD1	A:TRP111	4.8	4.0	1.0
	SG	A:CYS80	4.8	3.6	1.0

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.
ISSN: ISSN 0887-3585
PubMed: 15146478
DOI: 10.1002/PROT.20015

Page generated: Wed Jul 10 17:27:10 2024

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