Bromine in PDB 2i17: Human Aldose Reductase in Complex with Nadp+ and the Inhibitor IDD594 at Temperature of 60K

Enzymatic activity of Human Aldose Reductase in Complex with Nadp+ and the Inhibitor IDD594 at Temperature of 60K

All present enzymatic activity of Human Aldose Reductase in Complex with Nadp+ and the Inhibitor IDD594 at Temperature of 60K:
1.1.1.21;

Protein crystallography data

The structure of Human Aldose Reductase in Complex with Nadp+ and the Inhibitor IDD594 at Temperature of 60K, PDB code: 2i17 was solved by T.Petrova, S.Ginell, A.Mitshler, I.Hasemann, T.Schneider, A.Cousido, V.Y.Lunin, A.Joachimiak, A.Podjarny, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	50.00 / 0.81
*Space group*	P 1 2₁ 1
*Cell size a, b, c (Å), α, β, γ (°)*	49.214, 66.701, 47.307, 90.00, 92.27, 90.00
*R / R_free (%)*	8.1 / 9.1

Other elements in 2i17:

The structure of Human Aldose Reductase in Complex with Nadp+ and the Inhibitor IDD594 at Temperature of 60K 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 Temperature of 60K (pdb code 2i17). 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 Temperature of 60K, PDB code: 2i17:

Bromine binding site 1 out of 1 in 2i17

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Bromine Binding Sites List in 2i17

Bromine binding site 1 out of 1 in the Human Aldose Reductase in Complex with Nadp+ and the Inhibitor IDD594 at Temperature of 60K

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 Temperature of 60K within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Br321 b:4.2 occ:0.94	BR8	A:LDT321	0.0	4.2	0.9
	C25	A:LDT321	1.9	4.0	1.0
	C29	A:LDT321	2.8	4.0	1.0
	C28	A:LDT321	2.8	4.2	1.0
	OG1	A:THR114	3.0	3.8	1.0
	CE3	A:TRP112	3.8	3.5	1.0
	CD2	A:TRP112	3.9	3.4	1.0
	CB	A:CYS304	3.9	5.5	1.0
	CG	A:TRP112	3.9	3.3	1.0
	CB	A:TRP112	3.9	3.2	1.0
	CZ	A:PHE116	3.9	4.2	1.0
	CG2	A:THR114	4.0	4.3	1.0
	SG	A:CYS304	4.1	5.8	1.0
	CB	A:THR114	4.1	3.7	1.0
	C27	A:LDT321	4.1	4.0	1.0
	C26	A:LDT321	4.1	3.9	1.0
	CE1	A:PHE116	4.3	4.1	1.0
	CD1	A:TYR310	4.4	5.1	1.0
	CE1	A:TYR310	4.6	5.3	1.0
	CZ3	A:TRP112	4.6	3.9	1.0
	C24	A:LDT321	4.7	3.9	1.0
	CD1	A:TRP112	4.8	3.7	1.0
	CE2	A:TRP112	4.8	3.8	1.0
	SG	A:CYS81	4.8	3.2	1.0

Reference:

T.Petrova, S.Ginell, A.Mitschler, I.Hazemann, T.Schneider, A.Cousido, V.Y.Lunin, A.Joachimiak, A.Podjarny. Ultrahigh-Resolution Study of Protein Atomic Displacement Parameters at Cryotemperatures Obtained with A Helium Cryostat. Acta Crystallogr.,Sect.D V. 62 1535 2006.
ISSN: ISSN 0907-4449
PubMed: 17139089
DOI: 10.1107/S0907444906041035

Page generated: Wed Jul 10 18:09:54 2024

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