Fluorine in PDB 1iei: Crystal Structure of Human Aldose Reductase Complexed with the Inhibitor Zenarestat.

Enzymatic activity of Crystal Structure of Human Aldose Reductase Complexed with the Inhibitor Zenarestat.

All present enzymatic activity of Crystal Structure of Human Aldose Reductase Complexed with the Inhibitor Zenarestat.:
1.1.1.21;

Protein crystallography data

The structure of Crystal Structure of Human Aldose Reductase Complexed with the Inhibitor Zenarestat., PDB code: 1iei was solved by T.Kinoshita, H.Miyake, T.Fujii, S.Takakura, T.Goto, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	10.00 / 2.50
*Space group*	P 1
*Cell size a, b, c (Å), α, β, γ (°)*	40.400, 47.970, 47.660, 76.20, 76.70, 67.50
*R / R_free (%)*	17.8 / 19.9

Other elements in 1iei:

The structure of Crystal Structure of Human Aldose Reductase Complexed with the Inhibitor Zenarestat. also contains other interesting chemical elements:

Bromine	(Br)	1 atom
Chlorine	(Cl)	1 atom

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Crystal Structure of Human Aldose Reductase Complexed with the Inhibitor Zenarestat. (pdb code 1iei). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total only one binding site of Fluorine was determined in the Crystal Structure of Human Aldose Reductase Complexed with the Inhibitor Zenarestat., PDB code: 1iei:

Fluorine binding site 1 out of 1 in 1iei

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Fluorine Binding Sites List in 1iei

Fluorine binding site 1 out of 1 in the Crystal Structure of Human Aldose Reductase Complexed with the Inhibitor Zenarestat.

Mono view

Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Crystal Structure of Human Aldose Reductase Complexed with the Inhibitor Zenarestat. within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:F351 b:13.1 occ:1.00	F35	A:ZES351	0.0	13.1	1.0
	C18	A:ZES351	1.4	7.2	1.0
	C19	A:ZES351	2.3	7.8	1.0
	C15	A:ZES351	2.4	10.1	1.0
	O	A:CYS298	2.5	13.4	1.0
	C14	A:ZES351	2.8	9.9	1.0
	C	A:CYS298	3.1	12.9	1.0
	CB	A:LEU300	3.1	16.9	1.0
	N	A:LEU300	3.2	18.2	1.0
	N	A:ALA299	3.4	12.3	1.0
	CH2	A:TRP111	3.5	11.6	1.0
	C20	A:ZES351	3.5	6.9	1.0
	C	A:ALA299	3.5	18.2	1.0
	C22	A:ZES351	3.6	6.8	1.0
	CA	A:LEU300	3.6	18.9	1.0
	CA	A:ALA299	3.8	15.5	1.0
	CZ2	A:TRP111	3.9	14.9	1.0
	CZ3	A:TRP111	4.0	15.2	1.0
	C21	A:ZES351	4.1	9.3	1.0
	N11	A:ZES351	4.2	8.4	1.0
	CA	A:CYS298	4.3	12.2	1.0
	O	A:ALA299	4.3	21.6	1.0
	CB	A:CYS298	4.4	8.8	1.0
	O33	A:ZES351	4.4	7.1	1.0
	CG	A:LEU300	4.5	16.2	1.0
	OH	A:TYR309	4.6	18.4	1.0
	CE2	A:PHE311	4.7	2.0	1.0
	CD1	A:LEU300	4.7	13.4	1.0
	C	A:LEU300	4.7	19.4	1.0
	CE2	A:TRP111	4.8	13.5	1.0
	C12	A:ZES351	4.8	8.4	1.0
	O	A:LEU300	4.9	21.2	1.0
	CE3	A:TRP111	4.9	15.2	1.0
	O34	A:ZES351	5.0	19.8	1.0

Reference:

T.Kinoshita, H.Miyake, T.Fujii, S.Takakura, T.Goto. The Structure of Human Recombinant Aldose Reductase Complexed with the Potent Inhibitor Zenarestat. Acta Crystallogr.,Sect.D V. 58 622 2002.
ISSN: ISSN 0907-4449
PubMed: 11914486
DOI: 10.1107/S0907444902002378

Page generated: Wed Jul 31 11:36:57 2024

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