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Fluorine in PDB 2agt: Aldose Reductase Mutant Leu 300 Pro Complexed with Fidarestat

Enzymatic activity of Aldose Reductase Mutant Leu 300 Pro Complexed with Fidarestat

All present enzymatic activity of Aldose Reductase Mutant Leu 300 Pro Complexed with Fidarestat:
1.1.1.21;

Protein crystallography data

The structure of Aldose Reductase Mutant Leu 300 Pro Complexed with Fidarestat, PDB code: 2agt was solved by T.Petrova, H.Steuber, I.Hazemann, A.Cousido-Siah, A.Mitschler, R.Chung, M.Oka, G.Klebe, O.El-Kabbani, 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 / 1.00
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 49.118, 66.724, 47.092, 90.00, 92.79, 90.00
R / Rfree (%) 10.5 / 12.9

Other elements in 2agt:

The structure of Aldose Reductase Mutant Leu 300 Pro Complexed with Fidarestat also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Aldose Reductase Mutant Leu 300 Pro Complexed with Fidarestat (pdb code 2agt). 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 Aldose Reductase Mutant Leu 300 Pro Complexed with Fidarestat, PDB code: 2agt:

Fluorine binding site 1 out of 1 in 2agt

Go back to Fluorine Binding Sites List in 2agt
Fluorine binding site 1 out of 1 in the Aldose Reductase Mutant Leu 300 Pro Complexed with Fidarestat


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Aldose Reductase Mutant Leu 300 Pro Complexed with Fidarestat within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F320

b:8.0
occ:1.00
F17 A:FID320 0.0 8.0 1.0
C14 A:FID320 1.4 5.8 1.0
C15 A:FID320 2.3 7.0 1.0
C13 A:FID320 2.3 5.1 1.0
O A:VAL47 2.9 2.2 0.3
O A:VAL47 3.2 4.6 0.7
O A:HOH4027 3.4 8.4 1.0
O A:HOH4026 3.5 6.5 1.0
O A:HOH4539 3.5 42.8 1.0
O A:HOH4028 3.5 14.8 1.0
C16 A:FID320 3.6 7.7 1.0
C12 A:FID320 3.6 4.5 1.0
NE1 A:TRP20 3.6 4.0 1.0
C A:VAL47 3.6 2.1 0.3
CG1 A:VAL47 3.7 2.1 0.3
C A:VAL47 3.7 4.1 0.7
CG1 A:VAL47 3.7 5.7 0.7
CG2 A:VAL47 3.8 6.2 0.7
CD1 A:TRP20 3.8 3.9 1.0
CG2 A:VAL47 3.9 2.0 0.3
CD1 A:TYR48 3.9 3.4 1.0
C11 A:FID320 4.1 5.9 1.0
CA A:TYR48 4.1 3.5 1.0
N A:TYR48 4.2 3.1 1.0
CB A:VAL47 4.2 4.0 0.7
CB A:VAL47 4.2 3.5 0.3
O A:HOH4152 4.5 7.9 1.0
CE1 A:TYR48 4.5 3.2 1.0
CA A:VAL47 4.6 3.6 0.7
CA A:VAL47 4.6 3.7 0.3
CE2 A:TRP20 4.7 3.8 1.0
O A:HOH4017 4.9 7.1 1.0
C7I A:FID320 4.9 4.0 1.0
CG A:TRP20 4.9 3.4 1.0
CG A:TYR48 4.9 3.1 1.0

Reference:

T.Petrova, H.Steuber, I.Hazemann, A.Cousido-Siah, A.Mitschler, R.Chung, M.Oka, G.Klebe, O.El-Kabbani, A.Joachimiak, A.Podjarny. Factorizing Selectivity Determinants of Inhibitor Binding Toward Aldose and Aldehyde Reductases: Structural and Thermodynamic Properties of the Aldose Reductase Mutant LEU300PRO-Fidarestat Complex J.Med.Chem. V. 48 5659 2005.
ISSN: ISSN 0022-2623
PubMed: 16134934
DOI: 10.1021/JM050424+
Page generated: Sun Dec 13 11:34:45 2020

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