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Fluorine in PDB 1pwm: Crystal Structure of Human Aldose Reductase Complexed with Nadp and Fidarestat

Enzymatic activity of Crystal Structure of Human Aldose Reductase Complexed with Nadp and Fidarestat

All present enzymatic activity of Crystal Structure of Human Aldose Reductase Complexed with Nadp and Fidarestat:
1.1.1.21;

Protein crystallography data

The structure of Crystal Structure of Human Aldose Reductase Complexed with Nadp and Fidarestat, PDB code: 1pwm was solved by O.El-Kabbani, C.Darmanin, T.R.Schneider, I.Hazemann, F.Ruiz, M.Oka, A.Joachimiak, C.Schulze-Briese, T.Tomizaki, A.Mitschler, A.Podjarny, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 0.92
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 49.428, 67.042, 47.317, 90.00, 92.09, 90.00
R / Rfree (%) 10.4 / 12.9

Other elements in 1pwm:

The structure of Crystal Structure of Human Aldose Reductase Complexed with Nadp and Fidarestat also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Crystal Structure of Human Aldose Reductase Complexed with Nadp and Fidarestat (pdb code 1pwm). 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 Nadp and Fidarestat, PDB code: 1pwm:

Fluorine binding site 1 out of 1 in 1pwm

Go back to Fluorine Binding Sites List in 1pwm
Fluorine binding site 1 out of 1 in the Crystal Structure of Human Aldose Reductase Complexed with Nadp and Fidarestat


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 Nadp and Fidarestat within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F1320

b:8.2
occ:1.00
 F17 A:FID1320 0.0 8.2 1.0
C14 A:FID1320 1.4 6.8 1.0
C15 A:FID1320 2.3 7.8 1.0
C13 A:FID1320 2.3 6.4 1.0
O A:VAL47 3.1 8.3 0.3
O A:HOH1654 3.2 35.8 1.0
O A:VAL47 3.2 5.6 0.7
O A:HOH1347 3.4 10.2 1.0
O A:HOH1348 3.5 13.5 1.0
NE1 A:TRP20 3.6 5.9 1.0
O A:HOH1346 3.6 8.3 1.0
C16 A:FID1320 3.6 8.1 1.0
C12 A:FID1320 3.6 6.1 1.0
CG1 A:VAL47 3.7 6.4 0.7
CD1 A:TRP20 3.8 5.6 1.0
C A:VAL47 3.8 6.3 0.3
C A:VAL47 3.8 5.3 0.7
CG1 A:VAL47 3.8 5.9 0.3
CG2 A:VAL47 3.9 6.9 0.7
CD1 A:TYR48 3.9 5.1 1.0
CG2 A:VAL47 4.1 6.5 0.3
C11 A:FID1320 4.1 7.2 1.0
CA A:TYR48 4.2 5.6 1.0
N A:TYR48 4.3 5.3 1.0
CB A:VAL47 4.3 5.7 0.7
CB A:VAL47 4.4 6.6 0.3
CE1 A:TYR48 4.5 5.2 1.0
CE2 A:TRP20 4.6 5.8 1.0
O A:HOH1447 4.6 10.3 1.0
CA A:VAL47 4.7 5.5 0.7
CA A:VAL47 4.7 6.0 0.3
O A:HOH1337 4.8 9.3 1.0
C7I A:FID1320 4.9 6.0 1.0
CG A:TRP20 4.9 5.4 1.0
CG A:TYR48 4.9 5.3 1.0

Reference:

O.El-Kabbani, C.Darmanin, T.R.Schneider, I.Hazemann, F.Ruiz, M.Oka, A.Joachimiak, C.Schulze-Briese, T.Tomizaki, A.Mitschler, A.Podjarny. Ultrahigh Resolution Drug Design. II. Atomic Resolution Structures of Human Aldose Reductase Holoenzyme Complexed with Fidarestat and Minalrestat: Implications For the Binding of Cyclic Imide Inhibitors Proteins V. 55 805 2004.
ISSN: ISSN 0887-3585
PubMed: 15146479
DOI: 10.1002/PROT.20001
Page generated: Wed Jul 31 12:21:49 2024

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