Atomistry » Fluorine » PDB 4pb2-4q0d » 4puu
Atomistry »
  Fluorine »
    PDB 4pb2-4q0d »
      4puu »

Fluorine in PDB 4puu: Human Aldose Reductase Complexed with A Ligand with An Idd Structure (2-(2-Carbamoyl-5-Fluoro-Phenoxy)Acetic Acid) at 1.14 A

Enzymatic activity of Human Aldose Reductase Complexed with A Ligand with An Idd Structure (2-(2-Carbamoyl-5-Fluoro-Phenoxy)Acetic Acid) at 1.14 A

All present enzymatic activity of Human Aldose Reductase Complexed with A Ligand with An Idd Structure (2-(2-Carbamoyl-5-Fluoro-Phenoxy)Acetic Acid) at 1.14 A:
1.1.1.21;

Protein crystallography data

The structure of Human Aldose Reductase Complexed with A Ligand with An Idd Structure (2-(2-Carbamoyl-5-Fluoro-Phenoxy)Acetic Acid) at 1.14 A, PDB code: 4puu was solved by C.Rechlin, A.Heine, G.Klebe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 17.32 / 1.14
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 49.289, 66.394, 47.245, 90.00, 91.82, 90.00
R / Rfree (%) 13.7 / 15.6

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Human Aldose Reductase Complexed with A Ligand with An Idd Structure (2-(2-Carbamoyl-5-Fluoro-Phenoxy)Acetic Acid) at 1.14 A (pdb code 4puu). 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 Human Aldose Reductase Complexed with A Ligand with An Idd Structure (2-(2-Carbamoyl-5-Fluoro-Phenoxy)Acetic Acid) at 1.14 A, PDB code: 4puu:

Fluorine binding site 1 out of 1 in 4puu

Go back to Fluorine Binding Sites List in 4puu
Fluorine binding site 1 out of 1 in the Human Aldose Reductase Complexed with A Ligand with An Idd Structure (2-(2-Carbamoyl-5-Fluoro-Phenoxy)Acetic Acid) at 1.14 A


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Human Aldose Reductase Complexed with A Ligand with An Idd Structure (2-(2-Carbamoyl-5-Fluoro-Phenoxy)Acetic Acid) at 1.14 A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F402

b:13.7
occ:1.00
 F13 A:2WR402 0.0 13.7 1.0
C12 A:2WR402 1.3 11.5 1.0
C10 A:2WR402 2.4 12.4 1.0
C14 A:2WR402 2.4 9.6 1.0
O A:VAL47 3.1 5.9 1.0
O A:HOH544 3.6 14.2 1.0
O A:HOH549 3.6 10.2 1.0
C8 A:2WR402 3.6 11.9 1.0
C1 A:2WR402 3.6 8.2 1.0
C A:VAL47 3.7 5.0 1.0
CG1 A:VAL47 3.7 6.6 1.0
CD1 A:TYR48 3.8 5.5 1.0
NE1 A:TRP20 3.8 6.1 1.0
CD1 A:TRP20 3.9 5.8 1.0
CG2 A:VAL47 4.0 6.8 1.0
CA A:TYR48 4.1 5.7 1.0
C2 A:2WR402 4.1 10.8 1.0
N A:TYR48 4.1 5.0 1.0
CB A:VAL47 4.3 6.2 1.0
CE1 A:TYR48 4.3 5.3 1.0
CA A:VAL47 4.6 5.8 1.0
O A:HOH620 4.7 13.2 1.0
O16 A:2WR402 4.8 7.5 1.0
CG A:TYR48 4.8 5.4 1.0
CE2 A:TRP20 4.8 6.1 1.0
O A:HOH540 4.8 9.6 1.0
CB A:TYR48 5.0 5.6 1.0

Reference:

C.Rechlin, A.Heine, F.Scheer, P.Toth, W.Diederich, G.Klebe. Human Aldose Reductase: How Expensive Is the Opening of the Specificity Pocket? Idd Ligands Under Investigation To Be Published.
Page generated: Sun Dec 13 12:10:59 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy