Atomistry » Bromine » PDB 4x6i-4z8b » 4xzi
Atomistry »
  Bromine »
    PDB 4x6i-4z8b »
      4xzi »

Bromine in PDB 4xzi: Crystal Structure of Human Aldose Reductase Complexed with Nadp+ and JF0049

Enzymatic activity of Crystal Structure of Human Aldose Reductase Complexed with Nadp+ and JF0049

All present enzymatic activity of Crystal Structure of Human Aldose Reductase Complexed with Nadp+ and JF0049:
1.1.1.21;

Protein crystallography data

The structure of Crystal Structure of Human Aldose Reductase Complexed with Nadp+ and JF0049, PDB code: 4xzi was solved by A.Cousido-Siah, F.X.Ruiz, A.Mitschler, M.Dominguez, A.R.De Lera, J.Farres, X.Pares, A.Podjarny, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 37.03 / 2.45
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 74.065, 84.780, 105.239, 90.00, 90.00, 90.00
R / Rfree (%) 21.9 / 29

Bromine Binding Sites:

The binding sites of Bromine atom in the Crystal Structure of Human Aldose Reductase Complexed with Nadp+ and JF0049 (pdb code 4xzi). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total 8 binding sites of Bromine where determined in the Crystal Structure of Human Aldose Reductase Complexed with Nadp+ and JF0049, PDB code: 4xzi:
Jump to Bromine binding site number: 1; 2; 3; 4; 5; 6; 7; 8;

Bromine binding site 1 out of 8 in 4xzi

Go back to Bromine Binding Sites List in 4xzi
Bromine binding site 1 out of 8 in the Crystal Structure of Human Aldose Reductase Complexed with Nadp+ and JF0049


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Crystal Structure of Human Aldose Reductase Complexed with Nadp+ and JF0049 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br402

b:74.5
occ:0.60
BR7 A:F49402 0.0 74.5 0.6
C5 A:F49402 1.9 20.2 0.6
C6 A:F49402 2.8 27.5 0.6
C3 A:F49402 2.8 29.7 0.6
O24 A:F49402 3.0 12.1 0.6
BR6 A:F49402 3.2 71.1 0.6
CD1 A:PHE122 3.3 39.5 0.4
C25 A:F49402 3.4 16.8 0.6
OG A:SER302 3.4 34.3 1.0
CG A:PHE122 3.4 34.8 0.4
CB A:PHE122 3.6 29.1 0.4
CB A:PHE122 3.6 29.2 0.6
CG A:PHE122 3.8 35.5 0.6
CB A:SER302 3.9 11.6 1.0
CE1 A:PHE122 4.0 39.3 0.4
C4 A:F49402 4.0 33.8 0.6
C1 A:F49402 4.1 30.1 0.6
CD1 A:PHE122 4.1 39.3 0.6
CD2 A:PHE122 4.2 38.1 0.4
CD1 A:LEU124 4.3 33.7 1.0
CD2 A:PHE122 4.5 38.3 0.6
C2 A:F49402 4.6 37.5 0.6
CD2 A:LEU124 4.6 28.6 1.0
CG1 A:VAL130 4.7 23.6 1.0
CZ A:PHE122 4.7 36.4 0.4
CG A:LEU124 4.7 21.9 1.0
CE2 A:PHE122 4.8 37.4 0.4
CE1 A:PHE122 4.9 34.8 0.6
CA A:PHE122 5.0 26.8 0.6

Bromine binding site 2 out of 8 in 4xzi

Go back to Bromine Binding Sites List in 4xzi
Bromine binding site 2 out of 8 in the Crystal Structure of Human Aldose Reductase Complexed with Nadp+ and JF0049


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 2 of Crystal Structure of Human Aldose Reductase Complexed with Nadp+ and JF0049 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br402

b:31.8
occ:0.40
BR7 A:F49402 0.0 31.8 0.4
C5 A:F49402 1.9 29.3 0.4
C3 A:F49402 2.8 32.9 0.4
C6 A:F49402 2.9 20.9 0.4
O24 A:F49402 2.9 29.6 0.4
C25 A:F49402 3.3 23.8 0.4
BR4 A:F49402 3.4 69.8 0.6
BR6 A:F49402 3.4 19.3 0.4
NE1 A:TRP20 3.6 9.7 1.0
C1 A:F49402 4.1 30.2 0.4
C4 A:F49402 4.2 26.9 0.4
BR5 A:F49402 4.3 32.1 0.6
CE2 A:TRP20 4.3 18.5 1.0
CZ2 A:TRP20 4.4 18.5 1.0
CG A:PRO218 4.5 13.7 1.0
CD1 A:TRP20 4.6 14.4 1.0
CG A:LYS21 4.6 12.8 0.1
C2 A:F49402 4.6 22.9 0.4
CG A:LYS21 4.7 12.8 0.9
NZ A:LYS21 4.8 12.8 0.1
CD A:PRO218 4.9 12.8 1.0

Bromine binding site 3 out of 8 in 4xzi

Go back to Bromine Binding Sites List in 4xzi
Bromine binding site 3 out of 8 in the Crystal Structure of Human Aldose Reductase Complexed with Nadp+ and JF0049


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 3 of Crystal Structure of Human Aldose Reductase Complexed with Nadp+ and JF0049 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br402

b:71.1
occ:0.60
BR6 A:F49402 0.0 71.1 0.6
C6 A:F49402 1.9 27.5 0.6
C4 A:F49402 2.8 33.8 0.6
C5 A:F49402 2.8 20.2 0.6
CZ A:PHE122 3.2 36.4 0.4
CE1 A:PHE122 3.2 39.3 0.4
BR7 A:F49402 3.2 74.5 0.6
BR5 A:F49402 3.3 32.1 0.6
CE2 A:PHE122 3.7 37.4 0.4
CD1 A:PHE122 3.7 39.5 0.4
CE1 A:PHE122 3.9 34.8 0.6
CD1 A:PHE122 4.1 39.3 0.6
CZ A:PHE122 4.1 37.7 0.6
C2 A:F49402 4.1 37.5 0.6
CD2 A:PHE122 4.1 38.1 0.4
C3 A:F49402 4.2 29.7 0.6
CG A:PHE122 4.2 34.8 0.4
CE2 A:PHE122 4.4 39.3 0.6
CG A:PHE122 4.4 35.5 0.6
CD2 A:PHE122 4.5 38.3 0.6
C1 A:F49402 4.7 30.1 0.6

Bromine binding site 4 out of 8 in 4xzi

Go back to Bromine Binding Sites List in 4xzi
Bromine binding site 4 out of 8 in the Crystal Structure of Human Aldose Reductase Complexed with Nadp+ and JF0049


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 4 of Crystal Structure of Human Aldose Reductase Complexed with Nadp+ and JF0049 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br402

b:19.3
occ:0.40
BR6 A:F49402 0.0 19.3 0.4
C6 A:F49402 1.9 20.9 0.4
C4 A:F49402 2.8 26.9 0.4
C5 A:F49402 2.9 29.3 0.4
BR5 A:F49402 3.1 44.9 0.4
BR7 A:F49402 3.4 31.8 0.4
NE2 A:GLN49 3.7 28.0 1.0
C2 A:F49402 4.1 22.9 0.4
C3 A:F49402 4.1 32.9 0.4
C1 A:F49402 4.6 30.2 0.4
CE2 A:PHE122 4.7 39.3 0.6
BR5 A:F49402 4.7 32.1 0.6
BR4 A:F49402 4.8 69.8 0.6
CD A:GLN49 4.9 15.2 1.0

Bromine binding site 5 out of 8 in 4xzi

Go back to Bromine Binding Sites List in 4xzi
Bromine binding site 5 out of 8 in the Crystal Structure of Human Aldose Reductase Complexed with Nadp+ and JF0049


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 5 of Crystal Structure of Human Aldose Reductase Complexed with Nadp+ and JF0049 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br402

b:32.1
occ:0.60
BR5 A:F49402 0.0 32.1 0.6
C4 A:F49402 1.9 33.8 0.6
C2 A:F49402 2.8 37.5 0.6
C6 A:F49402 2.8 27.5 0.6
BR4 A:F49402 3.0 69.8 0.6
BR6 A:F49402 3.3 71.1 0.6
C25 A:F49402 3.6 23.8 0.4
C5 A:F49402 3.6 29.3 0.4
C3 A:F49402 3.8 32.9 0.4
C6 A:F49402 3.8 20.9 0.4
CE2 A:PHE122 4.1 37.4 0.4
C5 A:F49402 4.1 20.2 0.6
C1 A:F49402 4.1 30.1 0.6
C1 A:F49402 4.1 30.2 0.4
CE2 A:PHE122 4.1 39.3 0.6
C4 A:F49402 4.2 26.9 0.4
O24 A:F49402 4.3 29.6 0.4
BR7 A:F49402 4.3 31.8 0.4
C2 A:F49402 4.3 22.9 0.4
CZ A:PHE122 4.4 37.7 0.6
CZ A:PHE122 4.4 36.4 0.4
C3 A:F49402 4.7 29.7 0.6
BR6 A:F49402 4.7 19.3 0.4
CD2 A:PHE122 4.8 38.1 0.4
CZ3 A:TRP219 4.8 24.3 1.0
CD2 A:PHE122 4.8 38.3 0.6
CG A:PRO218 4.9 13.7 1.0
O18 A:F49402 5.0 23.4 0.4

Bromine binding site 6 out of 8 in 4xzi

Go back to Bromine Binding Sites List in 4xzi
Bromine binding site 6 out of 8 in the Crystal Structure of Human Aldose Reductase Complexed with Nadp+ and JF0049


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 6 of Crystal Structure of Human Aldose Reductase Complexed with Nadp+ and JF0049 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br402

b:44.9
occ:0.40
BR5 A:F49402 0.0 44.9 0.4
C4 A:F49402 1.9 26.9 0.4
CE2 A:PHE122 2.7 39.3 0.6
C6 A:F49402 2.8 20.9 0.4
C2 A:F49402 2.9 22.9 0.4
BR6 A:F49402 3.1 19.3 0.4
BR4 A:F49402 3.3 28.4 0.4
NE2 A:GLN49 3.4 28.0 1.0
CZ A:PHE122 3.5 37.7 0.6
CD2 A:PHE122 3.5 38.3 0.6
CE2 A:PHE122 3.6 37.4 0.4
CD2 A:PHE122 3.8 38.1 0.4
CD2 A:PHE121 3.9 37.2 1.0
CB A:PHE121 4.1 13.3 1.0
C5 A:F49402 4.1 29.3 0.4
C1 A:F49402 4.1 30.2 0.4
CG A:PHE121 4.4 22.0 1.0
CD A:GLN49 4.5 15.2 1.0
C3 A:F49402 4.6 32.9 0.4
CE1 A:PHE122 4.7 34.8 0.6
CG A:PHE122 4.7 35.5 0.6
CZ A:PHE122 4.8 36.4 0.4
CE2 A:PHE121 4.9 21.8 1.0
OE1 A:GLN49 5.0 18.9 1.0

Bromine binding site 7 out of 8 in 4xzi

Go back to Bromine Binding Sites List in 4xzi
Bromine binding site 7 out of 8 in the Crystal Structure of Human Aldose Reductase Complexed with Nadp+ and JF0049


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 7 of Crystal Structure of Human Aldose Reductase Complexed with Nadp+ and JF0049 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br402

b:69.8
occ:0.60
BR4 A:F49402 0.0 69.8 0.6
C3 A:F49402 1.2 32.9 0.4
O24 A:F49402 1.5 29.6 0.4
C25 A:F49402 1.7 23.8 0.4
C1 A:F49402 1.7 30.2 0.4
C2 A:F49402 1.9 37.5 0.6
C5 A:F49402 2.2 29.3 0.4
C7 A:F49402 2.5 23.0 0.4
C4 A:F49402 2.7 33.8 0.6
C2 A:F49402 2.8 22.9 0.4
N8 A:F49402 2.8 20.2 0.4
C1 A:F49402 2.9 30.1 0.6
BR5 A:F49402 3.0 32.1 0.6
C6 A:F49402 3.1 20.9 0.4
C9 A:F49402 3.2 22.6 0.4
N8 A:F49402 3.3 22.2 0.6
O18 A:F49402 3.3 23.4 0.4
C7 A:F49402 3.3 20.9 0.6
C4 A:F49402 3.3 26.9 0.4
BR7 A:F49402 3.4 31.8 0.4
C10 A:F49402 3.4 19.4 0.6
O23 A:F49402 3.5 21.8 0.6
C10 A:F49402 3.5 19.8 0.4
O23 A:F49402 3.9 21.4 0.4
C9 A:F49402 3.9 22.7 0.6
C6 A:F49402 4.0 27.5 0.6
N12 A:F49402 4.1 19.6 0.6
C11 A:F49402 4.2 20.3 0.4
C3 A:F49402 4.2 29.7 0.6
BR4 A:F49402 4.3 28.4 0.4
N12 A:F49402 4.4 18.4 0.4
O18 A:F49402 4.5 20.1 0.6
CZ3 A:TRP219 4.5 24.3 1.0
NE1 A:TRP20 4.6 9.7 1.0
C5 A:F49402 4.6 20.2 0.6
CZ2 A:TRP20 4.6 18.5 1.0
C11 A:F49402 4.6 19.2 0.6
C13 A:F49402 4.7 16.3 0.6
C13 A:F49402 4.7 16.8 0.4
BR6 A:F49402 4.8 19.3 0.4
CE2 A:PHE122 4.9 39.3 0.6
C19 A:F49402 4.9 14.7 0.6
CE2 A:TRP20 4.9 18.5 1.0

Bromine binding site 8 out of 8 in 4xzi

Go back to Bromine Binding Sites List in 4xzi
Bromine binding site 8 out of 8 in the Crystal Structure of Human Aldose Reductase Complexed with Nadp+ and JF0049


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 8 of Crystal Structure of Human Aldose Reductase Complexed with Nadp+ and JF0049 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br402

b:28.4
occ:0.40
BR4 A:F49402 0.0 28.4 0.4
C2 A:F49402 1.9 22.9 0.4
CD2 A:PHE122 2.6 38.3 0.6
C1 A:F49402 2.8 30.2 0.4
C4 A:F49402 2.8 26.9 0.4
C7 A:F49402 2.9 23.0 0.4
CE2 A:PHE122 3.2 39.3 0.6
CD2 A:PHE122 3.2 38.1 0.4
BR5 A:F49402 3.3 44.9 0.4
CB A:PHE121 3.5 13.3 1.0
C1 A:F49402 3.6 30.1 0.6
C7 A:F49402 3.6 20.9 0.6
CG2 A:VAL47 3.7 12.1 1.0
CZ2 A:TRP79 3.8 8.3 1.0
CG A:PHE122 3.8 35.5 0.6
C2 A:F49402 3.8 37.5 0.6
CE2 A:PHE122 4.1 37.4 0.4
C6 A:F49402 4.1 20.9 0.4
C3 A:F49402 4.1 32.9 0.4
CG A:PHE122 4.1 34.8 0.4
C3 A:F49402 4.1 29.7 0.6
CB A:PHE122 4.1 29.1 0.4
CB A:PHE122 4.2 29.2 0.6
C A:PHE121 4.2 13.2 1.0
N A:PHE122 4.2 9.2 1.0
BR4 A:F49402 4.3 69.8 0.6
O23 A:F49402 4.3 21.8 0.6
CE2 A:TRP79 4.3 12.6 1.0
N8 A:F49402 4.4 20.2 0.4
CH2 A:TRP79 4.4 9.8 1.0
CG A:PHE121 4.5 22.0 1.0
O A:PHE121 4.5 11.2 1.0
C4 A:F49402 4.5 33.8 0.6
CA A:PHE121 4.5 12.3 1.0
NE1 A:TRP79 4.5 10.5 1.0
CZ A:PHE122 4.6 37.7 0.6
C5 A:F49402 4.6 29.3 0.4
O24 A:F49402 4.6 12.1 0.6
CA A:PHE122 4.7 26.8 0.6
C5 A:F49402 4.8 20.2 0.6
CA A:PHE122 4.8 26.7 0.4
N8 A:F49402 4.8 22.2 0.6
O23 A:F49402 4.9 21.4 0.4
C6 A:F49402 4.9 27.5 0.6
CD1 A:PHE122 5.0 39.3 0.6

Reference:

F.X.Ruiz, A.Cousido-Siah, S.Porte, M.Dominguez, I.Crespo, C.Rechlin, A.Mitschler, A.R.De Lera, M.J.Martin, J.A.De La Fuente, G.Klebe, X.Pares, J.Farres, A.Podjarny. Structural Determinants of the Selectivity of 3-Benzyluracil-1-Acetic Acids Toward Human Enzymes Aldose Reductase and AKR1B10. Chemmedchem V. 10 1989 2015.
ISSN: ESSN 1860-7187
PubMed: 26549844
DOI: 10.1002/CMDC.201500393
Page generated: Mon Jul 7 07:49:48 2025

Last articles

Br in 6TVN
Br in 6U5M
Br in 6TU4
Br in 6U5Y
Br in 6TZR
Br in 6TZS
Br in 6TLL
Br in 6TQD
Br in 6TS9
Br in 6TQG
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy