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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

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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

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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

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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

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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

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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

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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

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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

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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

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