Bromine in PDB 4xzl: Crystal Structure of Human AKR1B10 Complexed with Nadp+ and JF0049

The structure of Crystal Structure of Human AKR1B10 Complexed with Nadp+ and JF0049, PDB code: 4xzl 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)	23.55 / 1.70
Space group	P 31
Cell size a, b, c (Å), α, β, γ (°)	79.129, 79.129, 50.146, 90.00, 90.00, 120.00
R / Rfree (%)	20.9 / 23.9

The binding sites of Bromine atom in the Crystal Structure of Human AKR1B10 Complexed with Nadp+ and JF0049 (pdb code 4xzl). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total 4 binding sites of Bromine where determined in the Crystal Structure of Human AKR1B10 Complexed with Nadp+ and JF0049, PDB code: 4xzl:
Jump to Bromine binding site number: 1; 2; 3; 4;

Bromine binding site 1 out of 4 in the Crystal Structure of Human AKR1B10 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 AKR1B10 Complexed with Nadp+ and JF0049 within 5.0Å range: probe atom residue distance (Å) B Occ X:Br402 b:66.6 occ:0.64 BR7 X:F49402 0.0 66.6 0.6 C5 X:F49402 1.9 46.9 0.6 C6 X:F49402 2.8 40.4 0.6 C3 X:F49402 2.9 43.5 0.6 O24 X:F49402 3.0 39.0 0.6 BR6 X:F49402 3.2 50.2 0.6 C25 X:F49402 3.9 43.9 0.6 CD X:ARG125 4.0 31.8 1.0 C4 X:F49402 4.1 37.5 0.6 CG X:GLN303 4.1 50.8 1.0 NE2 X:GLN303 4.1 49.0 1.0 C1 X:F49402 4.2 31.1 0.6 CD X:GLN303 4.3 45.0 1.0 NH1 X:ARG125 4.4 51.4 1.0 O X:GLY129 4.5 36.0 1.0 C2 X:F49402 4.6 43.3 0.6 CB X:GLN303 4.8 39.4 1.0 CG X:ARG125 4.9 34.2 1.0

Bromine binding site 2 out of 4 in the Crystal Structure of Human AKR1B10 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 AKR1B10 Complexed with Nadp+ and JF0049 within 5.0Å range: probe atom residue distance (Å) B Occ X:Br402 b:50.2 occ:0.64 BR6 X:F49402 0.0 50.2 0.6 C6 X:F49402 1.9 40.4 0.6 C5 X:F49402 2.8 46.9 0.6 C4 X:F49402 2.8 37.5 0.6 BR7 X:F49402 3.2 66.6 0.6 BR5 X:F49402 3.3 43.8 0.6 CG X:ARG125 3.9 34.2 1.0 CD X:ARG125 3.9 31.8 1.0 CG X:GLN303 4.0 50.8 1.0 C2 X:F49402 4.1 43.3 0.6 C3 X:F49402 4.2 43.5 0.6 CB X:ALA131 4.4 24.4 1.0 CD1 X:PHE123 4.4 28.4 1.0 O X:GLY129 4.5 36.0 1.0 CB X:GLN303 4.6 39.4 1.0 CB X:PHE123 4.6 22.8 1.0 CA X:ALA131 4.7 26.0 1.0 C1 X:F49402 4.7 31.1 0.6 N X:ALA131 4.8 26.0 1.0 CA X:PHE123 5.0 23.5 1.0

Bromine binding site 3 out of 4 in the Crystal Structure of Human AKR1B10 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 AKR1B10 Complexed with Nadp+ and JF0049 within 5.0Å range: probe atom residue distance (Å) B Occ X:Br402 b:43.8 occ:0.64 BR5 X:F49402 0.0 43.8 0.6 C4 X:F49402 1.9 37.5 0.6 C2 X:F49402 2.8 43.3 0.6 C6 X:F49402 2.8 40.4 0.6 BR4 X:F49402 3.0 54.3 0.6 O X:HOH619 3.2 24.1 1.0 BR6 X:F49402 3.3 50.2 0.6 CE2 X:PHE116 3.4 35.2 1.0 CZ X:PHE116 3.7 27.2 1.0 CD1 X:LEU301 3.9 45.0 1.0 CZ2 X:TRP80 4.0 20.7 1.0 CD1 X:PHE123 4.1 28.4 1.0 C5 X:F49402 4.1 46.9 0.6 CD2 X:LEU301 4.1 32.0 1.0 C1 X:F49402 4.1 31.1 0.6 CH2 X:TRP80 4.2 23.1 1.0 CE1 X:PHE123 4.4 23.6 1.0 CD2 X:PHE116 4.5 33.0 1.0 CG X:LEU301 4.6 32.5 1.0 C3 X:F49402 4.6 43.5 0.6 CE1 X:PHE116 5.0 28.4 1.0

Bromine binding site 4 out of 4 in the Crystal Structure of Human AKR1B10 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 AKR1B10 Complexed with Nadp+ and JF0049 within 5.0Å range: probe atom residue distance (Å) B Occ X:Br402 b:54.3 occ:0.64 BR4 X:F49402 0.0 54.3 0.6 C2 X:F49402 1.9 43.3 0.6 C4 X:F49402 2.8 37.5 0.6 C1 X:F49402 2.9 31.1 0.6 N8 X:F49402 3.0 40.0 0.6 BR5 X:F49402 3.0 43.8 0.6 C7 X:F49402 3.1 39.4 0.6 C10 X:F49402 3.2 36.8 0.6 O X:HOH619 3.3 24.1 1.0 CH2 X:TRP80 3.4 23.1 1.0 O23 X:F49402 3.5 44.6 0.6 C9 X:F49402 3.5 42.6 0.6 CD1 X:LEU301 3.8 45.0 1.0 N12 X:F49402 3.9 39.6 0.6 O18 X:F49402 4.0 42.7 0.6 C6 X:F49402 4.1 40.4 0.6 NE1 X:TRP112 4.2 13.5 0.6 CZ2 X:TRP80 4.2 20.7 1.0 C3 X:F49402 4.2 43.5 0.6 C11 X:F49402 4.2 37.5 0.6 CE1 X:PHE123 4.2 23.6 1.0 O21 X:F49402 4.3 32.8 0.6 C13 X:F49402 4.3 35.9 0.6 CZ3 X:TRP80 4.4 20.8 1.0 CE2 X:TRP112 4.6 23.2 0.6 C5 X:F49402 4.6 46.9 0.6 CD2 X:LEU301 4.7 32.0 1.0 CZ2 X:TRP112 4.8 24.8 0.6 CD1 X:PHE123 4.8 28.4 1.0 C19 X:F49402 4.8 29.7 0.6 CG X:LEU301 4.9 32.5 1.0 CD1 X:TRP112 4.9 24.5 0.6 C20 X:F49402 4.9 22.0 0.6

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