Bromine in PDB 5lix: Crystal Structure of Human AKR1B10 Complexed with Nadp+ and the Inhibitor MK184

The structure of Crystal Structure of Human AKR1B10 Complexed with Nadp+ and the Inhibitor MK184, PDB code: 5lix was solved by A.Cousido-Siah, F.X.Ruiz, A.Mitschler, J.Fanfrlik, M.Kamlar, J.Vesely, P.Hobza, A.Podjarny, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	23.10 / 1.95
Space group	P 31
Cell size a, b, c (Å), α, β, γ (°)	79.565, 79.565, 50.061, 90.00, 90.00, 120.00
R / Rfree (%)	19.5 / 24.3

The structure of Crystal Structure of Human AKR1B10 Complexed with Nadp+ and the Inhibitor MK184 also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Bromine atom in the Crystal Structure of Human AKR1B10 Complexed with Nadp+ and the Inhibitor MK184 (pdb code 5lix). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total 3 binding sites of Bromine where determined in the Crystal Structure of Human AKR1B10 Complexed with Nadp+ and the Inhibitor MK184, PDB code: 5lix:
Jump to Bromine binding site number: 1; 2; 3;

Bromine binding site 1 out of 3 in the Crystal Structure of Human AKR1B10 Complexed with Nadp+ and the Inhibitor MK184


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 the Inhibitor MK184 within 5.0Å range: probe atom residue distance (Å) B Occ X:Br402 b:50.4 occ:0.60 BR1 X:MK4402 0.0 50.4 0.6 C02 X:MK4402 1.9 39.5 0.6 C09 X:MK4402 2.8 40.0 0.6 C03 X:MK4402 2.9 40.9 0.6 O X:HOH549 2.9 47.9 0.4 C10 X:MK4402 3.0 19.3 0.6 OH X:TYR210 3.3 26.3 1.0 O7N X:NAP401 3.5 28.8 1.0 N11 X:MK4402 3.5 34.5 0.6 C4N X:NAP401 3.8 38.6 1.0 CD2 X:LEU301 3.8 51.5 0.4 CB X:CYS299 4.0 43.6 1.0 O21 X:MK4402 4.0 40.8 0.6 CZ X:TYR210 4.1 28.9 1.0 C07 X:MK4402 4.1 36.4 0.6 C04 X:MK4402 4.1 42.0 0.6 O X:CYS299 4.2 48.5 1.0 OD1 X:ASN161 4.2 32.1 1.0 C12 X:MK4402 4.2 37.4 0.6 ND2 X:ASN161 4.3 25.5 1.0 O13 X:MK4402 4.4 39.5 0.6 C7N X:NAP401 4.4 37.8 1.0 C22 X:MK4402 4.4 34.9 0.6 CD1 X:LEU302 4.5 45.8 0.4 CG X:ASN161 4.5 30.9 1.0 C3N X:NAP401 4.6 37.3 1.0 CE1 X:TYR210 4.6 27.6 1.0 C06 X:MK4402 4.6 46.3 0.6 O24 X:MK4402 4.6 30.0 0.6 C5N X:NAP401 4.7 28.3 1.0 C X:CYS299 4.8 46.3 1.0 CZ3 X:TRP112 4.8 25.7 1.0 CE2 X:TYR210 4.9 24.3 1.0 C23 X:MK4402 4.9 37.3 0.6 CA X:CYS299 5.0 45.5 1.0 CE3 X:TRP112 5.0 31.4 1.0

Bromine binding site 2 out of 3 in the Crystal Structure of Human AKR1B10 Complexed with Nadp+ and the Inhibitor MK184


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 the Inhibitor MK184 within 5.0Å range: probe atom residue distance (Å) B Occ X:Br402 b:53.2 occ:0.60 BR5 X:MK4402 0.0 53.2 0.6 C04 X:MK4402 1.9 42.0 0.6 C06 X:MK4402 2.9 46.3 0.6 C03 X:MK4402 2.9 40.9 0.6 N X:LEU302 3.0 48.9 0.4 N X:LEU302 3.0 52.1 0.6 CD1 X:LEU302 3.1 45.8 0.4 OD1 X:ASN300 3.1 57.8 1.0 N X:LEU301 3.2 51.0 0.4 N X:LEU301 3.2 51.0 0.6 CA X:LEU302 3.3 50.1 0.6 O X:LEU302 3.5 45.5 0.4 C X:ASN300 3.6 53.4 1.0 CB X:LEU302 3.6 43.0 0.4 C X:LEU301 3.6 53.3 0.4 CH2 X:TRP112 3.6 37.0 1.0 CA X:LEU302 3.6 47.5 0.4 C X:LEU301 3.7 54.0 0.6 CA X:ASN300 3.7 51.4 1.0 CA X:LEU301 3.9 50.1 0.4 CE2 X:PHE312 3.9 39.3 1.0 CA X:LEU301 3.9 50.1 0.6 CG X:LEU302 3.9 42.4 0.4 C X:LEU302 3.9 47.9 0.4 CB X:LEU302 4.0 46.9 0.6 CG X:ASN300 4.1 62.3 1.0 CZ2 X:TRP112 4.1 32.7 1.0 C07 X:MK4402 4.2 36.4 0.6 C02 X:MK4402 4.2 39.5 0.6 CD2 X:PHE312 4.2 36.4 1.0 OH X:TYR310 4.2 38.5 1.0 O X:ASN300 4.3 50.2 1.0 CZ3 X:TRP112 4.3 25.7 1.0 O X:LEU301 4.4 53.5 0.4 CB X:LEU301 4.4 49.7 0.6 C X:LEU302 4.5 50.6 0.6 CB X:ASN300 4.5 52.7 1.0 CE1 X:TYR310 4.6 36.4 1.0 CB X:LEU301 4.6 49.3 0.4 O X:LEU301 4.6 51.1 0.6 O X:CYS299 4.6 48.5 1.0 C09 X:MK4402 4.7 40.0 0.6 O X:LEU302 4.8 51.4 0.6 N X:ASN300 4.8 51.5 1.0 CZ X:TYR310 4.9 31.9 1.0

Bromine binding site 3 out of 3 in the Crystal Structure of Human AKR1B10 Complexed with Nadp+ and the Inhibitor MK184


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 the Inhibitor MK184 within 5.0Å range: probe atom residue distance (Å) B Occ X:Br402 b:46.4 occ:0.60 BR8 X:MK4402 0.0 46.4 0.6 CD2 X:LEU302 1.0 40.8 0.4 C07 X:MK4402 1.9 36.4 0.6 CG X:LEU302 2.1 42.4 0.4 CD1 X:LEU302 2.6 45.8 0.4 C06 X:MK4402 2.8 46.3 0.6 C09 X:MK4402 3.0 40.0 0.6 CB X:LEU302 3.4 43.0 0.4 C10 X:MK4402 3.4 19.3 0.6 CG X:TRP112 3.6 28.1 1.0 CD2 X:TRP112 3.6 31.0 1.0 O13 X:MK4402 3.7 39.5 0.6 CD1 X:TRP112 3.9 30.8 1.0 CZ X:PHE116 3.9 36.5 1.0 CE2 X:PHE116 3.9 34.3 1.0 CE2 X:TRP112 3.9 31.2 1.0 CH2 X:TRP80 3.9 29.5 1.0 NE1 X:TRP112 4.0 34.2 1.0 CB X:TRP112 4.1 25.7 1.0 N11 X:MK4402 4.1 34.5 0.6 CE3 X:TRP112 4.1 31.4 1.0 C04 X:MK4402 4.1 42.0 0.6 C12 X:MK4402 4.2 37.4 0.6 C02 X:MK4402 4.2 39.5 0.6 CZ2 X:TRP80 4.6 31.0 1.0 CA X:LEU302 4.6 47.5 0.4 CZ2 X:TRP112 4.6 32.7 1.0 CZ3 X:TRP80 4.6 28.8 1.0 C03 X:MK4402 4.7 40.9 0.6 CZ3 X:TRP112 4.7 25.7 1.0 N X:LEU302 4.9 48.9 0.4 CH2 X:TRP112 5.0 37.0 1.0

A.Cousido-Siah, F.X.Ruiz, J.Fanfrlik, J.Gimenez-Dejoz, A.Mitschler, M.Kamlar, J.Vesely, H.Ajani, X.Pares, J.Farres, P.Hobza, A.D.Podjarny. IDD388 Polyhalogenated Derivatives As Probes For An Improved Structure-Based Selectivity of AKR1B10 Inhibitors. Acs Chem.Biol. V. 11 2693 2016.
ISSN: ESSN 1554-8937
PubMed: 27359042
DOI: 10.1021/ACSCHEMBIO.6B00382