Potassium in PDB 1pr9: Human L-Xylulose Reductase Holoenzyme

All present enzymatic activity of Human L-Xylulose Reductase Holoenzyme:
1.1.1.10;

The structure of Human L-Xylulose Reductase Holoenzyme, PDB code: 1pr9 was solved by O.El-Kabbani, S.Ishikura, C.Darmanin, V.Carbone, R.P.-T.Chung, N.Usami, A.Hara, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 1.96
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	74.111, 87.938, 72.883, 90.00, 90.00, 90.00
R / Rfree (%)	17.8 / 22.7

The binding sites of Potassium atom in the Human L-Xylulose Reductase Holoenzyme (pdb code 1pr9). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Human L-Xylulose Reductase Holoenzyme, PDB code: 1pr9:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in the Human L-Xylulose Reductase Holoenzyme


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Human L-Xylulose Reductase Holoenzyme within 5.0Å range: probe atom residue distance (Å) B Occ A:K246 b:47.3 occ:1.00 O4 A:2HP247 2.0 39.6 1.0 P A:2HP247 2.8 36.2 1.0 O1 A:2HP247 2.9 37.5 1.0 O3 A:2HP247 3.2 32.0 1.0 OH A:TYR149 3.7 16.9 1.0 CE2 A:TYR149 3.8 13.2 1.0 C4N A:NAP245 3.8 19.0 1.0 CZ A:TYR149 4.0 19.9 1.0 O7N A:NAP245 4.2 17.4 1.0 C5N A:NAP245 4.2 16.7 1.0 O2 A:2HP247 4.2 24.4 1.0 C3N A:NAP245 4.3 22.6 1.0 NE1 A:TRP191 4.5 60.0 1.0 C7N A:NAP245 4.6 28.2 1.0 OG A:SER136 4.6 14.7 1.0 CD2 A:TYR149 4.7 11.3 1.0 NE2 A:HIS146 4.7 17.8 1.0 CD2 A:HIS146 4.8 15.4 1.0 C6N A:NAP245 4.9 20.8 1.0 C2N A:NAP245 5.0 19.4 1.0

Potassium binding site 2 out of 2 in the Human L-Xylulose Reductase Holoenzyme


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Human L-Xylulose Reductase Holoenzyme within 5.0Å range: probe atom residue distance (Å) B Occ B:K1246 b:54.3 occ:1.00 O4 B:2HP1247 2.0 50.4 1.0 O B:HOH462 2.7 36.4 1.0 O1 B:2HP1247 2.8 45.4 1.0 P B:2HP1247 2.9 48.6 1.0 O B:HOH459 3.0 35.0 1.0 CE2 B:TYR149 3.6 18.4 1.0 OH B:TYR149 3.7 16.3 1.0 C4N B:NAP1245 3.7 20.5 1.0 O3 B:2HP1247 3.8 60.0 1.0 CZ B:TYR149 4.0 17.4 1.0 O7N B:NAP1245 4.0 17.7 1.0 C5N B:NAP1245 4.0 23.6 1.0 O2 B:2HP1247 4.2 26.4 1.0 C3N B:NAP1245 4.2 15.9 1.0 OG B:SER136 4.5 15.5 1.0 C7N B:NAP1245 4.6 19.2 1.0 CD2 B:TYR149 4.6 14.5 1.0 NE1 B:TRP191 4.7 44.2 1.0 C6N B:NAP1245 4.7 16.2 1.0 SD B:MET186 4.8 33.0 1.0 CD2 B:HIS146 4.9 13.1 1.0 NE2 B:HIS146 4.9 16.6 1.0 C2N B:NAP1245 4.9 16.8 1.0 O B:HOH469 4.9 34.3 1.0

O.El-Kabbani, S.Ishikura, C.Darmanin, V.Carbone, R.P.-T.Chung, N.Usami, A.Hara. Crystal Structure of Human L-Xylulose Reductase Holoenzyme: Probing the Role of ASN107 with Site-Directed Mutagenesis Proteins V. 55 724 2004.
ISSN: ISSN 0887-3585
PubMed: 15103634
DOI: 10.1002/PROT.20047