Potassium in PDB 4zvj: Structure of Human Triose Phosphate Isomerase K13M

All present enzymatic activity of Structure of Human Triose Phosphate Isomerase K13M:
5.3.1.1;

The structure of Structure of Human Triose Phosphate Isomerase K13M, PDB code: 4zvj was solved by C.G.Amrich, C.Smith, A.Heroux, A.P.Vandemark, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	12.00 / 1.70
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	65.066, 73.530, 92.816, 90.00, 90.00, 90.00
R / Rfree (%)	14.7 / 18.7

The structure of Structure of Human Triose Phosphate Isomerase K13M also contains other interesting chemical elements:

Sodium

(Na)

1 atom

The binding sites of Potassium atom in the Structure of Human Triose Phosphate Isomerase K13M (pdb code 4zvj). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total only one binding site of Potassium was determined in the Structure of Human Triose Phosphate Isomerase K13M, PDB code: 4zvj:

Potassium binding site 1 out of 1 in the Structure of Human Triose Phosphate Isomerase K13M


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Structure of Human Triose Phosphate Isomerase K13M within 5.0Å range: probe atom residue distance (Å) B Occ B:K301 b:42.5 occ:1.00 O B:GLN223 2.7 30.3 1.0 O B:ALA221 2.7 35.6 1.0 O B:VAL226 2.8 28.7 1.0 O B:HOH423 2.9 51.0 1.0 HZ3 B:LYS247 3.1 62.1 1.0 O B:HOH553 3.5 51.0 1.0 C B:GLN223 3.8 31.3 1.0 C B:ALA221 3.9 34.1 1.0 C B:VAL226 3.9 26.7 1.0 HA B:PRO224 3.9 38.5 1.0 NZ B:LYS247 3.9 51.7 1.0 H B:VAL226 4.0 32.4 1.0 O B:PRO224 4.0 33.0 1.0 HA B:SER222 4.1 41.8 1.0 HZ1 B:LYS247 4.1 62.1 1.0 HA B:ASP227 4.2 29.9 1.0 C B:PRO224 4.2 32.5 1.0 C B:SER222 4.3 33.5 1.0 HZ2 B:LYS247 4.3 62.1 1.0 HB B:VAL226 4.3 31.9 1.0 O B:HOH564 4.3 50.2 1.0 CA B:PRO224 4.4 32.1 1.0 N B:GLN223 4.4 32.2 1.0 N B:VAL226 4.4 27.0 1.0 CA B:SER222 4.5 34.8 1.0 O B:SER222 4.5 34.0 1.0 N B:PRO224 4.5 32.0 1.0 HA B:ALA221 4.5 39.7 1.0 H B:GLN223 4.6 38.6 1.0 HD3 B:LYS247 4.6 57.2 1.0 N B:SER222 4.6 33.7 1.0 O B:HOH505 4.7 45.4 0.9 CA B:VAL226 4.7 26.1 1.0 CA B:GLN223 4.7 31.9 1.0 HE2 B:LYS247 4.8 59.8 1.0 CA B:ALA221 4.8 33.1 1.0 N B:ASP227 4.9 25.1 1.0 OD1 B:ASP227 4.9 29.5 1.0 N B:ASP225 4.9 31.1 1.0 CE B:LYS247 4.9 49.9 1.0 CA B:ASP227 5.0 24.9 1.0 CB B:VAL226 5.0 26.6 1.0

B.P.Roland, C.G.Amrich, C.J.Kammerer, K.A.Stuchul, S.B.Larsen, S.Rode, A.A.Aslam, A.Heroux, R.Wetzel, A.P.Vandemark, M.J.Palladino. Triosephosphate Isomerase I170V Alters Catalytic Site, Enhances Stability and Induces Pathology in A Drosophila Model of Tpi Deficiency. Biochim. Biophys. Acta V.1852 61 2015.
ISSN: ISSN 0006-3002
PubMed: 25463631
DOI: 10.1016/J.BBADIS.2014.10.010