Potassium in PDB 4poc: Structure of Triosephosphate Isomerase Wild Type Human Enzyme.

All present enzymatic activity of Structure of Triosephosphate Isomerase Wild Type Human Enzyme.:
5.3.1.1;

The structure of Structure of Triosephosphate Isomerase Wild Type Human Enzyme., PDB code: 4poc was solved by C.G.Amrich, A.A.Aslam, A.Heroux, A.P.Vandemark, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.56 / 1.60
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	47.920, 48.851, 93.966, 90.00, 103.66, 90.00
R / Rfree (%)	15.3 / 18.7

The structure of Structure of Triosephosphate Isomerase Wild Type Human Enzyme. also contains other interesting chemical elements:

Bromine	(Br)	2 atoms
Sodium	(Na)	1 atom

The binding sites of Potassium atom in the Structure of Triosephosphate Isomerase Wild Type Human Enzyme. (pdb code 4poc). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Structure of Triosephosphate Isomerase Wild Type Human Enzyme., PDB code: 4poc:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in the Structure of Triosephosphate Isomerase Wild Type Human Enzyme.


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Structure of Triosephosphate Isomerase Wild Type Human Enzyme. within 5.0Å range: probe atom residue distance (Å) B Occ A:K301 b:60.4 occ:1.00 O A:VAL226 2.6 39.5 1.0 O A:GLN223 2.6 48.9 1.0 O A:ALA221 2.8 47.5 1.0 O A:HOH519 2.9 49.3 1.0 HE2 A:LYS247 3.6 87.9 1.0 C A:GLN223 3.7 49.1 1.0 HA A:PRO224 3.7 58.3 1.0 HE3 A:LYS247 3.8 87.9 1.0 C A:VAL226 3.8 38.4 1.0 H A:VAL226 3.8 46.7 1.0 HZ3 A:LYS247 4.0 88.4 1.0 C A:ALA221 4.0 48.5 1.0 HZ2 A:LYS247 4.0 88.4 1.0 CE A:LYS247 4.0 73.2 1.0 HA A:ASP227 4.0 43.0 1.0 O A:PRO224 4.1 47.6 1.0 HB A:VAL226 4.1 46.8 1.0 C A:PRO224 4.2 46.4 1.0 NZ A:LYS247 4.2 73.7 1.0 CA A:PRO224 4.3 48.6 1.0 O A:HOH505 4.3 47.8 1.0 N A:VAL226 4.3 39.0 1.0 C A:SER222 4.4 50.4 1.0 O A:SER222 4.4 50.4 1.0 N A:PRO224 4.5 48.9 1.0 N A:GLN223 4.5 49.8 1.0 HA A:ALA221 4.5 58.2 1.0 CA A:VAL226 4.5 38.5 1.0 HA A:SER222 4.6 60.8 1.0 CA A:GLN223 4.7 49.9 1.0 H A:GLN223 4.7 59.8 1.0 N A:ASP227 4.7 37.2 1.0 CB A:VAL226 4.8 39.0 1.0 N A:ASP225 4.8 43.0 1.0 OD1 A:ASP227 4.8 39.7 1.0 CA A:ASP227 4.8 35.8 1.0 CA A:SER222 4.8 50.7 1.0 N A:SER222 4.9 49.6 1.0 CA A:ALA221 4.9 48.5 1.0 HG12 A:VAL226 5.0 46.5 1.0

Potassium binding site 2 out of 2 in the Structure of Triosephosphate Isomerase Wild Type Human Enzyme.


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Structure of Triosephosphate Isomerase Wild Type Human Enzyme. within 5.0Å range: probe atom residue distance (Å) B Occ B:K302 b:37.4 occ:1.00 O B:GLN223 2.6 35.4 1.0 O B:VAL226 2.7 26.2 1.0 O B:HOH440 2.7 39.8 1.0 O B:HOH462 2.8 36.6 0.8 O B:HOH503 2.8 51.2 1.0 O B:ALA221 2.8 35.7 1.0 O B:HOH493 2.8 42.7 1.0 HA B:PRO224 3.6 42.0 1.0 C B:GLN223 3.6 35.7 1.0 O B:HOH558 3.8 37.4 0.9 HE2 B:LYS247 3.8 56.6 1.0 H B:VAL226 3.8 34.0 1.0 C B:VAL226 3.8 26.2 1.0 HE3 B:LYS247 3.9 56.6 1.0 C B:ALA221 4.0 36.6 1.0 O B:PRO224 4.0 35.2 1.0 C B:PRO224 4.1 34.3 1.0 CA B:PRO224 4.1 35.0 1.0 HA B:ASP227 4.2 30.3 1.0 HB B:VAL226 4.2 34.5 1.0 N B:VAL226 4.3 28.3 1.0 N B:GLN223 4.3 34.5 1.0 CE B:LYS247 4.3 47.2 1.0 N B:PRO224 4.3 35.4 1.0 C B:SER222 4.4 35.2 1.0 HA B:SER222 4.4 43.7 1.0 H B:GLN223 4.5 41.4 1.0 HA B:ALA221 4.5 44.2 1.0 CA B:VAL226 4.5 27.2 1.0 O B:SER222 4.6 36.8 1.0 CA B:GLN223 4.6 35.6 1.0 N B:ASP225 4.8 31.5 1.0 CA B:SER222 4.8 36.4 1.0 N B:SER222 4.8 35.9 1.0 N B:ASP227 4.8 26.7 1.0 CB B:VAL226 4.9 28.8 1.0 OD1 B:ASP227 4.9 29.5 1.0 CA B:ALA221 4.9 36.9 1.0 HZ3 B:LYS247 4.9 59.0 1.0 CA B:ASP227 4.9 25.2 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