Potassium in PDB 5i3h: Structure-Function Studies on Role of Hydrophobic Clamping of A Basic Glutamate in Catalysis By Triosephosphate Isomerase

All present enzymatic activity of Structure-Function Studies on Role of Hydrophobic Clamping of A Basic Glutamate in Catalysis By Triosephosphate Isomerase:
5.3.1.1;

The structure of Structure-Function Studies on Role of Hydrophobic Clamping of A Basic Glutamate in Catalysis By Triosephosphate Isomerase, PDB code: 5i3h was solved by E.J.Drake, A.M.Gulick, J.P.Richard, X.Zhai, K.Kim, C.J.Reinhardt, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.47 / 2.25
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	46.282, 46.656, 60.981, 72.68, 88.47, 80.60
R / Rfree (%)	16.6 / 21.1

The binding sites of Potassium atom in the Structure-Function Studies on Role of Hydrophobic Clamping of A Basic Glutamate in Catalysis By Triosephosphate Isomerase (pdb code 5i3h). 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-Function Studies on Role of Hydrophobic Clamping of A Basic Glutamate in Catalysis By Triosephosphate Isomerase, PDB code: 5i3h:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in the Structure-Function Studies on Role of Hydrophobic Clamping of A Basic Glutamate in Catalysis By Triosephosphate Isomerase


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Structure-Function Studies on Role of Hydrophobic Clamping of A Basic Glutamate in Catalysis By Triosephosphate Isomerase within 5.0Å range: probe atom residue distance (Å) B Occ A:K301 b:33.2 occ:1.00 O A:HOH447 2.9 19.4 1.0 N A:ALA236 3.3 14.5 1.0 N A:VAL214 3.3 20.2 1.0 CB A:ALA236 3.3 16.2 1.0 O A:VAL214 3.4 18.2 1.0 CA A:SER213 3.8 20.4 1.0 CG1 A:VAL233 3.8 11.4 1.0 N A:GLY235 3.9 12.8 1.0 CA A:ALA236 3.9 12.9 1.0 C A:SER213 4.1 22.7 1.0 O A:HOH442 4.1 12.8 1.0 C A:VAL214 4.2 21.2 1.0 N A:GLY234 4.2 11.9 1.0 C A:GLY235 4.3 15.2 1.0 CA A:VAL214 4.3 21.4 1.0 CB A:SER213 4.4 23.2 1.0 CG2 A:VAL214 4.4 18.1 1.0 O A:HOH586 4.4 15.9 1.0 CA A:GLY235 4.4 12.4 1.0 C A:GLY234 4.4 16.1 1.0 O A:GLY212 4.6 16.4 1.0 CA A:GLY234 4.7 12.6 1.0 OG A:SER213 4.8 28.8 1.0 N A:SER213 4.9 17.9 1.0

Potassium binding site 2 out of 2 in the Structure-Function Studies on Role of Hydrophobic Clamping of A Basic Glutamate in Catalysis By Triosephosphate Isomerase


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Structure-Function Studies on Role of Hydrophobic Clamping of A Basic Glutamate in Catalysis By Triosephosphate Isomerase within 5.0Å range: probe atom residue distance (Å) B Occ A:K302 b:32.1 occ:1.00 O B:HOH561 2.9 15.2 1.0 OD1 A:ASN15 3.0 13.8 1.0 N B:ALA73 3.2 9.3 1.0 C B:GLY72 3.2 11.3 1.0 O A:HOH494 3.5 24.8 1.0 CA B:ALA73 3.5 10.8 1.0 O B:GLY72 3.5 10.2 1.0 O B:HOH607 3.6 20.6 1.0 CA B:GLY72 3.7 12.2 1.0 CB B:ALA73 3.9 13.4 1.0 CG A:ASN15 3.9 12.3 1.0 CD A:LYS13 3.9 10.0 1.0 ND2 A:ASN15 4.1 15.0 1.0 CB A:LYS13 4.3 8.8 1.0 O B:HOH503 4.5 12.7 1.0 CG A:LYS13 4.5 9.8 1.0 O A:HOH458 4.6 13.6 1.0 N B:GLY72 4.8 11.8 1.0 CE A:LYS13 4.9 12.5 1.0 C B:ALA73 4.9 10.6 1.0

J.P.Richard, T.L.Amyes, M.M.Malabanan, X.Zhai, K.J.Kim, C.J.Reinhardt, R.K.Wierenga, E.J.Drake, A.M.Gulick. Structure-Function Studies of Hydrophobic Residues That Clamp A Basic Glutamate Side Chain During Catalysis By Triosephosphate Isomerase. Biochemistry V. 55 3036 2016.
ISSN: ISSN 0006-2960
PubMed: 27149328
DOI: 10.1021/ACS.BIOCHEM.6B00311