Potassium in PDB 1h54: Maltose Phosphorylase From Lactobacillus Brevis

All present enzymatic activity of Maltose Phosphorylase From Lactobacillus Brevis:
2.4.1.8;

The structure of Maltose Phosphorylase From Lactobacillus Brevis, PDB code: 1h54 was solved by H.Van Tilbeurgh, M.-P.Egloff, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.1 / 2.15
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	83.750, 102.500, 114.000, 90.00, 111.30, 90.00
R / Rfree (%)	18.6 / 22.5

The binding sites of Potassium atom in the Maltose Phosphorylase From Lactobacillus Brevis (pdb code 1h54). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Maltose Phosphorylase From Lactobacillus Brevis, PDB code: 1h54:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in the Maltose Phosphorylase From Lactobacillus Brevis


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Maltose Phosphorylase From Lactobacillus Brevis within 5.0Å range: probe atom residue distance (Å) B Occ A:K1754 b:16.2 occ:1.00 O A:TYR488 2.6 9.8 1.0 O A:SER588 2.7 9.2 1.0 OE2 A:GLU489 2.7 15.5 1.0 O A:ILE585 2.8 10.5 1.0 O A:LEU586 3.0 10.7 1.0 O A:TYR590 3.0 13.2 1.0 OE1 A:GLU489 3.1 13.3 1.0 CD A:GLU489 3.1 15.9 1.0 OG A:SER588 3.5 7.5 1.0 C A:SER588 3.6 9.1 1.0 C A:TYR488 3.6 11.2 1.0 C A:LEU586 3.7 9.5 1.0 CB A:TYR488 3.8 9.6 1.0 C A:ILE585 3.9 9.4 1.0 CA A:LEU586 4.0 9.1 1.0 N A:TYR590 4.0 11.1 1.0 C A:TYR590 4.0 12.7 1.0 NZ A:LYS561 4.1 7.2 1.0 N A:SER588 4.2 9.8 1.0 CA A:SER588 4.3 9.4 1.0 CA A:TYR488 4.3 9.8 1.0 N A:LEU586 4.4 7.5 1.0 C A:PRO589 4.5 12.3 1.0 CG A:GLU489 4.5 12.6 1.0 CB A:SER588 4.5 10.0 1.0 N A:PRO589 4.5 9.9 1.0 CA A:TYR590 4.5 11.3 1.0 N A:GLU489 4.6 10.6 1.0 C A:ARG587 4.7 10.4 1.0 N A:ARG587 4.7 9.4 1.0 CE A:LYS561 4.7 7.6 1.0 CA A:PRO589 4.7 10.4 1.0 CA A:GLU489 4.9 11.9 1.0 CG A:TYR488 5.0 9.1 1.0

Potassium binding site 2 out of 2 in the Maltose Phosphorylase From Lactobacillus Brevis


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Maltose Phosphorylase From Lactobacillus Brevis within 5.0Å range: probe atom residue distance (Å) B Occ B:K1756 b:14.9 occ:1.00 OE1 B:GLU489 2.6 14.3 1.0 O B:SER588 2.7 11.1 1.0 O B:ILE585 2.7 13.0 1.0 O B:TYR488 2.8 10.3 1.0 O B:LEU586 3.0 9.7 1.0 O B:TYR590 3.1 11.4 1.0 OE2 B:GLU489 3.1 14.8 1.0 CD B:GLU489 3.1 12.9 1.0 OG B:SER588 3.6 12.1 1.0 C B:SER588 3.6 11.4 1.0 C B:LEU586 3.7 10.0 1.0 C B:TYR488 3.8 10.6 1.0 C B:ILE585 3.9 12.0 1.0 CB B:TYR488 3.9 9.7 1.0 NZ B:LYS561 4.0 12.2 1.0 N B:TYR590 4.0 12.5 1.0 CA B:LEU586 4.0 10.1 1.0 C B:TYR590 4.0 12.1 1.0 N B:SER588 4.1 9.7 1.0 CA B:SER588 4.3 10.1 1.0 N B:LEU586 4.4 11.0 1.0 CA B:TYR488 4.5 11.5 1.0 CA B:TYR590 4.5 11.6 1.0 C B:PRO589 4.5 14.2 1.0 CG B:GLU489 4.5 11.7 1.0 N B:PRO589 4.5 13.0 1.0 CB B:SER588 4.6 11.5 1.0 CE B:LYS561 4.6 10.7 1.0 N B:ARG587 4.6 9.3 1.0 C B:ARG587 4.6 8.8 1.0 CA B:PRO589 4.7 12.8 1.0 N B:GLU489 4.7 9.7 1.0

M.-P.Egloff, J.Uppenberg, L.Haalck, H.Van Tilbeurgh. Crystal Structure of Maltose Phosphorylase From Lactobacillus Brevis: Unexpected Evolutionary Relationship with Glucoamylases. Structure V. 9 689 2001.
ISSN: ISSN 0969-2126
PubMed: 11587643
DOI: 10.1016/S0969-2126(01)00626-8