Zinc in PDB 2fkm: Pmm/Pgm S108D Mutant with Alpha-D-Glucose 1,6-Bisphosphate Bound

All present enzymatic activity of Pmm/Pgm S108D Mutant with Alpha-D-Glucose 1,6-Bisphosphate Bound:
5.4.2.8;

The structure of Pmm/Pgm S108D Mutant with Alpha-D-Glucose 1,6-Bisphosphate Bound, PDB code: 2fkm was solved by C.A.Regni, L.J.Beamer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.83 / 1.90
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	70.222, 70.356, 84.392, 90.00, 90.00, 90.00
R / Rfree (%)	20.3 / 25.1

The binding sites of Zinc atom in the Pmm/Pgm S108D Mutant with Alpha-D-Glucose 1,6-Bisphosphate Bound (pdb code 2fkm). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Pmm/Pgm S108D Mutant with Alpha-D-Glucose 1,6-Bisphosphate Bound, PDB code: 2fkm:

Zinc binding site 1 out of 1 in the Pmm/Pgm S108D Mutant with Alpha-D-Glucose 1,6-Bisphosphate Bound


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Pmm/Pgm S108D Mutant with Alpha-D-Glucose 1,6-Bisphosphate Bound within 5.0Å range: probe atom residue distance (Å) B Occ X:Zn500 b:39.3 occ:1.00 OD1 X:ASP246 2.0 33.4 1.0 OD2 X:ASP242 2.0 34.5 1.0 OD2 X:ASP108 2.2 33.7 1.0 OD1 X:ASP108 2.6 38.2 1.0 CG X:ASP108 2.7 34.9 1.0 OD1 X:ASP244 2.8 37.6 1.0 CG X:ASP246 2.9 31.2 1.0 CG X:ASP242 3.0 31.0 1.0 OD1 X:ASP242 3.2 33.2 1.0 OD2 X:ASP246 3.3 32.6 1.0 CG X:ASP244 3.6 34.1 1.0 NZ X:LYS118 3.8 34.4 1.0 OD2 X:ASP244 3.8 38.3 1.0 CG X:ARG247 4.1 33.2 1.0 CB X:ASP108 4.1 34.9 1.0 NE2 X:HIS329 4.2 32.5 1.0 O1X X:G16464 4.2 48.6 1.0 CB X:ASP246 4.2 31.8 1.0 N X:ASP246 4.3 31.7 1.0 N X:ARG247 4.3 31.6 1.0 CB X:ASP242 4.3 31.0 1.0 O2X X:G16464 4.4 47.5 1.0 NE X:ARG247 4.5 36.7 1.0 CA X:ASP246 4.5 31.6 1.0 N X:ASP244 4.6 32.4 1.0 C X:ASP246 4.6 31.8 1.0 CD X:ARG247 4.6 33.8 1.0 ND1 X:HIS109 4.6 36.2 1.0 CB X:ARG247 4.7 31.8 1.0 CE1 X:HIS329 4.7 31.1 1.0 CB X:ASP244 4.8 32.8 1.0 N X:GLY245 4.9 32.0 1.0 CA X:ASP108 5.0 34.5 1.0 P' X:G16464 5.0 49.7 1.0

C.Regni, A.M.Schramm, L.J.Beamer. The Reaction of Phosphohexomutase From Pseudomonas Aeruginosa: Structural Insights Into A Simple Processive Enzyme. J.Biol.Chem. V. 281 15564 2006.
ISSN: ISSN 0021-9258
PubMed: 16595672
DOI: 10.1074/JBC.M600590200