Zinc in PDB 4mrq: Crystal Structure of Wild-Type Unphosphorylated Pmm/Pgm

All present enzymatic activity of Crystal Structure of Wild-Type Unphosphorylated Pmm/Pgm:
5.4.2.2; 5.4.2.8;

The structure of Crystal Structure of Wild-Type Unphosphorylated Pmm/Pgm, PDB code: 4mrq was solved by Y.Lee, L.Beamer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	38.90 / 1.90
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	70.541, 72.003, 92.349, 90.00, 90.00, 90.00
R / Rfree (%)	16.5 / 20.5

The binding sites of Zinc atom in the Crystal Structure of Wild-Type Unphosphorylated Pmm/Pgm (pdb code 4mrq). 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 Crystal Structure of Wild-Type Unphosphorylated Pmm/Pgm, PDB code: 4mrq:

Zinc binding site 1 out of 1 in the Crystal Structure of Wild-Type Unphosphorylated Pmm/Pgm


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Wild-Type Unphosphorylated Pmm/Pgm within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn501 b:22.4 occ:1.00 OD1 A:ASP246 1.9 19.2 1.0 OD2 A:ASP242 1.9 19.3 1.0 O41 A:TLA502 2.0 26.1 1.0 OD2 A:ASP244 2.1 20.9 1.0 C4 A:TLA502 2.6 30.1 1.0 O4 A:TLA502 2.6 28.5 1.0 CG A:ASP246 2.9 19.0 1.0 CG A:ASP242 2.9 20.0 1.0 CG A:ASP244 3.0 21.7 1.0 OD2 A:ASP246 3.2 18.4 1.0 OD1 A:ASP242 3.2 19.7 1.0 OD1 A:ASP244 3.3 19.9 1.0 NZ A:LYS118 3.6 22.2 1.0 C3 A:TLA502 4.1 37.8 1.0 CB A:SER108 4.1 29.4 1.0 N A:ASP246 4.2 18.6 1.0 CB A:ASP246 4.2 18.5 1.0 CB A:ASP242 4.2 21.5 1.0 NE A:ARG247 4.3 30.3 1.0 CG A:ARG247 4.4 24.5 1.0 OG A:SER108 4.4 31.7 1.0 CB A:ASP244 4.4 19.9 1.0 CA A:SER108 4.5 26.8 1.0 N A:ASP244 4.5 20.1 1.0 N A:ARG247 4.6 20.1 1.0 CA A:ASP246 4.6 18.6 1.0 O2 A:TLA502 4.6 42.6 1.0 CE1 A:HIS329 4.6 22.6 1.0 C2 A:TLA502 4.7 41.6 1.0 N A:GLY245 4.8 18.0 1.0 CA A:ASP244 4.8 19.4 1.0 C A:ASP246 4.8 19.7 1.0 CB A:ARG247 4.9 24.1 1.0 C A:SER108 4.9 27.1 1.0 O3 A:TLA502 4.9 38.4 1.0 CD A:ARG247 4.9 28.6 1.0 C A:ASP244 4.9 19.4 1.0 O A:HOH715 5.0 35.3 1.0

Y.Lee, M.T.Villar, A.Artigues, L.J.Beamer. Promotion of Enzyme Flexibility By Dephosphorylation and Coupling to the Catalytic Mechanism of A Phosphohexomutase. J.Biol.Chem. V. 289 4674 2014.
ISSN: ISSN 0021-9258
PubMed: 24403075
DOI: 10.1074/JBC.M113.532226