Zinc in PDB 3bkq: Structure of the P368G Mutant of Pmm/Pgm in Complex with Its Substrate

All present enzymatic activity of Structure of the P368G Mutant of Pmm/Pgm in Complex with Its Substrate:
5.4.2.2; 5.4.2.8;

The structure of Structure of the P368G Mutant of Pmm/Pgm in Complex with Its Substrate, PDB code: 3bkq was solved by R.Mehra-Chaudhary, L.J.Beamer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	44.20 / 2.05
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	70.604, 74.740, 86.924, 90.00, 90.00, 90.00
R / Rfree (%)	21.8 / 24.9

The binding sites of Zinc atom in the Structure of the P368G Mutant of Pmm/Pgm in Complex with Its Substrate (pdb code 3bkq). 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 Structure of the P368G Mutant of Pmm/Pgm in Complex with Its Substrate, PDB code: 3bkq:

Zinc binding site 1 out of 1 in the Structure of the P368G Mutant of Pmm/Pgm in Complex with Its Substrate


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of the P368G Mutant of Pmm/Pgm in Complex with Its Substrate within 5.0Å range: probe atom residue distance (Å) B Occ X:Zn500 b:29.0 occ:1.00 OD2 X:ASP242 1.9 28.9 1.0 OD1 X:ASP246 1.9 24.4 1.0 OD2 X:ASP244 2.1 25.7 1.0 O3P X:SEP108 2.1 42.2 1.0 OG X:SEP108 2.5 43.1 1.0 P X:SEP108 2.9 42.7 1.0 CG X:ASP246 2.9 27.8 1.0 CG X:ASP242 2.9 27.6 1.0 CG X:ASP244 3.0 25.5 1.0 OD1 X:ASP244 3.1 23.1 1.0 OD2 X:ASP246 3.2 28.3 1.0 OD1 X:ASP242 3.3 29.6 1.0 CB X:SEP108 3.9 39.6 1.0 NZ X:LYS118 3.9 28.5 1.0 O2P X:SEP108 3.9 46.1 1.0 O1P X:SEP108 4.1 44.3 1.0 CD X:ARG247 4.2 35.1 1.0 CB X:ASP242 4.2 27.0 1.0 CB X:ASP246 4.2 25.6 1.0 NH1 X:ARG247 4.3 43.7 1.0 CA X:SEP108 4.3 39.3 1.0 N X:ASP246 4.3 25.4 1.0 CB X:ASP244 4.4 24.3 1.0 N X:ASP244 4.5 25.2 1.0 N X:ARG247 4.5 27.4 1.0 CA X:ASP246 4.6 25.8 1.0 CE1 X:HIS329 4.7 30.2 1.0 CG X:ARG247 4.7 31.9 1.0 C X:SEP108 4.7 39.2 1.0 N X:GLY245 4.8 24.3 1.0 C X:ASP246 4.8 26.7 1.0 CA X:ASP244 4.8 24.8 1.0 CB X:ARG247 4.8 28.4 1.0 C X:ASP244 4.9 24.4 1.0 N X:HIS109 5.0 40.2 1.0

A.M.Schramm, R.Mehra-Chaudhary, C.M.Furdui, L.J.Beamer. Backbone Flexibility, Conformational Change, and Catalysis in A Phosphohexomutase From Pseudomonas Aeruginosa. Biochemistry V. 47 9154 2008.
ISSN: ISSN 0006-2960
PubMed: 18690721
DOI: 10.1021/BI8005219