Zinc in PDB 1p5g: Enzyme-Ligand Complex of P. Aeruginosa Pmm/Pgm

All present enzymatic activity of Enzyme-Ligand Complex of P. Aeruginosa Pmm/Pgm:
5.4.2.8;

The structure of Enzyme-Ligand Complex of P. Aeruginosa Pmm/Pgm, PDB code: 1p5g was solved by C.Regni, P.A.Tipton, L.J.Beamer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	25.00 / 1.61
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	70.591, 74.372, 85.994, 90.00, 90.00, 90.00
R / Rfree (%)	16 / 18.7

The binding sites of Zinc atom in the Enzyme-Ligand Complex of P. Aeruginosa Pmm/Pgm (pdb code 1p5g). 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 Enzyme-Ligand Complex of P. Aeruginosa Pmm/Pgm, PDB code: 1p5g:

Zinc binding site 1 out of 1 in the Enzyme-Ligand Complex of P. Aeruginosa Pmm/Pgm


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Enzyme-Ligand Complex of P. Aeruginosa Pmm/Pgm within 5.0Å range: probe atom residue distance (Å) B Occ X:Zn500 b:14.1 occ:1.00 OD1 X:ASP246 1.9 12.2 1.0 OD2 X:ASP242 1.9 12.4 1.0 O3P X:SEP108 2.0 22.4 1.0 OD2 X:ASP244 2.0 11.7 1.0 CG X:ASP242 2.9 11.6 1.0 CG X:ASP246 2.9 10.9 1.0 CG X:ASP244 2.9 13.1 1.0 OG X:SEP108 3.0 21.9 1.0 P X:SEP108 3.1 19.2 1.0 OD1 X:ASP244 3.1 13.3 1.0 OD1 X:ASP242 3.2 10.5 1.0 OD2 X:ASP246 3.2 12.3 1.0 CD X:ARG247 3.9 18.6 0.5 NZ X:LYS118 3.9 17.9 1.0 CB X:SEP108 4.0 19.9 1.0 NH1 X:ARG247 4.1 22.5 0.5 O2P X:SEP108 4.1 24.2 1.0 CE1 X:HIS329 4.1 12.6 1.0 CA X:SEP108 4.2 19.9 1.0 N X:ASP246 4.2 9.2 1.0 CG X:ARG247 4.2 14.4 0.5 CB X:ASP246 4.2 8.7 1.0 O1P X:SEP108 4.3 22.3 1.0 CB X:ASP242 4.3 11.3 1.0 CB X:ASP244 4.3 11.5 1.0 N X:ARG247 4.5 11.1 0.5 N X:ASP244 4.5 11.9 1.0 N X:ARG247 4.5 11.6 0.5 CA X:ASP246 4.5 9.5 1.0 NE2 X:HIS329 4.6 15.8 1.0 NE X:ARG247 4.6 20.0 0.5 C X:SEP108 4.6 20.4 1.0 CB X:ARG247 4.6 13.4 0.5 CZ X:ARG247 4.7 21.4 0.5 C X:ASP246 4.7 10.8 1.0 N X:GLY245 4.7 10.4 1.0 CB X:ARG247 4.8 11.9 0.5 CA X:ASP244 4.8 11.2 1.0 N X:HIS109 4.9 21.2 1.0 C X:ASP244 4.9 10.8 1.0

C.Regni, L.Naught, P.A.Tipton, L.J.Beamer. Structural Basis of Diverse Substrate Recognition By the Enzyme Pmm/Pgm From P. Aeruginosa. Structure V. 12 55 2004.
ISSN: ISSN 0969-2126
PubMed: 14725765
DOI: 10.1016/J.STR.2003.11.015