Zinc in PDB 1p5d: 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: 1p5d 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 / 1.60
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	70.700, 74.193, 84.836, 90.00, 90.00, 90.00
R / Rfree (%)	15.6 / 17.9

The binding sites of Zinc atom in the Enzyme-Ligand Complex of P. Aeruginosa Pmm/Pgm (pdb code 1p5d). 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: 1p5d:

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:14.6 occ:1.00 OD1 X:ASP246 1.9 13.8 1.0 OD2 X:ASP242 1.9 14.1 1.0 O3P X:SEP108 1.9 25.2 1.0 OD1 X:ASP244 2.0 14.3 1.0 CG X:ASP242 2.9 13.7 1.0 CG X:ASP246 2.9 11.5 1.0 CG X:ASP244 3.0 14.3 1.0 P X:SEP108 3.1 23.5 1.0 OG X:SEP108 3.1 24.4 1.0 OD1 X:ASP242 3.1 13.0 1.0 OD2 X:ASP246 3.2 12.8 1.0 OD2 X:ASP244 3.2 14.8 1.0 NZ X:LYS118 3.9 19.7 1.0 CG X:ARG247 4.0 13.9 0.4 O2P X:SEP108 4.1 25.7 1.0 CD X:ARG247 4.1 18.2 0.6 CB X:SEP108 4.1 21.1 1.0 CG X:ARG247 4.1 15.3 0.6 CE1 X:HIS329 4.2 15.6 1.0 N X:ASP246 4.2 10.8 1.0 O1P X:SEP108 4.2 27.4 1.0 CB X:ASP246 4.2 10.9 1.0 CB X:ASP242 4.2 12.3 1.0 CA X:SEP108 4.3 20.3 1.0 CD X:ARG247 4.3 13.9 0.4 CB X:ASP244 4.3 12.2 1.0 N X:ARG247 4.4 11.8 0.4 NE X:ARG247 4.4 16.4 0.4 N X:ARG247 4.4 11.8 0.6 N X:ASP244 4.5 12.2 1.0 CA X:ASP246 4.5 10.6 1.0 C X:SEP108 4.6 20.9 1.0 C X:ASP246 4.6 11.6 1.0 CA X:ASP244 4.7 12.0 1.0 CB X:ARG247 4.7 12.8 0.6 CB X:ARG247 4.8 12.4 0.4 N X:GLY245 4.8 11.8 1.0 NE2 X:HIS329 4.8 16.1 1.0 C X:ASP244 4.9 12.0 1.0 N X:HIS109 4.9 21.1 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