Zinc in PDB 1jaz: Crystal Structure of Monoclinic Form of D90E Mutant of Escherichia Coli Asparaginase II

All present enzymatic activity of Crystal Structure of Monoclinic Form of D90E Mutant of Escherichia Coli Asparaginase II:
3.5.1.1;

The structure of Crystal Structure of Monoclinic Form of D90E Mutant of Escherichia Coli Asparaginase II, PDB code: 1jaz was solved by D.Borek, M.Kozak, M.Jaskolski, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 2.27
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	73.118, 133.076, 62.565, 90.00, 108.78, 90.00
R / Rfree (%)	18 / 23.2

The binding sites of Zinc atom in the Crystal Structure of Monoclinic Form of D90E Mutant of Escherichia Coli Asparaginase II (pdb code 1jaz). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the Crystal Structure of Monoclinic Form of D90E Mutant of Escherichia Coli Asparaginase II, PDB code: 1jaz:
Jump to Zinc binding site number: 1; 2; 3;

Zinc binding site 1 out of 3 in the Crystal Structure of Monoclinic Form of D90E Mutant of Escherichia Coli Asparaginase II


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 Monoclinic Form of D90E Mutant of Escherichia Coli Asparaginase II within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn401 b:37.7 occ:1.00 O A:HOH415 1.7 29.7 1.0 O A:HOH416 1.9 29.5 1.0 OD2 A:ASP100 1.9 25.3 1.0 ND1 A:HIS197 2.0 26.9 1.0 CG A:ASP100 2.7 20.6 1.0 OD1 A:ASP100 2.9 22.0 1.0 CG A:HIS197 2.9 24.1 1.0 CE1 A:HIS197 3.1 23.7 1.0 CB A:HIS197 3.1 22.2 1.0 O A:HOH402 3.7 29.8 1.0 O A:HOH448 3.8 33.1 1.0 O A:ARG195 4.0 22.6 1.0 CD2 A:HIS197 4.1 24.7 1.0 NE2 A:HIS197 4.1 22.9 1.0 CB A:ASP100 4.2 21.4 1.0 CB A:ARG158 4.4 22.6 1.0 OD1 A:ASP156 4.5 25.5 1.0 CA A:HIS197 4.6 22.5 1.0 CB A:PRO193 4.6 25.0 1.0 CG A:PRO193 4.7 24.9 1.0 N A:ARG158 4.8 21.7 1.0 O A:ARG144 4.8 23.5 1.0 CA A:GLY145 4.9 22.6 1.0 O A:LYS196 4.9 23.9 1.0 N A:HIS197 5.0 23.0 1.0

Zinc binding site 2 out of 3 in the Crystal Structure of Monoclinic Form of D90E Mutant of Escherichia Coli Asparaginase II


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Monoclinic Form of D90E Mutant of Escherichia Coli Asparaginase II within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn402 b:33.4 occ:1.00 O B:HOH415 1.8 32.5 1.0 OD2 B:ASP100 1.9 27.9 1.0 ND1 B:HIS197 2.0 24.0 1.0 O B:HOH416 2.3 28.7 1.0 CG B:ASP100 2.7 22.8 1.0 OD1 B:ASP100 2.8 20.8 1.0 CG B:HIS197 2.9 23.2 1.0 CE1 B:HIS197 3.1 23.2 1.0 CB B:HIS197 3.2 21.2 1.0 O B:HOH404 3.8 30.6 1.0 O B:HOH456 3.8 29.8 1.0 O B:ARG195 4.1 24.3 1.0 CD2 B:HIS197 4.1 22.9 1.0 NE2 B:HIS197 4.2 21.1 1.0 CB B:ASP100 4.2 22.6 1.0 CB B:ARG158 4.4 23.4 1.0 OD1 B:ASP156 4.5 24.8 1.0 CB B:PRO193 4.5 24.0 1.0 CG B:PRO193 4.6 24.2 1.0 CA B:HIS197 4.6 21.8 1.0 CA B:GLY145 4.7 23.7 1.0 N B:ARG158 4.8 23.7 1.0 O B:ARG144 4.8 25.7 1.0 N B:HIS197 5.0 22.5 1.0

Zinc binding site 3 out of 3 in the Crystal Structure of Monoclinic Form of D90E Mutant of Escherichia Coli Asparaginase II


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structure of Monoclinic Form of D90E Mutant of Escherichia Coli Asparaginase II within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn403 b:43.7 occ:0.50 OD2 B:ASP200 1.9 30.9 1.0 CG B:ASP200 2.7 22.8 1.0 OD1 B:ASP200 2.9 29.1 1.0 CB B:ASP200 4.1 20.9 1.0 OG B:SER199 4.1 24.6 1.0 N B:ASP200 4.5 20.4 1.0 CA B:ASP200 4.7 20.8 1.0 OD1 B:ASP106 4.9 41.0 1.0

D.Borek, M.Kozak, J.Pei, M.Jaskolski. Crystal Structure of Active Site Mutant of Antileukemic L-Asparaginase Reveals Conserved Zinc-Binding Site. Febs J. V. 281 4097 2014.
ISSN: ISSN 1742-464X
PubMed: 25040257
DOI: 10.1111/FEBS.12906