Zinc in PDB 2cbn: Crystal Structure of Zipd From Escherichia Coli

All present enzymatic activity of Crystal Structure of Zipd From Escherichia Coli:
3.1.26.11;

The structure of Crystal Structure of Zipd From Escherichia Coli, PDB code: 2cbn was solved by E.Pohl, W.Meyer-Klaucke, B.Kostelecky, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50 / 2.9
Space group	P 64 2 2
Cell size a, b, c (Å), α, β, γ (°)	147.200, 147.200, 138.200, 90.00, 90.00, 120.00
R / Rfree (%)	23 / 25

The binding sites of Zinc atom in the Crystal Structure of Zipd From Escherichia Coli (pdb code 2cbn). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of Zipd From Escherichia Coli, PDB code: 2cbn:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of Zipd From Escherichia Coli


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 Zipd From Escherichia Coli within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn401 b:60.1 occ:1.00 NE2 A:HIS141 2.2 60.8 1.0 CE1 A:HIS64 2.3 58.5 1.0 ND1 A:HIS66 2.3 56.7 1.0 OD1 A:ASP212 2.6 68.0 1.0 ND1 A:HIS64 3.1 57.5 1.0 CG A:HIS66 3.1 56.0 1.0 CE1 A:HIS141 3.2 61.3 1.0 CE1 A:HIS66 3.2 57.8 1.0 CD2 A:HIS141 3.2 61.6 1.0 NE2 A:HIS64 3.3 57.0 1.0 ZN A:ZN402 3.3 54.4 1.0 CB A:HIS66 3.4 55.4 1.0 CG A:ASP212 3.6 66.1 1.0 CB A:ASP212 3.9 66.2 1.0 CD2 A:HIS69 4.1 53.6 1.0 OD1 A:ASP68 4.1 53.7 1.0 NE2 A:HIS69 4.1 53.7 1.0 CD2 A:HIS66 4.2 56.8 1.0 NE2 A:HIS66 4.2 58.9 1.0 ND1 A:HIS141 4.3 59.6 1.0 CG A:HIS64 4.3 56.7 1.0 CG A:HIS141 4.4 61.2 1.0 CD2 A:HIS64 4.4 57.6 1.0 OD2 A:ASP212 4.7 69.7 1.0 CE1 A:HIS248 4.8 65.3 1.0 CA A:HIS66 4.9 54.5 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of Zipd From Escherichia Coli


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 Zipd From Escherichia Coli within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn402 b:54.4 occ:1.00 OD1 A:ASP212 2.0 68.0 1.0 NE2 A:HIS270 2.1 55.1 1.0 NE2 A:HIS69 2.2 53.7 1.0 OD2 A:ASP68 2.7 60.9 1.0 CG A:ASP212 2.9 66.1 1.0 CD2 A:HIS69 3.0 53.6 1.0 OD1 A:ASP68 3.0 53.7 1.0 CE1 A:HIS270 3.1 56.8 1.0 CD2 A:HIS270 3.1 56.1 1.0 OD2 A:ASP212 3.1 69.7 1.0 CG A:ASP68 3.2 56.0 1.0 CE1 A:HIS69 3.3 52.7 1.0 ZN A:ZN401 3.3 60.1 1.0 CE1 A:HIS64 4.1 58.5 1.0 ND1 A:HIS270 4.2 55.9 1.0 NE2 A:HIS64 4.2 57.0 1.0 CG A:HIS69 4.2 54.4 1.0 CG A:HIS270 4.2 56.2 1.0 CB A:ASP212 4.3 66.2 1.0 ND1 A:HIS69 4.3 53.9 1.0 N A:GLY11 4.4 51.6 1.0 CE1 A:HIS248 4.5 65.3 1.0 CB A:ASP68 4.8 51.0 1.0 NE2 A:HIS141 4.9 60.8 1.0 CA A:GLY11 5.0 50.5 1.0

B.Kostelecky, E.Pohl, A.Vogel, O.Schilling, W.Meyer-Klaucke. The Crystal Structure of the Zinc Phosphodiesterase From Escherichia Coli Provides Insight Into Function and Cooperativity of Trnase Z-Family Proteins. J.Bacteriol. V. 188 1607 2006.
ISSN: ISSN 0021-9193
PubMed: 16452444
DOI: 10.1128/JB.188.4.1607-1614.2006