Zinc in PDB 2zbm: Crystal Structure of I115M Mutant Cold-Active Protein Tyrosine Phosphatase

All present enzymatic activity of Crystal Structure of I115M Mutant Cold-Active Protein Tyrosine Phosphatase:
3.1.3.48;

The structure of Crystal Structure of I115M Mutant Cold-Active Protein Tyrosine Phosphatase, PDB code: 2zbm was solved by H.Tsuruta, B.Mikami, C.Yamamoto, H.Yamagata, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 1.50
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	54.172, 77.559, 80.331, 90.00, 90.00, 90.00
R / Rfree (%)	12.2 / 19.7

The binding sites of Zinc atom in the Crystal Structure of I115M Mutant Cold-Active Protein Tyrosine Phosphatase (pdb code 2zbm). 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 I115M Mutant Cold-Active Protein Tyrosine Phosphatase, PDB code: 2zbm:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of I115M Mutant Cold-Active Protein Tyrosine Phosphatase


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 I115M Mutant Cold-Active Protein Tyrosine Phosphatase within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn401 b:15.9 occ:1.00 O A:HOH1240 1.9 15.9 1.0 OD1 A:ASP78 1.9 16.1 1.0 NE2 A:HIS80 2.0 14.0 1.0 O A:HOH1239 2.1 15.7 1.0 OD1 A:ASP114 2.2 12.3 1.0 CE1 A:HIS80 3.0 13.8 1.0 CG A:ASP78 3.0 13.5 1.0 CD2 A:HIS80 3.0 13.1 1.0 CG A:ASP114 3.2 11.7 1.0 ZN A:ZN402 3.2 14.9 1.0 CB A:ASP114 3.5 13.4 1.0 CB A:ASP78 3.6 14.8 1.0 O A:HOH1232 4.1 35.8 1.0 OD2 A:ASP78 4.1 14.6 1.0 OD1 A:ASP304 4.1 17.1 1.0 ND1 A:HIS80 4.1 15.1 1.0 O A:HIS286 4.2 16.7 1.0 CE1 A:HIS207 4.2 12.3 1.0 CG A:HIS80 4.2 16.2 1.0 NE2 A:HIS207 4.2 13.4 1.0 O A:HOH1279 4.3 25.5 1.0 OD2 A:ASP114 4.3 13.6 1.0 CA A:ASP78 4.4 13.9 1.0 CA A:HIS286 4.4 14.6 1.0 CD2 A:HIS150 4.4 14.1 1.0 C A:HIS286 4.7 16.3 1.0 O A:HOH1314 4.7 53.2 1.0 NE2 A:HIS150 4.8 13.4 1.0 ND2 A:ASN149 4.8 12.0 1.0 ND1 A:HIS286 4.9 15.1 1.0 N A:HIS286 4.9 15.1 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of I115M Mutant Cold-Active Protein Tyrosine Phosphatase


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 I115M Mutant Cold-Active Protein Tyrosine Phosphatase within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn402 b:14.9 occ:1.00 O A:HOH1240 2.0 15.9 1.0 NE2 A:HIS207 2.0 13.4 1.0 ND2 A:ASN149 2.1 12.0 1.0 ND1 A:HIS286 2.2 15.1 1.0 OD1 A:ASP114 2.3 12.3 1.0 CE1 A:HIS207 3.0 12.3 1.0 CD2 A:HIS207 3.0 13.8 1.0 CE1 A:HIS286 3.1 17.4 1.0 CG A:ASN149 3.2 16.4 1.0 CG A:HIS286 3.2 16.4 1.0 ZN A:ZN401 3.2 15.9 1.0 CG A:ASP114 3.2 11.7 1.0 O A:HOH1279 3.4 25.5 1.0 CA A:HIS286 3.6 14.6 1.0 OD2 A:ASP114 3.6 13.6 1.0 CB A:HIS286 3.6 16.3 1.0 OD1 A:ASP78 3.6 16.1 1.0 OD1 A:ASN149 3.6 19.2 1.0 O A:HIS286 4.1 16.7 1.0 CD2 A:HIS150 4.1 14.1 1.0 ND1 A:HIS207 4.1 14.7 1.0 CG A:HIS207 4.2 15.4 1.0 NE2 A:HIS286 4.3 18.6 1.0 CD2 A:HIS286 4.3 17.8 1.0 C A:HIS286 4.4 16.3 1.0 CB A:ASN149 4.4 13.9 1.0 N A:ASN149 4.4 12.3 1.0 CB A:ASP114 4.5 13.4 1.0 N A:HIS286 4.6 15.1 1.0 O A:THR255 4.6 16.8 1.0 NE2 A:HIS150 4.7 13.4 1.0 O A:HOH1239 4.7 15.7 1.0 CG A:ASP78 4.8 13.5 1.0 NE2 A:HIS80 4.9 14.0 1.0 CA A:ASN149 4.9 12.8 1.0

H.Tsuruta, B.Mikami, C.Yamamoto, H.Yamagata. The Role of Group Bulkiness in the Catalytic Activity of Psychrophile Cold-Active Protein Tyrosine Phosphatase Febs J. V. 275 4317 2008.
ISSN: ISSN 1742-464X
PubMed: 18647345
DOI: 10.1111/J.1742-4658.2008.06575.X