Zinc in PDB 2z72: New Structure of Cold-Active Protein Tyrosine Phosphatase at 1.1 Angstrom

All present enzymatic activity of New Structure of Cold-Active Protein Tyrosine Phosphatase at 1.1 Angstrom:
3.1.3.48;

The structure of New Structure of Cold-Active Protein Tyrosine Phosphatase at 1.1 Angstrom, PDB code: 2z72 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)	8.00 / 1.10
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	55.565, 77.306, 81.029, 90.00, 90.00, 90.00
R / Rfree (%)	11 / 16.1

The binding sites of Zinc atom in the New Structure of Cold-Active Protein Tyrosine Phosphatase at 1.1 Angstrom (pdb code 2z72). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the New Structure of Cold-Active Protein Tyrosine Phosphatase at 1.1 Angstrom, PDB code: 2z72:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the New Structure of Cold-Active Protein Tyrosine Phosphatase at 1.1 Angstrom


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of New Structure of Cold-Active Protein Tyrosine Phosphatase at 1.1 Angstrom within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn401 b:9.9 occ:1.00 O A:HOH1269 2.0 11.7 1.0 OD1 A:ASP78 2.0 9.0 1.0 NE2 A:HIS80 2.0 9.0 1.0 O A:HOH1267 2.1 11.3 1.0 OD1 A:ASP114 2.2 9.2 1.0 CE1 A:HIS80 3.0 8.9 1.0 CD2 A:HIS80 3.0 9.3 1.0 CG A:ASP78 3.1 8.6 1.0 CG A:ASP114 3.2 8.3 1.0 ZN A:ZN402 3.2 9.4 1.0 CB A:ASP114 3.5 8.3 1.0 CB A:ASP78 3.7 8.9 1.0 O A:HOH1259 4.1 23.0 1.0 ND1 A:HIS80 4.1 9.4 1.0 OD2 A:ASP78 4.2 9.5 1.0 O A:HIS286 4.2 11.8 1.0 CE1 A:HIS207 4.2 8.7 1.0 NE2 A:HIS207 4.2 8.3 1.0 CG A:HIS80 4.2 8.7 1.0 OD1 A:ASP304 4.2 10.7 1.0 O A:HOH1587 4.3 17.8 1.0 OD2 A:ASP114 4.4 8.9 1.0 CA A:HIS286 4.4 10.5 1.0 CD2 A:HIS150 4.4 9.3 1.0 CA A:ASP78 4.4 8.5 1.0 C A:HIS286 4.7 11.5 1.0 NE2 A:HIS150 4.8 10.6 1.0 OD1 A:ASN149 4.8 9.4 1.0 ND1 A:HIS286 4.9 10.8 1.0 N A:HIS286 4.9 10.6 1.0 NE A:ARG118 5.0 31.8 0.5 CA A:ASP114 5.0 7.7 1.0

Zinc binding site 2 out of 2 in the New Structure of Cold-Active Protein Tyrosine Phosphatase at 1.1 Angstrom


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of New Structure of Cold-Active Protein Tyrosine Phosphatase at 1.1 Angstrom within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn402 b:9.4 occ:1.00 O A:HOH1269 2.0 11.7 1.0 NE2 A:HIS207 2.0 8.3 1.0 OD1 A:ASN149 2.1 9.4 1.0 ND1 A:HIS286 2.1 10.8 1.0 OD1 A:ASP114 2.3 9.2 1.0 CD2 A:HIS207 3.0 8.2 1.0 CE1 A:HIS207 3.0 8.7 1.0 CE1 A:HIS286 3.1 12.4 1.0 CG A:HIS286 3.1 11.2 1.0 CG A:ASN149 3.1 8.8 1.0 ZN A:ZN401 3.2 9.9 1.0 CG A:ASP114 3.2 8.3 1.0 O A:HOH1587 3.4 17.8 1.0 CB A:HIS286 3.5 10.9 1.0 CA A:HIS286 3.6 10.5 1.0 ND2 A:ASN149 3.6 10.7 1.0 OD2 A:ASP114 3.6 8.9 1.0 OD1 A:ASP78 3.7 9.0 1.0 O A:HIS286 4.1 11.8 1.0 CD2 A:HIS150 4.1 9.3 1.0 ND1 A:HIS207 4.1 8.3 1.0 CG A:HIS207 4.2 7.9 1.0 CD2 A:HIS286 4.2 13.0 1.0 NE2 A:HIS286 4.3 14.9 1.0 C A:HIS286 4.3 11.5 1.0 CB A:ASN149 4.4 9.1 1.0 CB A:ASP114 4.4 8.3 1.0 N A:ASN149 4.5 8.3 1.0 O A:THR255 4.6 10.4 1.0 N A:HIS286 4.6 10.6 1.0 NE2 A:HIS150 4.7 10.6 1.0 O A:HOH1267 4.8 11.3 1.0 CG A:ASP78 4.9 8.6 1.0 NE2 A:HIS80 4.9 9.0 1.0 CA A:ASN149 4.9 8.2 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