Zinc in PDB 1tau: Taq Polymerase (E.C.2.7.7.7)/Dna/B-Octylglucoside Complex

All present enzymatic activity of Taq Polymerase (E.C.2.7.7.7)/Dna/B-Octylglucoside Complex:
2.7.7.7;

The structure of Taq Polymerase (E.C.2.7.7.7)/Dna/B-Octylglucoside Complex, PDB code: 1tau was solved by S.H.Eom, J.Wang, T.A.Steitz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 3.00
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	107.600, 107.600, 170.010, 90.00, 90.00, 120.00
R / Rfree (%)	24.4 / 30.5

The binding sites of Zinc atom in the Taq Polymerase (E.C.2.7.7.7)/Dna/B-Octylglucoside Complex (pdb code 1tau). 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 Taq Polymerase (E.C.2.7.7.7)/Dna/B-Octylglucoside Complex, PDB code: 1tau:

Zinc binding site 1 out of 1 in the Taq Polymerase (E.C.2.7.7.7)/Dna/B-Octylglucoside Complex


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Taq Polymerase (E.C.2.7.7.7)/Dna/B-Octylglucoside Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn900 b:58.5 occ:1.00 OD2 A:ASP18 2.2 58.9 1.0 OD1 A:ASP142 2.3 64.6 1.0 CD2 A:HIS21 2.6 70.2 1.0 OD2 A:ASP119 2.6 64.5 1.0 OD1 A:ASP119 2.6 60.8 1.0 CG A:ASP119 2.7 57.9 1.0 CG A:ASP142 2.8 63.6 1.0 OD2 A:ASP142 3.1 65.4 1.0 CG A:ASP18 3.3 54.9 1.0 NE2 A:HIS21 3.4 74.8 1.0 CG A:HIS21 3.5 68.5 1.0 HE2 A:HIS21 3.7 0.0 1.0 OD1 A:ASP18 3.7 57.2 1.0 HG1 A:THR140 3.9 0.0 1.0 CB A:ASP119 3.9 50.5 1.0 CB A:ASP142 4.0 64.3 1.0 CB A:HIS21 4.0 58.4 1.0 OG1 A:THR140 4.1 45.7 1.0 CD1 A:LEU145 4.4 69.1 1.0 CB A:ASP18 4.5 45.8 1.0 CE1 A:HIS21 4.5 71.8 1.0 ND1 A:HIS21 4.5 73.0 1.0 CA A:ASP119 4.6 47.1 1.0 CD1 A:LEU122 4.6 41.0 1.0 H A:ASP142 4.7 0.0 1.0 H A:HIS21 4.9 0.0 1.0 N A:ASP119 5.0 42.2 1.0

S.H.Eom, J.Wang, T.A.Steitz. Structure of Taq Ploymerase with Dna at the Polymerase Active Site. Nature V. 382 278 1996.
ISSN: ISSN 0028-0836
PubMed: 8717047
DOI: 10.1038/382278A0