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Zinc in PDB 1taq: Structure of Taq Dna Polymerase

Enzymatic activity of Structure of Taq Dna Polymerase

All present enzymatic activity of Structure of Taq Dna Polymerase:
2.7.7.7;

Protein crystallography data

The structure of Structure of Taq Dna Polymerase, PDB code: 1taq was solved by Y.Kim, S.H.Eom, J.Wang, D.-S.Lee, S.W.Suh, T.A.Steitz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.00 / 2.40
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 107.421, 107.421, 170.245, 90.00, 90.00, 120.00
R / Rfree (%) 20.2 / 32.3

Zinc Binding Sites:

The binding sites of Zinc atom in the Structure of Taq Dna Polymerase (pdb code 1taq). 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 Structure of Taq Dna Polymerase, PDB code: 1taq:

Zinc binding site 1 out of 1 in 1taq

Go back to Zinc Binding Sites List in 1taq
Zinc binding site 1 out of 1 in the Structure of Taq Dna Polymerase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Taq Dna Polymerase 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 2.2 64.6 1.0
OD1 A:ASP119 2.2 60.8 1.0
CG A:ASP18 3.0 54.9 1.0
CG A:ASP142 3.1 63.6 1.0
CG A:ASP119 3.1 57.9 1.0
CD1 A:LEU122 3.4 41.0 1.0
OD2 A:ASP119 3.5 64.5 1.0
OG1 A:THR140 3.5 45.7 1.0
OD2 A:ASP142 3.5 65.4 1.0
CD2 A:HIS21 3.6 70.2 1.0
OD1 A:ASP18 3.6 57.2 1.0
CD1 A:LEU145 3.7 69.1 1.0
CB A:ASP18 3.8 45.8 1.0
CG A:LEU145 4.1 67.5 1.0
CB A:ASP142 4.2 64.3 1.0
CG A:HIS21 4.3 68.5 1.0
CB A:ASP119 4.4 50.5 1.0
CB A:HIS21 4.4 58.4 1.0
CD2 A:LEU145 4.5 64.3 1.0
CB A:THR140 4.5 49.1 1.0
CA A:ASP119 4.6 47.1 1.0
NE2 A:HIS21 4.6 74.8 1.0
CG A:LEU122 4.9 36.3 1.0
N A:ASP119 5.0 42.2 1.0

Reference:

Y.Kim, S.H.Eom, J.Wang, D.S.Lee, S.W.Suh, T.A.Steitz. Crystal Structure of Thermus Aquaticus Dna Polymerase. Nature V. 376 612 1995.
ISSN: ISSN 0028-0836
PubMed: 7637814
DOI: 10.1038/376612A0
Page generated: Mon Jan 25 16:13:53 2021

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