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Atomistry » Zinc » PDB 1h71-1hld » 1hk8 » |
Zinc in PDB 1hk8: Structural Basis For Allosteric Substrate Specificity Regulation in Class III Ribonucleotide Reductases: Nrdd in Complex with DgtpEnzymatic activity of Structural Basis For Allosteric Substrate Specificity Regulation in Class III Ribonucleotide Reductases: Nrdd in Complex with Dgtp
All present enzymatic activity of Structural Basis For Allosteric Substrate Specificity Regulation in Class III Ribonucleotide Reductases: Nrdd in Complex with Dgtp:
1.17.4.2; Protein crystallography data
The structure of Structural Basis For Allosteric Substrate Specificity Regulation in Class III Ribonucleotide Reductases: Nrdd in Complex with Dgtp, PDB code: 1hk8
was solved by
K.-M.Larsson,
J.Andersson,
B.-M.Sjoeberg,
P.Nordlund,
D.T.Logan,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 1hk8:
The structure of Structural Basis For Allosteric Substrate Specificity Regulation in Class III Ribonucleotide Reductases: Nrdd in Complex with Dgtp also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Structural Basis For Allosteric Substrate Specificity Regulation in Class III Ribonucleotide Reductases: Nrdd in Complex with Dgtp
(pdb code 1hk8). 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 Structural Basis For Allosteric Substrate Specificity Regulation in Class III Ribonucleotide Reductases: Nrdd in Complex with Dgtp, PDB code: 1hk8: Zinc binding site 1 out of 1 in 1hk8Go back to![]() ![]()
Zinc binding site 1 out
of 1 in the Structural Basis For Allosteric Substrate Specificity Regulation in Class III Ribonucleotide Reductases: Nrdd in Complex with Dgtp
![]() Mono view ![]() Stereo pair view
Reference:
D.T.Logan,
E.Mulliez,
K.-M.Larsson,
S.Bodevin,
M.Atta,
P.E.Garnaud,
B.-M.Sjoberg,
M.Fontecave.
A Metal-Binding Site in the Catalytic Subunit of Anaerobic Ribonucleotide Reductase. Proc.Natl.Acad.Sci.Usa V. 100 3826 2003.
Page generated: Sun Oct 13 02:15:47 2024
ISSN: ISSN 0027-8424 PubMed: 12655046 DOI: 10.1073/PNAS.0736456100 |
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