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Atomistry » Zinc » PDB 4fvt-4g2w » 4g25 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Zinc » PDB 4fvt-4g2w » 4g25 » |
Zinc in PDB 4g25: Crystal Structure of Proteinaceous Rnase P 1 (PRORP1) From A. Thaliana, Semet Substituted Form with SrEnzymatic activity of Crystal Structure of Proteinaceous Rnase P 1 (PRORP1) From A. Thaliana, Semet Substituted Form with Sr
All present enzymatic activity of Crystal Structure of Proteinaceous Rnase P 1 (PRORP1) From A. Thaliana, Semet Substituted Form with Sr:
3.1.26.5; Protein crystallography data
The structure of Crystal Structure of Proteinaceous Rnase P 1 (PRORP1) From A. Thaliana, Semet Substituted Form with Sr, PDB code: 4g25
was solved by
M.Koutmos,
M.J.Howard,
C.A.Fierke,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 4g25:
The structure of Crystal Structure of Proteinaceous Rnase P 1 (PRORP1) From A. Thaliana, Semet Substituted Form with Sr also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Crystal Structure of Proteinaceous Rnase P 1 (PRORP1) From A. Thaliana, Semet Substituted Form with Sr
(pdb code 4g25). 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 Crystal Structure of Proteinaceous Rnase P 1 (PRORP1) From A. Thaliana, Semet Substituted Form with Sr, PDB code: 4g25: Zinc binding site 1 out of 1 in 4g25Go back to Zinc Binding Sites List in 4g25
Zinc binding site 1 out
of 1 in the Crystal Structure of Proteinaceous Rnase P 1 (PRORP1) From A. Thaliana, Semet Substituted Form with Sr
Mono view Stereo pair view
Reference:
M.J.Howard,
W.H.Lim,
C.A.Fierke,
M.Koutmos.
Mitochondrial Ribonuclease P Structure Provides Insight Into the Evolution of Catalytic Strategies For Precursor-Trna 5' Processing. Proc.Natl.Acad.Sci.Usa V. 109 16149 2012.
Page generated: Wed Dec 16 05:18:51 2020
ISSN: ISSN 0027-8424 PubMed: 22991464 DOI: 10.1073/PNAS.1209062109 |
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