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Atomistry » Calcium » PDB 5vlk-5w4t » 5vmq | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Calcium » PDB 5vlk-5w4t » 5vmq » |
Calcium in PDB 5vmq: Structure of the R105A Mutant Catalytic Trimer of Escherichia Coli Aspartate Transcarbamoylase at 2.0-A ResolutionEnzymatic activity of Structure of the R105A Mutant Catalytic Trimer of Escherichia Coli Aspartate Transcarbamoylase at 2.0-A Resolution
All present enzymatic activity of Structure of the R105A Mutant Catalytic Trimer of Escherichia Coli Aspartate Transcarbamoylase at 2.0-A Resolution:
2.1.3.2; Protein crystallography data
The structure of Structure of the R105A Mutant Catalytic Trimer of Escherichia Coli Aspartate Transcarbamoylase at 2.0-A Resolution, PDB code: 5vmq
was solved by
P.T.Beernink,
J.A.Endrizzi,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 5vmq:
The structure of Structure of the R105A Mutant Catalytic Trimer of Escherichia Coli Aspartate Transcarbamoylase at 2.0-A Resolution also contains other interesting chemical elements:
Calcium Binding Sites:
The binding sites of Calcium atom in the Structure of the R105A Mutant Catalytic Trimer of Escherichia Coli Aspartate Transcarbamoylase at 2.0-A Resolution
(pdb code 5vmq). This binding sites where shown within
5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Structure of the R105A Mutant Catalytic Trimer of Escherichia Coli Aspartate Transcarbamoylase at 2.0-A Resolution, PDB code: 5vmq: Calcium binding site 1 out of 1 in 5vmqGo back to Calcium Binding Sites List in 5vmq
Calcium binding site 1 out
of 1 in the Structure of the R105A Mutant Catalytic Trimer of Escherichia Coli Aspartate Transcarbamoylase at 2.0-A Resolution
Mono view Stereo pair view
Reference:
J.A.Endrizzi,
P.T.Beernink.
Charge Neutralization in the Active Site of the Catalytic Trimer of Aspartate Transcarbamoylase Promotes Diverse Structural Changes. Protein Sci. V. 26 2221 2017.
Page generated: Mon Jul 15 12:34:32 2024
ISSN: ESSN 1469-896X PubMed: 28833948 DOI: 10.1002/PRO.3277 |
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