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Atomistry » Sodium » PDB 1z2u-1zud » 1za2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Sodium » PDB 1z2u-1zud » 1za2 » |
Sodium in PDB 1za2: Structure of Wild-Type E. Coli Aspartate Transcarbamoylase in the Presence of Ctp, Carbamoyl Phosphate at 2.50 A ResolutionEnzymatic activity of Structure of Wild-Type E. Coli Aspartate Transcarbamoylase in the Presence of Ctp, Carbamoyl Phosphate at 2.50 A Resolution
All present enzymatic activity of Structure of Wild-Type E. Coli Aspartate Transcarbamoylase in the Presence of Ctp, Carbamoyl Phosphate at 2.50 A Resolution:
2.1.3.2; Protein crystallography data
The structure of Structure of Wild-Type E. Coli Aspartate Transcarbamoylase in the Presence of Ctp, Carbamoyl Phosphate at 2.50 A Resolution, PDB code: 1za2
was solved by
J.Wang,
K.A.Stieglitz,
J.P.Cardia,
E.R.Kantrowitz,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 1za2:
The structure of Structure of Wild-Type E. Coli Aspartate Transcarbamoylase in the Presence of Ctp, Carbamoyl Phosphate at 2.50 A Resolution also contains other interesting chemical elements:
Sodium Binding Sites:
The binding sites of Sodium atom in the Structure of Wild-Type E. Coli Aspartate Transcarbamoylase in the Presence of Ctp, Carbamoyl Phosphate at 2.50 A Resolution
(pdb code 1za2). This binding sites where shown within
5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Structure of Wild-Type E. Coli Aspartate Transcarbamoylase in the Presence of Ctp, Carbamoyl Phosphate at 2.50 A Resolution, PDB code: 1za2: Sodium binding site 1 out of 1 in 1za2Go back to![]() ![]()
Sodium binding site 1 out
of 1 in the Structure of Wild-Type E. Coli Aspartate Transcarbamoylase in the Presence of Ctp, Carbamoyl Phosphate at 2.50 A Resolution
![]() Mono view ![]() Stereo pair view
Reference:
J.Wang,
K.A.Stieglitz,
J.P.Cardia,
E.R.Kantrowitz.
Structural Basis For Ordered Substrate Binding and Cooperativity in Aspartate Transcarbamoylase Proc.Natl.Acad.Sci.Usa V. 102 8881 2005.
Page generated: Mon Oct 7 01:40:51 2024
ISSN: ISSN 0027-8424 PubMed: 15951418 DOI: 10.1073/PNAS.0503742102 |
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