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Atomistry » Sodium » PDB 1t4b-1u8r » 1tae | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Sodium » PDB 1t4b-1u8r » 1tae » |
Sodium in PDB 1tae: Structural Rearrangement Accompanying Nad+ Synthesis Within A Bacterial Dna Ligase CrystalEnzymatic activity of Structural Rearrangement Accompanying Nad+ Synthesis Within A Bacterial Dna Ligase Crystal
All present enzymatic activity of Structural Rearrangement Accompanying Nad+ Synthesis Within A Bacterial Dna Ligase Crystal:
6.5.1.2; Protein crystallography data
The structure of Structural Rearrangement Accompanying Nad+ Synthesis Within A Bacterial Dna Ligase Crystal, PDB code: 1tae
was solved by
K.S.Gajiwala,
C.Pinko,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Sodium Binding Sites:
The binding sites of Sodium atom in the Structural Rearrangement Accompanying Nad+ Synthesis Within A Bacterial Dna Ligase Crystal
(pdb code 1tae). This binding sites where shown within
5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the Structural Rearrangement Accompanying Nad+ Synthesis Within A Bacterial Dna Ligase Crystal, PDB code: 1tae: Jump to Sodium binding site number: 1; 2; Sodium binding site 1 out of 2 in 1taeGo back to![]() ![]()
Sodium binding site 1 out
of 2 in the Structural Rearrangement Accompanying Nad+ Synthesis Within A Bacterial Dna Ligase Crystal
![]() Mono view ![]() Stereo pair view
Sodium binding site 2 out of 2 in 1taeGo back to![]() ![]()
Sodium binding site 2 out
of 2 in the Structural Rearrangement Accompanying Nad+ Synthesis Within A Bacterial Dna Ligase Crystal
![]() Mono view ![]() Stereo pair view
Reference:
K.S.Gajiwala,
C.Pinko.
Structural Rearrangement Accompanying Nad+ Synthesis Within A Bacterial Dna Ligase Crystal. Structure V. 12 1449 2004.
Page generated: Sun Oct 6 22:37:56 2024
ISSN: ISSN 0969-2126 PubMed: 15296738 DOI: 10.1016/J.STR.2004.05.017 |
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