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Atomistry » Magnesium » PDB 2ppq-2q0e » 2q0e | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Magnesium » PDB 2ppq-2q0e » 2q0e » |
Magnesium in PDB 2q0e: Terminal Uridylyl Transferase 4 From Trypanosoma Brucei with Bound GtpEnzymatic activity of Terminal Uridylyl Transferase 4 From Trypanosoma Brucei with Bound Gtp
All present enzymatic activity of Terminal Uridylyl Transferase 4 From Trypanosoma Brucei with Bound Gtp:
2.7.7.52; Protein crystallography data
The structure of Terminal Uridylyl Transferase 4 From Trypanosoma Brucei with Bound Gtp, PDB code: 2q0e
was solved by
J.Stagno,
H.Luecke,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Terminal Uridylyl Transferase 4 From Trypanosoma Brucei with Bound Gtp
(pdb code 2q0e). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Terminal Uridylyl Transferase 4 From Trypanosoma Brucei with Bound Gtp, PDB code: 2q0e: Jump to Magnesium binding site number: 1; 2; Magnesium binding site 1 out of 2 in 2q0eGo back to![]() ![]()
Magnesium binding site 1 out
of 2 in the Terminal Uridylyl Transferase 4 From Trypanosoma Brucei with Bound Gtp
![]() Mono view ![]() Stereo pair view
Magnesium binding site 2 out of 2 in 2q0eGo back to![]() ![]()
Magnesium binding site 2 out
of 2 in the Terminal Uridylyl Transferase 4 From Trypanosoma Brucei with Bound Gtp
![]() Mono view ![]() Stereo pair view
Reference:
J.Stagno,
I.Aphasizheva,
R.Aphasizhev,
H.Luecke.
Dual Role of the Rna Substrate in Selectivity and Catalysis By Terminal Uridylyl Transferases. Proc.Natl.Acad.Sci.Usa V. 104 14634 2007.
Page generated: Wed Aug 14 02:23:50 2024
ISSN: ISSN 0027-8424 PubMed: 17785418 DOI: 10.1073/PNAS.0704259104 |
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