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Atomistry » Aluminium » PDB 1a6e-1tx4 » 1e2e » |
Aluminium in PDB 1e2e: Human Thymidylate Kinase Complexed with Thymidine Monophosphate, Adenosine Diphosphate,A Magnesium-Ion and ALF3Enzymatic activity of Human Thymidylate Kinase Complexed with Thymidine Monophosphate, Adenosine Diphosphate,A Magnesium-Ion and ALF3
All present enzymatic activity of Human Thymidylate Kinase Complexed with Thymidine Monophosphate, Adenosine Diphosphate,A Magnesium-Ion and ALF3:
2.7.4.9; Protein crystallography data
The structure of Human Thymidylate Kinase Complexed with Thymidine Monophosphate, Adenosine Diphosphate,A Magnesium-Ion and ALF3, PDB code: 1e2e
was solved by
N.Ostermann,
I.Schlichting,
R.Brundiers,
M.Konrad,
J.Reinstein,
T.Veit,
R.S.Goody,
A.Lavie,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 1e2e:
The structure of Human Thymidylate Kinase Complexed with Thymidine Monophosphate, Adenosine Diphosphate,A Magnesium-Ion and ALF3 also contains other interesting chemical elements:
Aluminium Binding Sites:
The binding sites of Aluminium atom in the Human Thymidylate Kinase Complexed with Thymidine Monophosphate, Adenosine Diphosphate,A Magnesium-Ion and ALF3
(pdb code 1e2e). This binding sites where shown within
5.0 Angstroms radius around Aluminium atom.
In total only one binding site of Aluminium was determined in the Human Thymidylate Kinase Complexed with Thymidine Monophosphate, Adenosine Diphosphate,A Magnesium-Ion and ALF3, PDB code: 1e2e: Aluminium binding site 1 out of 1 in 1e2eGo back to![]() ![]()
Aluminium binding site 1 out
of 1 in the Human Thymidylate Kinase Complexed with Thymidine Monophosphate, Adenosine Diphosphate,A Magnesium-Ion and ALF3
![]() Mono view ![]() Stereo pair view
Reference:
N.Ostermann,
I.Schlichting,
R.Brundiers,
M.Konrad,
J.Reinstein,
T.Veit,
R.S.Goody,
A.Lavie.
Insights Into the Phosphoryltransfer Mechanism of Human Thymidylate Kinase Gained From Crystal Structures of Enzyme Complexes Along the Reaction Coordinate Structure V. 8 629 2000.
Page generated: Sun Jul 6 21:34:15 2025
ISSN: ISSN 0969-2126 PubMed: 10873853 DOI: 10.1016/S0969-2126(00)00149-0 |
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