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Atomistry » Cobalt » PDB 6kgh-6oxc » 6nnc » |
Cobalt in PDB 6nnc: Structure of Dihydrofolate Reductase From Mycobacterium Tuberculosis in Complex with Nadph and PemetrexedEnzymatic activity of Structure of Dihydrofolate Reductase From Mycobacterium Tuberculosis in Complex with Nadph and Pemetrexed
All present enzymatic activity of Structure of Dihydrofolate Reductase From Mycobacterium Tuberculosis in Complex with Nadph and Pemetrexed:
1.5.1.3; Protein crystallography data
The structure of Structure of Dihydrofolate Reductase From Mycobacterium Tuberculosis in Complex with Nadph and Pemetrexed, PDB code: 6nnc
was solved by
J.A.Ribeiro,
S.M.Chavez-Pacheco,
M.V.B.Dias,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Cobalt Binding Sites:
The binding sites of Cobalt atom in the Structure of Dihydrofolate Reductase From Mycobacterium Tuberculosis in Complex with Nadph and Pemetrexed
(pdb code 6nnc). This binding sites where shown within
5.0 Angstroms radius around Cobalt atom.
In total 2 binding sites of Cobalt where determined in the Structure of Dihydrofolate Reductase From Mycobacterium Tuberculosis in Complex with Nadph and Pemetrexed, PDB code: 6nnc: Jump to Cobalt binding site number: 1; 2; Cobalt binding site 1 out of 2 in 6nncGo back to![]() ![]()
Cobalt binding site 1 out
of 2 in the Structure of Dihydrofolate Reductase From Mycobacterium Tuberculosis in Complex with Nadph and Pemetrexed
![]() Mono view ![]() Stereo pair view
Cobalt binding site 2 out of 2 in 6nncGo back to![]() ![]()
Cobalt binding site 2 out
of 2 in the Structure of Dihydrofolate Reductase From Mycobacterium Tuberculosis in Complex with Nadph and Pemetrexed
![]() Mono view ![]() Stereo pair view
Reference:
J.A.Ribeiro,
S.M.Chavez-Pacheco,
G.S.De Oliveira,
C.D.S.Silva,
J.H.P.Giudice,
G.A.Libreros-Zuniga,
M.V.B.Dias.
Crystal Structures of the Closed Form of Mycobacterium Tuberculosis Dihydrofolate Reductase in Complex with Dihydrofolate and Antifolates. Acta Crystallogr D Struct V. 75 682 2019BIOL.
Page generated: Tue Jul 30 18:53:42 2024
ISSN: ISSN 2059-7983 PubMed: 31282477 DOI: 10.1107/S205979831900901X |
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