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Atomistry » Cobalt » PDB 8im2-8sfb » 8kho » |
Cobalt in PDB 8kho: Crystal Structure of Human Methionine Aminopeptidase 12 (MAP12) in Complex with Two Cobalt Ions and MethionineEnzymatic activity of Crystal Structure of Human Methionine Aminopeptidase 12 (MAP12) in Complex with Two Cobalt Ions and Methionine
All present enzymatic activity of Crystal Structure of Human Methionine Aminopeptidase 12 (MAP12) in Complex with Two Cobalt Ions and Methionine:
3.4.11.18; Protein crystallography data
The structure of Crystal Structure of Human Methionine Aminopeptidase 12 (MAP12) in Complex with Two Cobalt Ions and Methionine, PDB code: 8kho
was solved by
Y.Lee,
E.Lee,
H.Hahn,
H.Kim,
Y.Heo,
D.M.Jang,
H.J.Kim,
H.S.Kim,
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 Crystal Structure of Human Methionine Aminopeptidase 12 (MAP12) in Complex with Two Cobalt Ions and Methionine
(pdb code 8kho). This binding sites where shown within
5.0 Angstroms radius around Cobalt atom.
In total 2 binding sites of Cobalt where determined in the Crystal Structure of Human Methionine Aminopeptidase 12 (MAP12) in Complex with Two Cobalt Ions and Methionine, PDB code: 8kho: Jump to Cobalt binding site number: 1; 2; Cobalt binding site 1 out of 2 in 8khoGo back to Cobalt Binding Sites List in 8kho
Cobalt binding site 1 out
of 2 in the Crystal Structure of Human Methionine Aminopeptidase 12 (MAP12) in Complex with Two Cobalt Ions and Methionine
Mono view Stereo pair view
Cobalt binding site 2 out of 2 in 8khoGo back to Cobalt Binding Sites List in 8kho
Cobalt binding site 2 out
of 2 in the Crystal Structure of Human Methionine Aminopeptidase 12 (MAP12) in Complex with Two Cobalt Ions and Methionine
Mono view Stereo pair view
Reference:
Y.Lee,
H.Kim,
E.Lee,
H.Hahn,
Y.Heo,
D.M.Jang,
K.Kwak,
H.J.Kim,
H.S.Kim.
Structural Insights Into N-Terminal Methionine Cleavage By the Human Mitochondrial Methionine Aminopeptidase, METAP1D. Sci Rep V. 13 22326 2023.
Page generated: Tue Jul 30 19:57:40 2024
ISSN: ESSN 2045-2322 PubMed: 38102161 DOI: 10.1038/S41598-023-49332-6 |
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