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Atomistry » Cobalt » PDB 4rut-4xc6 » 4u75 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Cobalt » PDB 4rut-4xc6 » 4u75 » |
Cobalt in PDB 4u75: Hsmetap (F309M) in Complex with MethionineEnzymatic activity of Hsmetap (F309M) in Complex with Methionine
All present enzymatic activity of Hsmetap (F309M) in Complex with Methionine:
3.4.11.18; Protein crystallography data
The structure of Hsmetap (F309M) in Complex with Methionine, PDB code: 4u75
was solved by
T.Arya,
A.Addlagatta,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 4u75:
The structure of Hsmetap (F309M) in Complex with Methionine also contains other interesting chemical elements:
Cobalt Binding Sites:
The binding sites of Cobalt atom in the Hsmetap (F309M) in Complex with Methionine
(pdb code 4u75). This binding sites where shown within
5.0 Angstroms radius around Cobalt atom.
In total 2 binding sites of Cobalt where determined in the Hsmetap (F309M) in Complex with Methionine, PDB code: 4u75: Jump to Cobalt binding site number: 1; 2; Cobalt binding site 1 out of 2 in 4u75Go back to Cobalt Binding Sites List in 4u75
Cobalt binding site 1 out
of 2 in the Hsmetap (F309M) in Complex with Methionine
Mono view Stereo pair view
Cobalt binding site 2 out of 2 in 4u75Go back to Cobalt Binding Sites List in 4u75
Cobalt binding site 2 out
of 2 in the Hsmetap (F309M) in Complex with Methionine
Mono view Stereo pair view
Reference:
T.Arya,
R.Reddi,
C.Kishor,
R.J.Ganji,
S.Bhukya,
R.Gumpena,
S.Mcgowan,
M.Drag,
A.Addlagatta.
Identification of the Molecular Basis of Inhibitor Selectivity Between the Human and Streptococcal Type I Methionine Aminopeptidases J.Med.Chem. V. 58 2350 2015.
Page generated: Sun Dec 13 10:46:03 2020
ISSN: ISSN 0022-2623 PubMed: 25699713 DOI: 10.1021/JM501790E |
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