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Atomistry » Cobalt » PDB 1a0c-1e1c » 1b59 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Cobalt » PDB 1a0c-1e1c » 1b59 » |
Cobalt in PDB 1b59: Complex of Human Methionine Aminopeptidase-2 Complexed with OvalicinEnzymatic activity of Complex of Human Methionine Aminopeptidase-2 Complexed with Ovalicin
All present enzymatic activity of Complex of Human Methionine Aminopeptidase-2 Complexed with Ovalicin:
3.4.11.18; Protein crystallography data
The structure of Complex of Human Methionine Aminopeptidase-2 Complexed with Ovalicin, PDB code: 1b59
was solved by
S.Liu,
J.C.Clardy,
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 Complex of Human Methionine Aminopeptidase-2 Complexed with Ovalicin
(pdb code 1b59). This binding sites where shown within
5.0 Angstroms radius around Cobalt atom.
In total 2 binding sites of Cobalt where determined in the Complex of Human Methionine Aminopeptidase-2 Complexed with Ovalicin, PDB code: 1b59: Jump to Cobalt binding site number: 1; 2; Cobalt binding site 1 out of 2 in 1b59Go back to Cobalt Binding Sites List in 1b59
Cobalt binding site 1 out
of 2 in the Complex of Human Methionine Aminopeptidase-2 Complexed with Ovalicin
Mono view Stereo pair view
Cobalt binding site 2 out of 2 in 1b59Go back to Cobalt Binding Sites List in 1b59
Cobalt binding site 2 out
of 2 in the Complex of Human Methionine Aminopeptidase-2 Complexed with Ovalicin
Mono view Stereo pair view
Reference:
S.Liu,
J.Widom,
C.W.Kemp,
C.M.Crews,
J.Clardy.
Structure of Human Methionine Aminopeptidase-2 Complexed with Fumagillin. Science V. 282 1324 1998.
Page generated: Tue Jul 30 14:06:53 2024
ISSN: ISSN 0036-8075 PubMed: 9812898 DOI: 10.1126/SCIENCE.282.5392.1324 |
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