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Atomistry » Cobalt » PDB 1a0c-1e1c » 1b6a | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Cobalt » PDB 1a0c-1e1c » 1b6a » |
Cobalt in PDB 1b6a: Human Methionine Aminopeptidase 2 Complexed with Tnp-470Enzymatic activity of Human Methionine Aminopeptidase 2 Complexed with Tnp-470
All present enzymatic activity of Human Methionine Aminopeptidase 2 Complexed with Tnp-470:
3.4.11.18; Protein crystallography data
The structure of Human Methionine Aminopeptidase 2 Complexed with Tnp-470, PDB code: 1b6a
was solved by
S.Liu,
J.C.Clardy,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 1b6a:
The structure of Human Methionine Aminopeptidase 2 Complexed with Tnp-470 also contains other interesting chemical elements:
Cobalt Binding Sites:
The binding sites of Cobalt atom in the Human Methionine Aminopeptidase 2 Complexed with Tnp-470
(pdb code 1b6a). This binding sites where shown within
5.0 Angstroms radius around Cobalt atom.
In total 2 binding sites of Cobalt where determined in the Human Methionine Aminopeptidase 2 Complexed with Tnp-470, PDB code: 1b6a: Jump to Cobalt binding site number: 1; 2; Cobalt binding site 1 out of 2 in 1b6aGo back to![]() ![]()
Cobalt binding site 1 out
of 2 in the Human Methionine Aminopeptidase 2 Complexed with Tnp-470
![]() Mono view ![]() Stereo pair view
Cobalt binding site 2 out of 2 in 1b6aGo back to![]() ![]()
Cobalt binding site 2 out
of 2 in the Human Methionine Aminopeptidase 2 Complexed with Tnp-470
![]() 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: Sun Dec 13 10:34:13 2020
ISSN: ISSN 0036-8075 PubMed: 9812898 DOI: 10.1126/SCIENCE.282.5392.1324 |
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