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Atomistry » Platinum » PDB 4nsj-5bna » 4qot | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Platinum » PDB 4nsj-5bna » 4qot » |
Platinum in PDB 4qot: Crystal Structure of Human Copper Chaperone Bound to the Platinum IonEnzymatic activity of Crystal Structure of Human Copper Chaperone Bound to the Platinum Ion
All present enzymatic activity of Crystal Structure of Human Copper Chaperone Bound to the Platinum Ion:
3.6.3.54; Protein crystallography data
The structure of Crystal Structure of Human Copper Chaperone Bound to the Platinum Ion, PDB code: 4qot
was solved by
B.D.Belviso,
A.Galliani,
R.Caliandro,
F.Arnesano,
G.Natile,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Platinum Binding Sites:
The binding sites of Platinum atom in the Crystal Structure of Human Copper Chaperone Bound to the Platinum Ion
(pdb code 4qot). This binding sites where shown within
5.0 Angstroms radius around Platinum atom.
In total 2 binding sites of Platinum where determined in the Crystal Structure of Human Copper Chaperone Bound to the Platinum Ion, PDB code: 4qot: Jump to Platinum binding site number: 1; 2; Platinum binding site 1 out of 2 in 4qotGo back to![]() ![]()
Platinum binding site 1 out
of 2 in the Crystal Structure of Human Copper Chaperone Bound to the Platinum Ion
![]() Mono view ![]() Stereo pair view
Platinum binding site 2 out of 2 in 4qotGo back to![]() ![]()
Platinum binding site 2 out
of 2 in the Crystal Structure of Human Copper Chaperone Bound to the Platinum Ion
![]() Mono view ![]() Stereo pair view
Reference:
B.D.Belviso,
A.Galliani,
A.Lasorsa,
V.Mirabelli,
R.Caliandro,
F.Arnesano,
G.Natile.
Oxaliplatin Binding to Human Copper Chaperone ATOX1 and Protein Dimerization Inorg.Chem. V. 55 6563 2016.
Page generated: Wed Dec 16 02:05:00 2020
ISSN: ISSN 0020-1669 PubMed: 27305454 DOI: 10.1021/ACS.INORGCHEM.6B00750 |
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