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2GGP
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BU of 2ggp by Molmil
Solution structure of the Atx1-Cu(I)-Ccc2a complex
Descriptor: COPPER (I) ION, Metal homeostasis factor ATX1, Probable copper-transporting ATPase
Authors:Banci, L, Bertini, I, Cantini, F, Felli, I.C, Gonnelli, L, Hadjiliadis, N, Pierattelli, R, Rosato, A, Voulgaris, P, Structural Proteomics in Europe (SPINE)
Deposit date:2006-03-24
Release date:2006-08-08
Last modified:2022-03-09
Method:SOLUTION NMR
Cite:The Atx1-Ccc2 complex is a metal-mediated protein-protein interaction.
Nat.Chem.Biol., 2, 2006
1Y3J
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BU of 1y3j by Molmil
Solution structure of the copper(I) form of the fifth domain of Menkes protein
Descriptor: COPPER (II) ION, Copper-transporting ATPase 1
Authors:Banci, L, Chasapis, C.T, Ciofi-Baffoni, S, Hadjiliadis, N, Rosato, A, Structural Proteomics in Europe (SPINE)
Deposit date:2004-11-25
Release date:2005-03-08
Last modified:2022-03-02
Method:SOLUTION NMR
Cite:An NMR study of the interaction between the human copper(I) chaperone and the second and fifth metal-binding domains of the Menkes protein
Febs J., 272, 2005
1Y3K
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BU of 1y3k by Molmil
Solution structure of the apo form of the fifth domain of Menkes protein
Descriptor: Copper-transporting ATPase 1
Authors:Banci, L, Chasapis, C.T, Ciofi-Baffoni, S, Hadjiliadis, N, Rosato, A, Structural Proteomics in Europe (SPINE)
Deposit date:2004-11-25
Release date:2005-03-08
Last modified:2022-03-02
Method:SOLUTION NMR
Cite:An NMR study of the interaction between the human copper(I) chaperone and the second and fifth metal-binding domains of the Menkes protein
Febs J., 272, 2005
3CJK
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BU of 3cjk by Molmil
Crystal structure of the adduct HAH1-Cd(II)-MNK1.
Descriptor: CADMIUM ION, Copper transport protein ATOX1, Copper-transporting ATPase 1
Authors:Banci, L, Bertini, I, Calderone, V, Felli, I, Della-Malva, N, Pavelkova, A, Rosato, A.
Deposit date:2008-03-13
Release date:2008-12-30
Last modified:2023-08-30
Method:X-RAY DIFFRACTION (1.8 Å)
Cite:Copper(I)-mediated protein-protein interactions result from suboptimal interaction surfaces.
Biochem.J., 422, 2009

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