3DXS
Crystal structure of a copper binding domain from HMA7, a P-type ATPase
Summary for 3DXS
Entry DOI | 10.2210/pdb3dxs/pdb |
Related | 1fee 1osd |
Descriptor | Copper-transporting ATPase RAN1, ZINC ION, LITHIUM ION, ... (4 entities in total) |
Functional Keywords | copper transport, cxxc motif, ferredoxin-like fold, atp-binding, copper, ethylene signaling pathway, hydrolase, ion transport, magnesium, membrane, metal-binding, nucleotide-binding, phosphoprotein, transmembrane, transport |
Biological source | Arabidopsis thaliana (mouse-ear cress) |
Cellular location | Membrane; Multi-pass membrane protein: Q9S7J8 |
Total number of polymer chains | 1 |
Total formula weight | 8137.47 |
Authors | Zimmermann, M.,Xiao, Z.,Clarke, O.B.,Gulbis, J.M.,Wedd, A.G. (deposition date: 2008-07-25, release date: 2009-08-11, Last modification date: 2021-11-10) |
Primary citation | Zimmermann, M.,Clarke, O.B.,Gulbis, J.M.,Keizer, D.W.,Jarvis, R.S.,Cobbett, C.S.,Hinds, M.G.,Xiao, Z.,Wedd, A.G. Metal binding affinities of Arabidopsis zinc and copper transporters: selectivities match the relative, but not the absolute, affinities of their amino-terminal domains. Biochemistry, 48:11640-11654, 2009 Cited by PubMed: 19883117DOI: 10.1021/bi901573b PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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