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; PubMed: 19883117; DOI: 10.1021/bi901573b

Experimental method

X-RAY DIFFRACTION (1.7 Å)