2K1R
The solution NMR structure of the complex between MNK1 and HAH1 mediated by Cu(I)
Summary for 2K1R
Entry DOI | 10.2210/pdb2k1r/pdb |
Related | 1KVJ 1TL4 3CJK |
Descriptor | Copper-transporting ATPase 1, Copper transport protein ATOX1, COPPER (II) ION (3 entities in total) |
Functional Keywords | mnk1, hah1, protein-protein interaction, atp7a, spine 2, structural proteomics in europe, alternative splicing, atp-binding, copper, copper transport, cytoplasm, disease mutation, endoplasmic reticulum, glycoprotein, golgi apparatus, hydrolase, ion transport, magnesium, membrane, metal-binding, nucleotide-binding, phosphoprotein, polymorphism, transmembrane, transport, chaperone, hydrolase-chaperone complex, structural genomics, hydrolase/chaperone |
Biological source | Homo sapiens (human) More |
Cellular location | Golgi apparatus, trans-Golgi network membrane; Multi-pass membrane protein. Isoform 3: Cytoplasm, cytosol (Probable). Isoform 5: Endoplasmic reticulum: Q04656 |
Total number of polymer chains | 2 |
Total formula weight | 15525.36 |
Authors | Bertini, I.,Banci, L.C.,Felli, I.C.,Pavelkova, A.,Rosato, A.,Structural Proteomics in Europe (SPINE) (deposition date: 2008-03-14, release date: 2009-03-31, Last modification date: 2022-03-16) |
Primary citation | Bertini, I.,Banci, L.C.,Felli, I.C.,Pavelkova, A.,Rosato, A. The solution structure of the copper(I)-mediated complex between the first soluble domain of the Menkes protein and the metallochaperone HAH1. To be Published, |
Experimental method | SOLUTION NMR |
Structure validation
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