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