EC Number |
Subunits |
Reference |
---|
7.2.2.9 | ? |
x * 110000, SDS-PAGE |
719999 |
7.2.2.9 | ? |
x * 150000, SDS-PAGE |
719036 |
7.2.2.9 | ? |
x * 180000, ATP7A, SDS-PAGE, x * 165000, ATP7B, SDS-PAGE |
712175 |
7.2.2.9 | ? |
x * 195000, GST-tagged enzyme, SDS-PAGE |
718542 |
7.2.2.9 | ? |
x * 97000, splicing variant in cytosol and plasma membrane, SDS-PAGE, x * 64000, splicing variant in nucleus, SDS-PAGE |
710815 |
7.2.2.9 | More |
analysis of the solution NMR structures of the N-domain of ATP7A in the ATP-free and ATP-bound forms, The structures consist of a twisted antiparallel six-stranded beta-sheet flanked by two pairs of alpha-helices, overview. Structure comparisons to Archeoglobus fulgidus CopA, overview |
712460 |
7.2.2.9 | More |
ATP7B from HEK-293 and Hep-G2 cells have different electrophoretic properties, ATP7B in Hep-G2 and HEK-293 cells differ in size, but not in post-translational modifications |
701335 |
7.2.2.9 | More |
PcpA comtains a heavy-metal-associated domain, a P-type ATPase domain, and a haloacid dehalogenase-like hydrolase domain |
-, 712728 |
7.2.2.9 | More |
peptide mapping and identification of putative Cu-responsive peptides, overview |
712170 |
7.2.2.9 | More |
small changes in individual sites, induced by copper binding or mutation, result in stabilization of distinct conformations of the entire N-ATP7B and altered exposure of sites for interactions with regulatory proteins. Structure modeling and molecular dynamics simulations, hydrogen bonding may play a role in the N-ATP7B folding and redox state, overview |
712486 |