EC Number |
Reference |
---|
7.2.2.8 | - |
688411 |
7.2.2.8 | NMR structure of metal-binding domain MBD1, shows the characteristic beta,alpha,beta,beta,alpha,beta ferredoxin fold. The copper binding motif CxxC appears to experience complex dynamics |
752245 |
7.2.2.8 | sitting drop method, crystal structure of the apo, oxidized C-terminal-metal binding domain to 2.0 A resolution. In the structure, two C-terminal-metal binding domain monomers form a domain-swapped dimer |
723738 |
7.2.2.8 | structural model of a deletion mutant lacking the four N-terminal metal-binding domains |
751096 |
7.2.2.8 | structural modeling. The ion-entry path involves one transient Met148-Cys382 ion-binding site and one intramembranous site formed by trigonal coordination to Cys384, Asn689, and Met717. The protein anchors predominantly in the cytoplasmic leaflet with exposed positive charges on the putative MB docking platform |
750064 |
7.2.2.8 | structure determination of the 73-147 domain in the 1-151 construct, in the apo state through 1H, 15N and 13C NMR spectroscopies, the structure of the Cu(I)-loaded 73-147 domain has been also determined in the construct 73-151 |
725695 |
7.2.2.8 | wild-type and selenomethionine CopA-ATP binding domain, hanging drop vapor diffusion method, using 100 mM sodium acetate, pH 4.6, 58% polyethylene glycol 4000, and 1020% glycerol |
669437 |
7.2.2.8 | with bound adenosine 5'-[beta, gamma-methylene]triphosphate or ADP and Mg2+, vapor diffusion method, using 5% (w/v) PEG 6000, 1.25-1.5M NaCl and 100 mM MES, pH 5.5-5.75, at 10°C |
711847 |