Copper in PDB 1yjt: Solution Structure of the Cu(I) Form of the Sixth Soluble Domain A69P Mutant of Menkes Protein

All present enzymatic activity of Solution Structure of the Cu(I) Form of the Sixth Soluble Domain A69P Mutant of Menkes Protein:
3.6.3.4;

The binding sites of Copper atom in the Solution Structure of the Cu(I) Form of the Sixth Soluble Domain A69P Mutant of Menkes Protein (pdb code 1yjt). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total only one binding site of Copper was determined in the Solution Structure of the Cu(I) Form of the Sixth Soluble Domain A69P Mutant of Menkes Protein, PDB code: 1yjt:

Copper binding site 1 out of 1 in the Solution Structure of the Cu(I) Form of the Sixth Soluble Domain A69P Mutant of Menkes Protein


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Solution Structure of the Cu(I) Form of the Sixth Soluble Domain A69P Mutant of Menkes Protein within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu76 b:0.6 occ:1.00 SG A:CYS15 2.2 1.3 1.0 SG A:CYS18 2.2 0.7 1.0 H A:CYS18 2.5 0.6 1.0 HB3 A:SER17 2.9 1.6 1.0 H A:CYS15 3.1 1.1 1.0 N A:CYS18 3.2 0.6 1.0 CB A:CYS15 3.2 1.0 1.0 CB A:CYS18 3.3 0.6 1.0 N A:CYS15 3.4 0.9 1.0 HB2 A:CYS18 3.4 0.6 1.0 HB3 A:CYS15 3.4 1.2 1.0 H A:THR14 3.6 0.9 1.0 O A:CYS15 3.6 0.7 1.0 CA A:CYS15 3.7 0.9 1.0 CA A:CYS18 3.8 0.5 1.0 C A:CYS15 3.9 0.8 1.0 H A:SER17 3.9 0.9 1.0 CB A:SER17 3.9 0.9 1.0 C A:SER17 4.1 0.8 1.0 HA A:CYS18 4.2 0.6 1.0 HB2 A:CYS15 4.2 1.4 1.0 HB3 A:CYS18 4.2 0.6 1.0 CA A:SER17 4.3 0.9 1.0 N A:SER17 4.3 0.8 1.0 C A:THR14 4.3 1.1 1.0 HB2 A:SER17 4.4 2.0 1.0 N A:THR14 4.5 1.1 1.0 HA A:CYS15 4.7 1.0 1.0 H A:VAL19 4.8 0.6 1.0 OG A:SER17 4.8 1.9 1.0 HA A:MET13 4.9 0.9 1.0 N A:ALA16 4.9 0.9 1.0 HG21 A:THR14 4.9 2.6 1.0

L.Banci, I.Bertini, F.Cantini, M.Migliardi, A.Rosato, S.Wang. An Atomic-Level Investigation of the Disease-Causing A629P Mutant of the Menkes Protein, ATP7A J.Mol.Biol. V. 352 409 2005.
ISSN: ISSN 0022-2836
PubMed: 16083905
DOI: 10.1016/J.JMB.2005.07.034