Copper in PDB 1oq6: Solution Structure of Copper-S46V Copa From Bacillus Subtilis

All present enzymatic activity of Solution Structure of Copper-S46V Copa From Bacillus Subtilis:
3.6.3.4;

The binding sites of Copper atom in the Solution Structure of Copper-S46V Copa From Bacillus Subtilis (pdb code 1oq6). 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 Copper-S46V Copa From Bacillus Subtilis, PDB code: 1oq6:

Copper binding site 1 out of 1 in the Solution Structure of Copper-S46V Copa From Bacillus Subtilis


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 Copper-S46V Copa From Bacillus Subtilis within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu77 b:2.1 occ:1.00 H A:CYS20 2.0 0.5 1.0 SG A:CYS17 2.2 1.7 1.0 SG A:CYS20 2.2 1.2 1.0 HB1 A:ALA19 2.4 1.7 1.0 N A:CYS20 2.8 0.4 1.0 H A:CYS17 3.2 1.0 1.0 CB A:CYS20 3.3 0.5 1.0 O A:CYS17 3.3 2.3 1.0 HB2 A:CYS20 3.3 0.8 1.0 H A:ALA19 3.3 1.4 1.0 HG1 A:THR16 3.4 3.4 1.0 CB A:ALA19 3.4 0.6 1.0 CB A:CYS17 3.4 1.6 1.0 CA A:CYS20 3.6 0.4 1.0 HB2 A:CYS17 3.6 2.1 1.0 C A:CYS17 3.7 1.4 1.0 C A:ALA19 3.7 0.4 1.0 CA A:CYS17 3.8 1.3 1.0 OG1 A:THR16 3.8 2.6 1.0 N A:CYS17 3.8 0.9 1.0 N A:ALA19 3.8 0.7 1.0 CA A:ALA19 3.8 0.5 1.0 HB2 A:ALA19 3.9 1.4 1.0 HB A:THR16 4.0 2.5 1.0 HB3 A:ALA19 4.1 1.6 1.0 HA A:CYS20 4.1 0.4 1.0 H A:ALA21 4.2 0.4 1.0 HB3 A:CYS20 4.2 0.8 1.0 HB3 A:CYS17 4.3 2.2 1.0 HH12 A:ARG23 4.4 5.6 1.0 CB A:THR16 4.5 2.5 1.0 N A:ALA18 4.6 1.1 1.0 NH1 A:ARG23 4.7 4.4 1.0 HH11 A:ARG23 4.8 4.2 1.0 C A:THR16 4.8 1.2 1.0 O A:ALA19 4.8 0.5 1.0 HA A:CYS17 4.9 2.0 1.0 C A:CYS20 4.9 0.3 1.0 C A:ALA18 4.9 1.0 1.0 HA A:ALA19 4.9 0.7 1.0 N A:ALA21 5.0 0.3 1.0

L.Banci, I.Bertini, S.Ciofi-Baffoni, L.Gonnelli, X.C.Su. A Core Mutation Affecting the Folding Properties of A Soluble Domain of the Atpase Protein Copa From Bacillus Subtilis J.Mol.Biol. V. 331 473 2003.
ISSN: ISSN 0022-2836
PubMed: 12888353
DOI: 10.1016/S0022-2836(03)00769-1