Copper in PDB 7paz: Reduced Mutant P80I Pseudoazurin From A. Faecalis

The structure of Reduced Mutant P80I Pseudoazurin From A. Faecalis, PDB code: 7paz was solved by E.T.Adman, C.A.P.Libeu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	26.00 / 2.00
Space group	P 65
Cell size a, b, c (Å), α, β, γ (°)	50.790, 50.790, 98.250, 90.00, 90.00, 120.00
R / Rfree (%)	20.6 / n/a

The binding sites of Copper atom in the Reduced Mutant P80I Pseudoazurin From A. Faecalis (pdb code 7paz). 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 Reduced Mutant P80I Pseudoazurin From A. Faecalis, PDB code: 7paz:

Copper binding site 1 out of 1 in the Reduced Mutant P80I Pseudoazurin From A. Faecalis


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Reduced Mutant P80I Pseudoazurin From A. Faecalis within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu124 b:29.0 occ:1.00 ND1 A:HIS40 2.0 24.1 1.0 ND1 A:HIS81 2.1 29.9 1.0 SG A:CYS78 2.1 28.2 1.0 SD A:MET86 3.0 26.7 1.0 CE1 A:HIS40 3.0 20.6 1.0 CE1 A:HIS81 3.0 31.0 1.0 CG A:HIS40 3.1 27.1 1.0 CG A:HIS81 3.2 30.2 1.0 CB A:CYS78 3.2 21.9 1.0 CB A:HIS40 3.4 28.7 1.0 O A:GLY39 3.5 45.6 1.0 CA A:HIS40 3.5 33.2 1.0 CB A:HIS81 3.6 24.1 1.0 CE A:MET86 3.8 16.4 1.0 N A:HIS81 3.9 26.0 1.0 NE2 A:HIS40 4.1 24.5 1.0 CD2 A:HIS40 4.2 26.1 1.0 NE2 A:HIS81 4.2 30.0 1.0 CB A:ILE80 4.3 26.1 1.0 CD2 A:HIS81 4.3 30.3 1.0 C A:GLY39 4.3 36.5 1.0 N A:HIS40 4.4 36.3 1.0 CA A:HIS81 4.4 19.9 1.0 N A:ASN41 4.5 30.8 1.0 CG A:MET86 4.6 28.8 1.0 CG2 A:ILE80 4.6 21.8 1.0 C A:HIS40 4.6 33.5 1.0 CA A:CYS78 4.6 25.7 1.0 C A:ILE80 4.6 27.6 1.0 CA A:ILE80 4.8 25.8 1.0 CB A:MET86 4.9 25.7 1.0 N A:ILE80 5.0 24.7 1.0

C.A.Libeu, M.Kukimoto, M.Nishiyama, S.Horinouchi, E.T.Adman. Site-Directed Mutants of Pseudoazurin: Explanation of Increased Redox Potentials From X-Ray Structures and From Calculation of Redox Potential Differences. Biochemistry V. 36 13160 1997.
ISSN: ISSN 0006-2960
PubMed: 9341204
DOI: 10.1021/BI9704111