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Copper in PDB 5paz: Reduced Mutant P80A Pseudoazurin From A. Faecalis

Protein crystallography data

The structure of Reduced Mutant P80A Pseudoazurin From A. Faecalis, PDB code: 5paz 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) 10.30 / 1.76
Space group P 65
Cell size a, b, c (Å), α, β, γ (°) 50.060, 50.060, 98.720, 90.00, 90.00, 120.00
R / Rfree (%) 16.8 / n/a

Copper Binding Sites:

The binding sites of Copper atom in the Reduced Mutant P80A Pseudoazurin From A. Faecalis (pdb code 5paz). 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 P80A Pseudoazurin From A. Faecalis, PDB code: 5paz:

Copper binding site 1 out of 1 in 5paz

Go back to Copper Binding Sites List in 5paz
Copper binding site 1 out of 1 in the Reduced Mutant P80A 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 P80A Pseudoazurin From A. Faecalis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu124

b:18.0
occ:1.00
ND1 A:HIS81 2.0 18.4 1.0
ND1 A:HIS40 2.1 18.4 1.0
SG A:CYS78 2.2 17.6 1.0
CE1 A:HIS81 2.9 22.0 1.0
CE1 A:HIS40 2.9 17.5 1.0
SD A:MET86 3.0 15.8 1.0
CG A:HIS81 3.1 15.4 1.0
CG A:HIS40 3.1 17.7 1.0
CB A:CYS78 3.2 11.7 1.0
CA A:HIS40 3.5 17.7 1.0
CB A:HIS81 3.5 13.9 1.0
CB A:HIS40 3.5 14.3 1.0
O A:GLY39 3.6 22.0 1.0
CE A:MET86 3.8 12.2 1.0
N A:HIS81 4.0 16.1 1.0
NE2 A:HIS81 4.1 19.2 1.0
NE2 A:HIS40 4.1 19.1 1.0
CD2 A:HIS81 4.2 19.4 1.0
CD2 A:HIS40 4.2 19.9 1.0
N A:HIS40 4.2 18.0 1.0
C A:GLY39 4.3 20.1 1.0
CB A:ALA80 4.4 18.7 1.0
CA A:HIS81 4.4 14.6 1.0
CG A:MET86 4.5 12.8 1.0
CA A:CYS78 4.6 10.8 1.0
N A:ASN41 4.6 17.1 1.0
C A:HIS40 4.6 18.9 1.0
C A:ALA80 4.9 16.2 1.0
CB A:MET86 4.9 15.2 1.0

Reference:

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
Page generated: Sun Dec 13 11:19:37 2020

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