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Copper in PDB 3paz: Reduced Native Pseudoazurin From A. Faecalis

Protein crystallography data

The structure of Reduced Native Pseudoazurin From A. Faecalis, PDB code: 3paz 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) 22.30 / 1.73
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 (%) 16.4 / n/a

Copper Binding Sites:

The binding sites of Copper atom in the Reduced Native Pseudoazurin From A. Faecalis (pdb code 3paz). 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 Native Pseudoazurin From A. Faecalis, PDB code: 3paz:

Copper binding site 1 out of 1 in 3paz

Go back to Copper Binding Sites List in 3paz
Copper binding site 1 out of 1 in the Reduced Native 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 Native Pseudoazurin From A. Faecalis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu124

b:27.4
occ:1.00
ND1 A:HIS40 2.1 20.5 1.0
SG A:CYS78 2.2 21.1 1.0
ND1 A:HIS81 2.3 26.6 1.0
SD A:MET86 2.8 20.5 1.0
CE1 A:HIS40 3.1 19.4 1.0
CG A:HIS40 3.1 20.3 1.0
CB A:CYS78 3.2 15.4 1.0
CG A:HIS81 3.3 22.6 1.0
CE1 A:HIS81 3.3 26.4 1.0
CB A:HIS40 3.4 18.0 1.0
CE A:MET86 3.5 14.5 1.0
CB A:HIS81 3.5 16.9 1.0
CA A:HIS40 3.5 21.9 1.0
O A:GLY39 3.7 29.1 1.0
NE2 A:HIS40 4.2 21.1 1.0
CG A:MET86 4.2 14.0 1.0
CD2 A:HIS40 4.2 21.1 1.0
N A:HIS81 4.2 18.9 1.0
C A:GLY39 4.4 28.0 1.0
N A:HIS40 4.4 23.2 1.0
NE2 A:HIS81 4.4 20.3 1.0
CD2 A:HIS81 4.4 21.1 1.0
CA A:HIS81 4.5 15.7 1.0
CG A:PRO80 4.6 25.2 1.0
CA A:CYS78 4.6 15.0 1.0
N A:ASN41 4.6 19.6 1.0
C A:HIS40 4.6 22.0 1.0
CB A:MET86 4.7 14.5 1.0
CD A:PRO80 4.9 23.6 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: Fri Sep 4 08:13:42 2020
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