Copper in PDB 5lxz: W288A Mutant of Glxa From Streptomyces Lividans: Cu-Bound Form

The structure of W288A Mutant of Glxa From Streptomyces Lividans: Cu-Bound Form, PDB code: 5lxz was solved by A.K.Chaplin, M.A.Hough, J.A.R.Worrall, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.48 / 1.49
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	70.510, 80.870, 140.290, 90.00, 90.00, 90.00
R / Rfree (%)	16.3 / 18.1

The binding sites of Copper atom in the W288A Mutant of Glxa From Streptomyces Lividans: Cu-Bound Form (pdb code 5lxz). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the W288A Mutant of Glxa From Streptomyces Lividans: Cu-Bound Form, PDB code: 5lxz:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in the W288A Mutant of Glxa From Streptomyces Lividans: Cu-Bound Form


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of W288A Mutant of Glxa From Streptomyces Lividans: Cu-Bound Form within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu701 b:8.8 occ:0.70 NE2 B:HIS502 2.0 9.8 1.0 OH B:TYR289 2.1 20.9 0.7 NE2 B:HIS589 2.1 7.3 1.0 O B:HOH805 2.2 17.0 0.7 OH B:TYR501 2.8 19.4 1.0 CZ B:TYR289 2.9 15.9 0.7 CD2 B:HIS502 3.0 9.0 1.0 CD2 B:HIS589 3.0 7.4 1.0 CE1 B:HIS502 3.0 10.1 1.0 CE1 B:HIS589 3.1 7.2 1.0 CE1 B:TYR289 3.4 14.8 0.7 CZ B:TYR501 3.5 12.8 1.0 CE1 B:TYR289 3.6 6.8 0.3 CE1 B:PHE120 3.8 18.6 1.0 CE1 B:TYR501 3.9 12.8 1.0 O B:HOH1043 3.9 24.2 0.6 CE2 B:TYR289 4.0 15.6 0.7 OH B:TYR289 4.0 7.3 0.3 ND1 B:HIS502 4.1 9.8 1.0 ND1 B:HIS589 4.1 7.2 1.0 CG B:HIS502 4.1 8.6 1.0 CG B:HIS589 4.1 6.6 1.0 CZ B:TYR289 4.2 6.9 0.3 CZ B:PHE120 4.2 19.0 1.0 CE2 B:TYR501 4.2 11.4 1.0 SG B:CYS121 4.3 13.9 0.3 CD1 B:TYR289 4.4 6.8 0.3 CD1 B:TYR289 4.6 12.4 0.7 O B:HOH1043 4.7 14.1 0.4 CD1 B:PHE120 4.8 17.0 1.0 O B:HOH1371 4.8 10.4 0.3 O B:HOH950 5.0 30.9 1.0

Copper binding site 2 out of 2 in the W288A Mutant of Glxa From Streptomyces Lividans: Cu-Bound Form


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of W288A Mutant of Glxa From Streptomyces Lividans: Cu-Bound Form within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu702 b:16.9 occ:0.40 OD1 B:ASP94 1.8 22.3 1.0 OE1 B:GLU142 1.8 37.9 1.0 O B:HOH815 2.0 22.5 0.4 NH2 B:ARG140 2.6 23.8 0.4 CG B:ASP94 2.7 19.4 1.0 CD B:GLU142 2.9 33.0 1.0 OD2 B:ASP94 2.9 23.2 1.0 OE2 B:GLU142 3.2 36.0 1.0 O B:TYR141 3.4 17.3 0.4 CG B:ARG140 3.7 19.4 0.4 O B:HOH893 3.8 16.8 0.6 CZ B:ARG140 3.8 23.2 0.4 CD B:ARG140 3.9 20.7 0.4 CB B:ASP94 4.1 16.1 1.0 OE1 B:GLN90 4.1 32.6 1.0 O B:GLN90 4.2 14.4 1.0 CG B:GLU142 4.2 28.6 1.0 NE B:ARG140 4.3 22.4 0.4 NH1 B:ARG140 4.4 19.2 0.6 CA B:ASP94 4.4 14.3 1.0 N B:ASP94 4.5 13.9 1.0 C B:TYR141 4.6 17.3 0.4 CB B:GLU142 4.6 25.6 1.0 N B:TYR141 4.8 15.3 0.4 CA B:GLU142 4.9 21.1 1.0 NH1 B:ARG140 4.9 24.2 0.4 O B:HOH855 4.9 36.3 1.0 O B:HOH861 5.0 31.9 1.0 OG B:SER93 5.0 13.7 1.0

A.K.Chaplin, D.A.Svistunenko, M.A.Hough, M.T.Wilson, E.Vijgenboom, J.A.R.Worrall. The Role of A Second-Coordination Sphere Tryptophan Residue in the Maturation of the Catalytic Metalloradical Site in the Auxillary Activity Family 5 (AA5) Glxa From Streptomyces Lividans To Be Published.