Copper in PDB 4unm: Structure of Galactose Oxidase Homologue From Streptomyces Lividans

The structure of Structure of Galactose Oxidase Homologue From Streptomyces Lividans, PDB code: 4unm 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)	53.5 / 1.77
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	50.360, 126.630, 107.550, 90.00, 91.10, 90.00
R / Rfree (%)	18.767 / 22.819

The binding sites of Copper atom in the Structure of Galactose Oxidase Homologue From Streptomyces Lividans (pdb code 4unm). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Structure of Galactose Oxidase Homologue From Streptomyces Lividans, PDB code: 4unm:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in the Structure of Galactose Oxidase Homologue From Streptomyces Lividans


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Structure of Galactose Oxidase Homologue From Streptomyces Lividans within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu700 b:22.5 occ:1.00 OH A:TYR289 1.8 16.5 1.0 NE2 A:HIS502 2.1 19.3 1.0 NE2 A:HIS589 2.2 15.3 1.0 OH A:TYR501 2.2 23.3 1.0 O A:HOH2057 2.4 25.2 1.0 CZ A:TYR289 2.9 16.9 1.0 CE1 A:HIS502 3.1 20.5 1.0 CE1 A:HIS589 3.1 14.4 1.0 CD2 A:HIS502 3.1 18.6 1.0 CZ A:TYR501 3.1 21.1 1.0 SG A:CYS121 3.2 18.8 1.0 CD2 A:HIS589 3.2 14.8 1.0 CE1 A:TYR289 3.5 17.7 1.0 CE1 A:TYR501 3.8 20.8 1.0 CE2 A:TYR501 3.9 21.1 1.0 CE2 A:TYR289 4.0 16.4 1.0 ND1 A:HIS502 4.2 20.0 1.0 ND1 A:HIS589 4.2 13.9 1.0 CG A:HIS502 4.2 19.1 1.0 CG A:HIS589 4.3 14.1 1.0 O A:HOH2178 4.4 34.4 1.0 CE2 A:PHE120 4.8 28.0 1.0 CD1 A:TYR289 4.8 16.3 1.0 CB A:CYS121 4.9 16.9 1.0 CD2 A:PHE120 4.9 24.9 1.0 CZ2 A:TRP288 5.0 21.1 1.0

Copper binding site 2 out of 2 in the Structure of Galactose Oxidase Homologue From Streptomyces Lividans


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Structure of Galactose Oxidase Homologue From Streptomyces Lividans within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu700 b:30.5 occ:1.00 OH B:TYR289 2.0 23.7 1.0 OH B:TYR501 2.1 31.8 1.0 NE2 B:HIS502 2.2 26.8 1.0 NE2 B:HIS589 2.2 20.8 1.0 O B:HOH2030 2.5 32.9 1.0 CZ B:TYR289 3.0 24.0 1.0 CZ B:TYR501 3.1 33.0 1.0 CE1 B:HIS502 3.1 28.0 1.0 CD2 B:HIS502 3.2 23.8 1.0 SG B:CYS121 3.2 27.1 1.0 CD2 B:HIS589 3.2 20.8 1.0 CE1 B:HIS589 3.2 19.5 1.0 CE1 B:TYR289 3.5 24.2 1.0 CE2 B:TYR501 3.8 31.2 1.0 CE1 B:TYR501 3.8 30.4 1.0 O B:HOH2089 4.1 43.5 1.0 CE2 B:TYR289 4.1 25.3 1.0 ND1 B:HIS502 4.2 26.4 1.0 CG B:HIS502 4.3 25.5 1.0 ND1 B:HIS589 4.3 21.0 1.0 CG B:HIS589 4.3 19.6 1.0 CD1 B:TYR289 4.8 24.1 1.0 CB B:CYS121 4.9 23.8 1.0 CZ2 B:TRP288 4.9 31.2 1.0 CE2 B:PHE120 4.9 29.4 1.0 CD1 B:TYR501 5.0 30.9 1.0

A.K.Chaplin, M.L.Petrus, G.Mangiameli, M.A.Hough, D.A.Svistunenko, P.Nicholls, D.Claessen, E.Vijgenboom, J.A.Worrall. Glxa Is A New Structural Member of the Radical Copper Oxidase Family and Is Required For Glycan Deposition at Hyphal Tips and Morphogenesis of Streptomyces Lividans. Biochem.J. V. 469 433 2015.
ISSN: ISSN 0264-6021
PubMed: 26205496
DOI: 10.1042/BJ20150190