Copper in PDB 7ciy: Crystal Structure of N191G-Mutated Tyrosinase From Streptomyces Castaneoglobisporus in Complex with the Caddie Protein Obtained By Soaking in the Solution Containing Cu(II) and Hydroxylamine For 24 H

The structure of Crystal Structure of N191G-Mutated Tyrosinase From Streptomyces Castaneoglobisporus in Complex with the Caddie Protein Obtained By Soaking in the Solution Containing Cu(II) and Hydroxylamine For 24 H, PDB code: 7ciy was solved by K.Oda, Y.Matoba, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 1.47
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	64.85, 97.4, 54.98, 90, 90, 90
R / Rfree (%)	n/a / n/a

The binding sites of Copper atom in the Crystal Structure of N191G-Mutated Tyrosinase From Streptomyces Castaneoglobisporus in Complex with the Caddie Protein Obtained By Soaking in the Solution Containing Cu(II) and Hydroxylamine For 24 H (pdb code 7ciy). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 7 binding sites of Copper where determined in the Crystal Structure of N191G-Mutated Tyrosinase From Streptomyces Castaneoglobisporus in Complex with the Caddie Protein Obtained By Soaking in the Solution Containing Cu(II) and Hydroxylamine For 24 H, PDB code: 7ciy:
Jump to Copper binding site number: 1; 2; 3; 4; 5; 6; 7;

Copper binding site 1 out of 7 in the Crystal Structure of N191G-Mutated Tyrosinase From Streptomyces Castaneoglobisporus in Complex with the Caddie Protein Obtained By Soaking in the Solution Containing Cu(II) and Hydroxylamine For 24 H


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Crystal Structure of N191G-Mutated Tyrosinase From Streptomyces Castaneoglobisporus in Complex with the Caddie Protein Obtained By Soaking in the Solution Containing Cu(II) and Hydroxylamine For 24 H within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu302 b:16.0 occ:0.54 CU A:CU302 0.0 16.0 0.5 CU A:CU302 1.1 16.4 0.5 NE2 A:HIS38 1.8 15.6 1.0 NE2 A:HIS63 1.9 14.1 1.0 NE2 A:HIS54 2.1 17.6 1.0 CD2 A:HIS38 2.6 15.8 1.0 O2 A:PEO301 2.8 15.7 0.5 CE1 A:HIS63 2.8 12.7 1.0 CE1 A:HIS54 2.9 16.8 1.0 O A:HOH401 2.9 16.1 0.5 CD2 A:HIS63 3.0 13.6 1.0 CE1 A:HIS38 3.0 15.4 1.0 CD2 A:HIS54 3.3 17.7 1.0 O1 A:PEO301 3.3 16.5 0.5 CG A:HIS38 3.8 15.3 1.0 ND1 A:HIS63 3.9 11.3 1.0 ND1 A:HIS38 4.0 15.4 1.0 CZ3 A:TRP62 4.0 13.0 1.0 CG A:HIS63 4.0 11.4 1.0 ND1 A:HIS54 4.1 16.8 1.0 CZ A:PHE212 4.2 11.7 1.0 CG A:HIS54 4.3 17.1 1.0 CU A:CU303 4.3 13.3 0.5 NE2 A:HIS216 4.5 13.5 1.0 CE2 A:PHE212 4.6 10.7 1.0 CE3 A:TRP62 4.6 13.2 1.0 CE1 A:HIS216 4.7 12.8 1.0 O A:GLY53 4.9 14.7 1.0 CD1 A:ILE42 4.9 22.5 1.0 CU A:CU303 4.9 14.4 0.5 CH2 A:TRP62 4.9 14.8 1.0 CG1 A:ILE42 4.9 20.8 1.0

Copper binding site 2 out of 7 in the Crystal Structure of N191G-Mutated Tyrosinase From Streptomyces Castaneoglobisporus in Complex with the Caddie Protein Obtained By Soaking in the Solution Containing Cu(II) and Hydroxylamine For 24 H


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Crystal Structure of N191G-Mutated Tyrosinase From Streptomyces Castaneoglobisporus in Complex with the Caddie Protein Obtained By Soaking in the Solution Containing Cu(II) and Hydroxylamine For 24 H within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu302 b:16.4 occ:0.46 CU A:CU302 0.0 16.4 0.5 CU A:CU302 1.1 16.0 0.5 O2 A:PEO301 1.7 15.7 0.5 O A:HOH401 2.0 16.1 0.5 NE2 A:HIS54 2.1 17.6 1.0 NE2 A:HIS38 2.1 15.6 1.0 O1 A:PEO301 2.2 16.5 0.5 NE2 A:HIS63 2.3 14.1 1.0 CD2 A:HIS54 2.9 17.7 1.0 CE1 A:HIS38 3.0 15.4 1.0 CE1 A:HIS63 3.1 12.7 1.0 CE1 A:HIS54 3.2 16.8 1.0 CD2 A:HIS38 3.3 15.8 1.0 CD2 A:HIS63 3.4 13.6 1.0 CU A:CU303 3.4 13.3 0.5 NE2 A:HIS216 4.0 13.5 1.0 CU A:CU303 4.0 14.4 0.5 OE2 B:G1X98 4.0 23.6 0.5 CG A:HIS54 4.1 17.1 1.0 ND1 A:HIS38 4.2 15.4 1.0 ND1 A:HIS54 4.2 16.8 1.0 CE1 A:HIS216 4.2 12.8 1.0 ND1 A:HIS63 4.3 11.3 1.0 CZ A:PHE212 4.3 11.7 1.0 OZ B:G1X98 4.3 25.9 1.0 CG A:HIS38 4.3 15.3 1.0 CE2 A:PHE212 4.4 10.7 1.0 CG A:HIS63 4.4 11.4 1.0 CD1 A:ILE42 4.5 22.5 1.0 CE1 A:PHE59 4.7 11.5 1.0 CG1 A:ILE42 4.8 20.8 1.0 NE2 A:HIS190 4.9 14.8 1.0 CD2 A:HIS216 4.9 12.3 1.0

Copper binding site 3 out of 7 in the Crystal Structure of N191G-Mutated Tyrosinase From Streptomyces Castaneoglobisporus in Complex with the Caddie Protein Obtained By Soaking in the Solution Containing Cu(II) and Hydroxylamine For 24 H


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Crystal Structure of N191G-Mutated Tyrosinase From Streptomyces Castaneoglobisporus in Complex with the Caddie Protein Obtained By Soaking in the Solution Containing Cu(II) and Hydroxylamine For 24 H within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu303 b:14.4 occ:0.54 CU A:CU303 0.0 14.4 0.5 CU A:CU303 1.0 13.3 0.5 NE2 A:HIS194 1.9 13.4 1.0 NE2 A:HIS216 1.9 13.5 1.0 NE2 A:HIS190 2.3 14.8 1.0 O A:HOH401 2.4 16.1 0.5 CE1 A:HIS194 2.8 12.2 1.0 O1 A:PEO301 2.8 16.5 0.5 CD2 A:HIS216 2.9 12.3 1.0 CE1 A:HIS216 2.9 12.8 1.0 CD2 A:HIS194 3.0 12.2 1.0 O2 A:PEO301 3.0 15.7 0.5 CD2 A:HIS190 3.1 13.9 1.0 CE1 A:HIS190 3.3 14.1 1.0 OE2 B:G1X98 3.8 23.6 0.5 ND1 A:HIS194 3.9 11.2 1.0 CD2 A:HIS215 3.9 11.9 1.0 CE2 A:PHE212 4.0 10.7 1.0 CG A:HIS216 4.0 10.6 1.0 ND1 A:HIS216 4.0 11.2 1.0 CU A:CU302 4.0 16.4 0.5 CG A:HIS194 4.0 11.6 1.0 NE2 A:HIS215 4.2 12.2 1.0 CG A:HIS190 4.3 12.9 1.0 OZ B:G1X98 4.3 25.9 1.0 ND1 A:HIS190 4.4 13.8 1.0 CE2 B:G1X98 4.4 21.2 1.0 CD2 A:PHE212 4.5 10.5 1.0 CZ B:G1X98 4.6 20.8 1.0 CZ A:PHE212 4.6 11.7 1.0 CU A:CU302 4.9 16.0 0.5 NE2 A:HIS63 5.0 14.1 1.0

Copper binding site 4 out of 7 in the Crystal Structure of N191G-Mutated Tyrosinase From Streptomyces Castaneoglobisporus in Complex with the Caddie Protein Obtained By Soaking in the Solution Containing Cu(II) and Hydroxylamine For 24 H


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 4 of Crystal Structure of N191G-Mutated Tyrosinase From Streptomyces Castaneoglobisporus in Complex with the Caddie Protein Obtained By Soaking in the Solution Containing Cu(II) and Hydroxylamine For 24 H within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu303 b:13.3 occ:0.46 CU A:CU303 0.0 13.3 0.5 CU A:CU303 1.0 14.4 0.5 O1 A:PEO301 1.9 16.5 0.5 NE2 A:HIS190 1.9 14.8 1.0 O A:HOH401 2.0 16.1 0.5 NE2 A:HIS216 2.3 13.5 1.0 O2 A:PEO301 2.3 15.7 0.5 NE2 A:HIS194 2.3 13.4 1.0 CE1 A:HIS190 2.8 14.1 1.0 CE1 A:HIS216 2.9 12.8 1.0 OE2 B:G1X98 3.0 23.6 0.5 CD2 A:HIS190 3.1 13.9 1.0 CE1 A:HIS194 3.3 12.2 1.0 CD2 A:HIS194 3.3 12.2 1.0 CU A:CU302 3.4 16.4 0.5 CD2 A:HIS216 3.5 12.3 1.0 CE2 B:G1X98 3.9 21.2 1.0 ND1 A:HIS190 3.9 13.8 1.0 OZ B:G1X98 4.0 25.9 1.0 CG A:HIS190 4.1 12.9 1.0 ND1 A:HIS216 4.2 11.2 1.0 CZ B:G1X98 4.3 20.8 1.0 CU A:CU302 4.3 16.0 0.5 ND1 A:HIS194 4.4 11.2 1.0 CE2 A:PHE212 4.4 10.7 1.0 CG A:HIS194 4.4 11.6 1.0 CG A:HIS216 4.4 10.6 1.0 NE2 A:HIS63 4.5 14.1 1.0 CE1 A:PHE59 4.5 11.5 1.0 CD2 A:HIS215 4.8 11.9 1.0 NE2 A:HIS215 4.8 12.2 1.0 CZ A:PHE59 4.8 12.0 1.0 CD2 B:G1X98 4.9 20.2 1.0 NE2 A:HIS38 4.9 15.6 1.0 CD2 A:HIS63 4.9 13.6 1.0 CZ A:PHE212 4.9 11.7 1.0 NE2 A:HIS54 5.0 17.6 1.0

Copper binding site 5 out of 7 in the Crystal Structure of N191G-Mutated Tyrosinase From Streptomyces Castaneoglobisporus in Complex with the Caddie Protein Obtained By Soaking in the Solution Containing Cu(II) and Hydroxylamine For 24 H


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 5 of Crystal Structure of N191G-Mutated Tyrosinase From Streptomyces Castaneoglobisporus in Complex with the Caddie Protein Obtained By Soaking in the Solution Containing Cu(II) and Hydroxylamine For 24 H within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu304 b:35.6 occ:0.50 NE2 A:HIS277 1.9 35.7 1.0 NE2 A:HIS279 2.3 68.8 1.0 O A:HOH555 2.4 27.9 0.5 CE1 A:HIS279 2.9 67.6 1.0 CD2 A:HIS277 2.9 36.6 1.0 CE1 A:HIS277 3.0 36.8 1.0 CD2 A:HIS279 3.6 70.2 1.0 CG A:HIS277 4.1 38.2 1.0 ND1 A:HIS277 4.1 38.1 1.0 ND1 A:HIS279 4.2 68.7 1.0 O A:HOH491 4.5 39.0 1.0 CG A:HIS279 4.5 70.7 1.0 CG A:PRO231 5.0 24.4 1.0

Copper binding site 6 out of 7 in the Crystal Structure of N191G-Mutated Tyrosinase From Streptomyces Castaneoglobisporus in Complex with the Caddie Protein Obtained By Soaking in the Solution Containing Cu(II) and Hydroxylamine For 24 H


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 6 of Crystal Structure of N191G-Mutated Tyrosinase From Streptomyces Castaneoglobisporus in Complex with the Caddie Protein Obtained By Soaking in the Solution Containing Cu(II) and Hydroxylamine For 24 H within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu201 b:31.4 occ:0.81 O B:HIS68 1.9 37.5 1.0 OE1 B:GLU67 1.9 34.8 1.0 NE2 B:HIS82 2.0 21.0 0.8 ND1 B:HIS68 2.0 36.9 1.0 N B:HIS68 2.6 35.8 1.0 CE1 B:HIS82 2.6 19.8 0.2 C B:HIS68 2.8 38.8 1.0 CE1 B:HIS68 2.9 37.6 1.0 CE1 B:HIS82 3.0 19.9 0.8 CD2 B:HIS82 3.0 20.2 0.8 CA B:HIS68 3.1 37.9 1.0 CG B:HIS68 3.1 37.2 1.0 CD B:GLU67 3.2 38.0 1.0 ND1 B:HIS82 3.2 19.5 0.2 C B:GLU67 3.3 37.9 1.0 CB B:GLU67 3.3 39.5 1.0 CB B:HIS68 3.6 38.1 1.0 NE2 B:HIS82 3.7 19.3 0.2 CG B:GLU67 3.9 39.4 1.0 CA B:GLU67 3.9 39.0 1.0 N B:GLY70 4.0 49.5 1.0 NE2 B:HIS68 4.0 38.3 1.0 O A:MET43 4.0 22.8 1.0 N B:GLY69 4.0 42.9 1.0 ND1 B:HIS82 4.1 18.8 0.8 O B:GLU67 4.1 38.9 1.0 OE2 B:GLU67 4.1 40.6 1.0 CG B:HIS82 4.1 18.5 0.8 CD2 B:HIS68 4.1 38.0 1.0 CG B:HIS82 4.4 18.6 0.2 CA B:GLY69 4.5 46.8 1.0 CD2 B:HIS82 4.6 18.8 0.2 O B:HOH372 4.7 70.3 1.0 C B:GLY69 4.7 50.1 1.0 CA B:GLY70 4.8 47.4 1.0 O B:HOH366 4.9 26.1 1.0

Copper binding site 7 out of 7 in the Crystal Structure of N191G-Mutated Tyrosinase From Streptomyces Castaneoglobisporus in Complex with the Caddie Protein Obtained By Soaking in the Solution Containing Cu(II) and Hydroxylamine For 24 H


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 7 of Crystal Structure of N191G-Mutated Tyrosinase From Streptomyces Castaneoglobisporus in Complex with the Caddie Protein Obtained By Soaking in the Solution Containing Cu(II) and Hydroxylamine For 24 H within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu201 b:24.3 occ:0.19 O1 B:NO3202 2.0 27.8 0.8 CE B:MET84 2.0 24.7 0.8 SD B:MET84 2.3 22.7 0.2 N B:NO3202 2.3 23.6 0.8 NE2 B:HIS97 2.4 22.3 0.2 CG B:MET84 2.5 21.7 0.2 O3 B:NO3202 2.8 24.5 0.8 CE1 B:HIS97 2.9 22.1 0.2 O2 B:NO3202 2.9 20.5 0.8 SD B:MET84 3.0 25.8 0.8 NE2 B:HIS82 3.1 19.3 0.2 CB B:MET84 3.3 20.8 0.8 O A:ILE42 3.3 20.6 1.0 CB B:MET84 3.3 20.9 0.2 CD2 B:HIS82 3.4 18.8 0.2 CE1 B:HIS97 3.5 21.7 0.8 CE B:MET84 3.5 24.7 0.2 CD2 B:HIS97 3.7 21.9 0.2 CG B:MET84 3.8 23.1 0.8 CA A:MET43 3.8 21.3 1.0 ND1 B:HIS97 3.8 21.6 0.8 ND1 B:HIS82 3.9 18.8 0.8 CE1 B:HIS82 3.9 19.9 0.8 O A:MET43 4.1 22.8 1.0 ND1 B:HIS97 4.1 21.4 0.2 C A:ILE42 4.2 19.0 1.0 C A:MET43 4.3 21.1 1.0 CE1 B:HIS82 4.4 19.8 0.2 N A:MET43 4.5 20.1 1.0 CG B:HIS97 4.6 21.2 0.2 CA B:MET84 4.6 17.2 1.0 CG2 A:ILE42 4.6 20.7 1.0 CD1 B:ILE92 4.7 24.4 1.0 N B:MET84 4.7 15.8 1.0 O A:HOH519 4.7 27.6 1.0 CG B:HIS82 4.7 18.6 0.2 CG1 B:ILE92 4.8 18.3 1.0 CB A:MET43 4.8 23.2 1.0 NE2 B:HIS97 4.8 22.0 0.8 CG A:MET43 4.9 25.1 1.0 C B:VAL83 4.9 14.5 1.0

Y.Matoba, K.Oda, Y.Muraki, T.Masuda. The Basicity of An Active-Site Water Molecule Discriminates Between Tyrosinase and Catechol Oxidase Activity. Int.J.Biol.Macromol. 2021.
ISSN: ISSN 0141-8130
PubMed: 34089758
DOI: 10.1016/J.IJBIOMAC.2021.05.206