Copper in PDB 7cit: Crystal Structure of 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 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: 7cit 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 / 1.50
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	64.56, 96.08, 54.65, 90, 90, 90
R / Rfree (%)	n/a / n/a

The binding sites of Copper atom in the Crystal Structure of 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 7cit). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 9 binding sites of Copper where determined in the Crystal Structure of 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: 7cit:
Jump to Copper binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9;

Copper binding site 1 out of 9 in the Crystal Structure of 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 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:17.3 occ:0.32 CU A:CU302 0.0 17.3 0.3 CU A:CU302 1.1 17.9 0.5 NE2 A:HIS63 1.8 17.6 1.0 NE2 A:HIS38 1.9 17.1 0.8 NE2 A:HIS54 2.1 19.6 0.8 NE2 A:HIS54 2.5 19.4 0.2 O2 A:PEO301 2.5 18.7 0.3 CD2 A:HIS38 2.6 16.5 0.8 CE1 A:HIS63 2.6 17.1 1.0 CD2 A:HIS38 2.7 17.2 0.2 O A:HOH401 2.7 18.3 0.7 CE1 A:HIS54 2.7 19.3 0.2 CU A:CU302 2.7 18.5 0.2 NE2 A:HIS38 2.8 17.2 0.2 O1 A:PEO301 2.9 18.6 0.3 CE1 A:HIS54 2.9 19.3 0.8 CD2 A:HIS63 3.0 16.7 1.0 CE1 A:HIS38 3.1 17.2 0.8 CD2 A:HIS54 3.2 19.2 0.8 CD2 A:HIS54 3.6 19.1 0.2 ND1 A:HIS63 3.8 16.2 1.0 CG A:HIS38 3.8 17.1 0.8 ND1 A:HIS54 3.8 19.1 0.2 CG A:HIS63 4.0 15.8 1.0 CU A:CU303 4.0 17.2 0.7 ND1 A:HIS38 4.0 17.6 0.8 CG A:HIS38 4.0 17.0 0.2 CE1 A:HIS38 4.1 17.3 0.2 ND1 A:HIS54 4.1 19.0 0.8 CZ A:PHE212 4.2 14.8 1.0 CG A:HIS54 4.2 19.2 0.8 CZ3 A:TRP62 4.2 15.8 1.0 CG A:HIS54 4.3 19.0 0.2 NE2 A:HIS216 4.3 16.8 1.0 CE2 A:PHE212 4.4 14.8 1.0 CU A:CU303 4.4 16.9 0.3 OE2 B:G1X98 4.5 16.9 0.4 CE1 A:HIS216 4.5 15.7 1.0 ND1 A:HIS38 4.7 17.2 0.2 OZ B:G1X98 4.7 19.4 1.0 CE3 A:TRP62 4.8 15.9 1.0 O A:GLY53 4.9 18.6 1.0

Copper binding site 2 out of 9 in the Crystal Structure of 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 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:17.9 occ:0.47 CU A:CU302 0.0 17.9 0.5 CU A:CU302 1.1 17.3 0.3 O2 A:PEO301 1.4 18.7 0.3 CU A:CU302 1.9 18.5 0.2 O A:HOH401 1.9 18.3 0.7 O1 A:PEO301 2.1 18.6 0.3 NE2 A:HIS54 2.1 19.4 0.2 NE2 A:HIS38 2.1 17.1 0.8 NE2 A:HIS54 2.1 19.6 0.8 NE2 A:HIS63 2.4 17.6 1.0 NE2 A:HIS38 2.7 17.2 0.2 CE1 A:HIS54 2.8 19.3 0.2 CD2 A:HIS54 2.9 19.2 0.8 CE1 A:HIS38 2.9 17.2 0.8 CD2 A:HIS38 3.1 17.2 0.2 CU A:CU303 3.1 17.2 0.7 CE1 A:HIS63 3.1 17.1 1.0 CD2 A:HIS54 3.1 19.1 0.2 CD2 A:HIS38 3.2 16.5 0.8 CE1 A:HIS54 3.3 19.3 0.8 OE2 B:G1X98 3.4 16.9 0.4 CD2 A:HIS63 3.6 16.7 1.0 CU A:CU303 3.6 16.9 0.3 OZ B:G1X98 3.9 19.4 1.0 CE1 A:HIS38 3.9 17.3 0.2 NE2 A:HIS216 3.9 16.8 1.0 ND1 A:HIS54 4.0 19.1 0.2 ND1 A:HIS38 4.1 17.6 0.8 CG A:HIS54 4.1 19.2 0.8 CG A:HIS54 4.1 19.0 0.2 CE2 A:PHE212 4.3 14.8 1.0 CE1 A:HIS216 4.3 15.7 1.0 CG A:HIS38 4.3 17.1 0.8 ND1 A:HIS54 4.3 19.0 0.8 ND1 A:HIS63 4.3 16.2 1.0 CZ A:PHE212 4.3 14.8 1.0 CG A:HIS38 4.4 17.0 0.2 CE2 B:G1X98 4.5 18.2 1.0 CD1 A:ILE42 4.5 25.8 1.0 NE2 A:HIS190 4.6 15.8 1.0 CG A:HIS63 4.6 15.8 1.0 CZ B:G1X98 4.7 18.3 1.0 ND1 A:HIS38 4.8 17.2 0.2 NE2 A:HIS194 4.8 16.2 1.0 CE1 A:PHE59 4.8 13.8 1.0 CD2 A:HIS216 4.8 15.4 1.0 CG1 A:ILE42 4.9 22.9 1.0 CE1 A:HIS190 5.0 15.3 1.0

Copper binding site 3 out of 9 in the Crystal Structure of 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 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:18.5 occ:0.21 CU A:CU302 0.0 18.5 0.2 O2 A:PEO301 1.8 18.7 0.3 CU A:CU302 1.9 17.9 0.5 O A:HOH401 2.0 18.3 0.7 NE2 A:HIS38 2.1 17.2 0.2 OZ B:G1X98 2.2 19.4 1.0 CE1 A:HIS38 2.3 17.2 0.8 NE2 A:HIS54 2.3 19.4 0.2 OE2 B:G1X98 2.4 16.9 0.4 NE2 A:HIS38 2.4 17.1 0.8 CU A:CU302 2.7 17.3 0.3 NE2 A:HIS54 2.8 19.6 0.8 O1 A:PEO301 2.9 18.6 0.3 CE1 A:HIS38 2.9 17.3 0.2 CZ B:G1X98 3.0 18.3 1.0 CE2 B:G1X98 3.1 18.2 1.0 CE1 A:HIS54 3.2 19.3 0.2 CD1 A:ILE42 3.2 25.8 1.0 CD2 A:HIS54 3.3 19.1 0.2 CD2 A:HIS38 3.3 17.2 0.2 CD2 A:HIS54 3.4 19.2 0.8 CU A:CU303 3.4 17.2 0.7 ND1 A:HIS38 3.6 17.6 0.8 CD2 A:HIS38 3.8 16.5 0.8 CG1 A:ILE42 3.8 22.9 1.0 CE1 A:HIS54 3.8 19.3 0.8 CU A:CU303 3.9 16.9 0.3 OG A:SER206 4.1 14.8 1.0 ND1 A:HIS38 4.1 17.2 0.2 NE2 A:HIS63 4.3 17.6 1.0 ND1 A:HIS54 4.3 19.1 0.2 NE2 A:HIS194 4.3 16.2 1.0 CE1 B:G1X98 4.3 17.2 1.0 CG A:HIS38 4.3 17.0 0.2 CG A:HIS38 4.4 17.1 0.8 CG A:HIS54 4.4 19.0 0.2 CE1 A:HIS194 4.4 16.2 1.0 O B:HOH349 4.4 39.5 1.0 CG A:HIS54 4.5 19.2 0.8 CD2 B:G1X98 4.5 18.4 1.0 CE2 A:PHE212 4.5 14.8 1.0 ND1 A:HIS54 4.7 19.0 0.8 NE2 A:HIS190 4.9 15.8 1.0 CE1 A:HIS63 4.9 17.1 1.0 NE2 A:HIS216 4.9 16.8 1.0

Copper binding site 4 out of 9 in the Crystal Structure of 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 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:16.9 occ:0.32 CU A:CU303 0.0 16.9 0.3 CU A:CU303 0.8 17.2 0.7 NE2 A:HIS194 1.8 16.2 1.0 NE2 A:HIS216 1.9 16.8 1.0 NE2 A:HIS190 2.2 15.8 1.0 O A:HOH401 2.2 18.3 0.7 O2 A:PEO301 2.4 18.7 0.3 CE1 A:HIS194 2.7 16.2 1.0 CD2 A:HIS216 2.8 15.4 1.0 O1 A:PEO301 2.9 18.6 0.3 CE1 A:HIS216 2.9 15.7 1.0 CD2 A:HIS194 3.0 15.2 1.0 CD2 A:HIS190 3.0 15.1 1.0 CE1 A:HIS190 3.3 15.3 1.0 CU A:CU302 3.6 17.9 0.5 OE2 B:G1X98 3.6 16.9 0.4 CU A:CU302 3.9 18.5 0.2 CG A:HIS216 3.9 14.0 1.0 ND1 A:HIS194 3.9 15.8 1.0 ND1 A:HIS216 3.9 15.2 1.0 CE2 A:PHE212 4.0 14.8 1.0 CG A:HIS194 4.0 15.2 1.0 CD2 A:HIS215 4.1 15.5 1.0 CE2 B:G1X98 4.2 18.2 1.0 CG A:HIS190 4.2 14.2 1.0 NE2 A:HIS215 4.3 15.0 1.0 OZ B:G1X98 4.3 19.4 1.0 ND1 A:HIS190 4.4 14.8 1.0 CU A:CU302 4.4 17.3 0.3 CZ B:G1X98 4.5 18.3 1.0 CD2 A:PHE212 4.6 14.2 1.0 CZ A:PHE212 4.6 14.8 1.0 NE2 A:HIS63 4.6 17.6 1.0 CD2 A:HIS63 5.0 16.7 1.0 NE2 A:HIS38 5.0 17.1 0.8

Copper binding site 5 out of 9 in the Crystal Structure of 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 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:17.2 occ:0.68 CU A:CU303 0.0 17.2 0.7 CU A:CU303 0.8 16.9 0.3 O2 A:PEO301 1.8 18.7 0.3 NE2 A:HIS190 1.9 15.8 1.0 O A:HOH401 2.0 18.3 0.7 O1 A:PEO301 2.1 18.6 0.3 NE2 A:HIS194 2.2 16.2 1.0 NE2 A:HIS216 2.2 16.8 1.0 CE1 A:HIS190 2.8 15.3 1.0 OE2 B:G1X98 2.9 16.9 0.4 CE1 A:HIS216 3.0 15.7 1.0 CD2 A:HIS190 3.0 15.1 1.0 CU A:CU302 3.1 17.9 0.5 CE1 A:HIS194 3.1 16.2 1.0 CD2 A:HIS194 3.2 15.2 1.0 CU A:CU302 3.4 18.5 0.2 CD2 A:HIS216 3.4 15.4 1.0 CE2 B:G1X98 3.7 18.2 1.0 ND1 A:HIS190 4.0 14.8 1.0 CU A:CU302 4.0 17.3 0.3 OZ B:G1X98 4.0 19.4 1.0 CG A:HIS190 4.1 14.2 1.0 ND1 A:HIS216 4.2 15.2 1.0 CZ B:G1X98 4.2 18.3 1.0 ND1 A:HIS194 4.3 15.8 1.0 CG A:HIS194 4.3 15.2 1.0 NE2 A:HIS63 4.3 17.6 1.0 CE2 A:PHE212 4.4 14.8 1.0 CG A:HIS216 4.4 14.0 1.0 NE2 A:HIS54 4.4 19.4 0.2 CE1 A:PHE59 4.5 13.8 1.0 CD2 B:G1X98 4.6 18.4 1.0 NE2 A:HIS38 4.7 17.1 0.8 CD2 A:HIS215 4.8 15.5 1.0 CD2 A:HIS54 4.8 19.1 0.2 NE2 A:HIS215 4.8 15.0 1.0 CD2 A:HIS63 4.8 16.7 1.0 CD2 A:HIS54 4.9 19.2 0.8 NE2 A:HIS54 4.9 19.6 0.8 NE2 A:HIS38 4.9 17.2 0.2 CZ A:PHE59 4.9 15.7 1.0 CE1 A:HIS63 4.9 17.1 1.0 CZ A:PHE212 5.0 14.8 1.0

Copper binding site 6 out of 9 in the Crystal Structure of 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 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:80.8 occ:0.50 NE2 A:HIS277 2.0 79.5 1.0 O A:HOH581 2.8 36.1 0.5 CE1 A:HIS277 2.8 78.7 1.0 CD2 A:HIS277 3.1 79.0 1.0 ND1 A:HIS277 4.0 78.2 1.0 CG A:HIS277 4.1 78.1 1.0 O A:HOH627 4.8 57.3 1.0 CG A:PRO231 4.9 35.9 1.0

Copper binding site 7 out of 9 in the Crystal Structure of 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 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:Cu305 b:51.0 occ:0.38 NE2 A:HIS180 2.1 25.9 1.0 CE1 A:HIS180 3.0 25.9 1.0 CD2 A:HIS180 3.1 24.5 1.0 OE2 A:GLU175 3.9 49.3 1.0 CA A:GLY186 4.0 24.9 1.0 O A:HOH527 4.0 41.7 1.0 ND1 A:HIS180 4.2 24.8 1.0 OE1 A:GLU175 4.2 48.8 1.0 CG A:HIS180 4.2 22.9 1.0 N A:GLY186 4.3 23.4 1.0 CD A:GLU175 4.5 39.7 1.0 C A:ARG185 4.8 23.7 1.0 O A:HOH537 4.9 35.7 1.0 CB A:ARG185 5.0 26.7 1.0

Copper binding site 8 out of 9 in the Crystal Structure of 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 8 of Crystal Structure of 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:27.5 occ:0.38 O1 B:NO3202 1.6 26.1 0.6 SD B:MET84 2.1 25.0 0.4 NE2 B:HIS97 2.1 24.8 0.4 N B:NO3202 2.2 25.9 0.6 NE2 B:HIS82 2.3 26.5 0.4 CE B:MET84 2.3 24.5 0.6 CE B:MET84 2.4 24.1 0.4 O3 B:NO3202 2.7 26.8 0.6 O2 B:NO3202 2.8 25.0 0.6 CG B:MET84 2.9 24.7 0.4 CE1 B:HIS97 2.9 24.2 0.4 SD B:MET84 3.0 24.9 0.6 CD2 B:HIS82 3.0 25.9 0.4 O A:ILE42 3.2 25.7 1.0 CE1 B:HIS97 3.2 24.1 0.6 CD2 B:HIS97 3.3 24.2 0.4 CB B:MET84 3.3 23.9 0.6 CB B:MET84 3.3 23.6 0.4 CE1 B:HIS82 3.4 27.4 0.4 ND1 B:HIS97 3.6 23.8 0.6 CG B:MET84 3.8 24.0 0.6 ND1 B:HIS82 3.8 25.7 0.6 CA A:MET43 3.8 24.7 1.0 CE1 B:HIS82 4.0 27.5 0.6 C A:ILE42 4.1 22.0 1.0 ND1 B:HIS97 4.1 23.6 0.4 O A:MET43 4.2 27.3 1.0 CG B:HIS82 4.3 25.1 0.4 CG B:HIS97 4.3 23.2 0.4 C A:MET43 4.3 24.6 1.0 N A:MET43 4.4 23.3 1.0 ND1 B:HIS82 4.4 27.0 0.4 NE2 B:HIS97 4.5 24.2 0.6 O A:HOH439 4.5 29.2 1.0 CA B:MET84 4.6 21.2 1.0 CG2 A:ILE42 4.6 24.5 1.0 CG1 B:ILE92 4.6 24.0 1.0 N B:MET84 4.7 20.2 1.0 CD1 B:ILE92 4.7 31.4 1.0 C B:VAL83 4.9 19.6 1.0 CB A:MET43 4.9 26.4 1.0 CG B:HIS97 4.9 23.4 0.6 CG A:MET43 4.9 28.8 1.0

Copper binding site 9 out of 9 in the Crystal Structure of 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 9 of Crystal Structure of 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:36.0 occ:0.62 OE1 B:GLU67 1.5 40.6 1.0 O B:HIS68 1.9 42.7 1.0 NE2 B:HIS82 2.0 30.5 0.6 ND1 B:HIS68 2.0 40.8 1.0 N B:HIS68 2.5 42.2 1.0 CD B:GLU67 2.7 44.0 1.0 C B:HIS68 2.7 44.5 1.0 CE1 B:HIS82 2.8 27.5 0.6 CE1 B:HIS68 2.8 42.3 1.0 CA B:HIS68 3.0 43.6 1.0 CD2 B:HIS82 3.1 27.7 0.6 CG B:HIS68 3.1 42.5 1.0 C B:GLU67 3.2 46.1 1.0 CE1 B:HIS82 3.4 27.4 0.4 ND1 B:HIS82 3.4 27.0 0.4 CB B:GLU67 3.4 46.6 1.0 OE2 B:GLU67 3.5 50.5 1.0 CB B:HIS68 3.6 44.0 1.0 CG B:GLU67 3.7 46.7 1.0 CA B:GLU67 3.9 48.8 1.0 N B:GLY70 3.9 54.4 1.0 O B:GLU67 4.0 48.6 1.0 N B:GLY69 4.0 47.1 1.0 O A:MET43 4.0 27.3 1.0 ND1 B:HIS82 4.0 25.7 0.6 NE2 B:HIS68 4.0 42.9 1.0 CG B:HIS82 4.1 25.2 0.6 CD2 B:HIS68 4.2 42.8 1.0 CA B:GLY70 4.4 54.0 1.0 C B:GLY69 4.5 54.2 1.0 CA B:GLY69 4.6 50.4 1.0 NE2 B:HIS82 4.7 26.5 0.4 O B:HOH357 4.8 34.2 1.0 CG B:HIS82 4.8 25.1 0.4

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