Copper in PDB 5jrr: Crystal Structure of Native Laccase From Thermus Thermophilus HB27

All present enzymatic activity of Crystal Structure of Native Laccase From Thermus Thermophilus HB27:
1.10.3.2;

The structure of Crystal Structure of Native Laccase From Thermus Thermophilus HB27, PDB code: 5jrr was solved by A.Diaz-Vilchis, R.R.Ruiz-Arellano, E.Rosas-Benitez, E.Rudino-Pinera, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.68 / 1.90
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	93.400, 109.790, 96.420, 90.00, 90.00, 90.00
R / Rfree (%)	18.5 / 23

The binding sites of Copper atom in the Crystal Structure of Native Laccase From Thermus Thermophilus HB27 (pdb code 5jrr). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 4 binding sites of Copper where determined in the Crystal Structure of Native Laccase From Thermus Thermophilus HB27, PDB code: 5jrr:
Jump to Copper binding site number: 1; 2; 3; 4;

Copper binding site 1 out of 4 in the Crystal Structure of Native Laccase From Thermus Thermophilus HB27


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 Native Laccase From Thermus Thermophilus HB27 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu501 b:19.4 occ:0.47 NE2 A:HIS398 1.8 13.1 1.0 NE2 A:HIS444 1.9 19.8 1.0 NE2 A:HIS137 2.1 19.6 0.6 NE2 A:HIS137 2.1 19.9 0.4 O2 A:OXY519 2.3 19.3 0.5 CD2 A:HIS137 2.5 22.4 0.6 CD2 A:HIS137 2.5 22.3 0.4 O1 A:OXY519 2.6 29.7 0.5 CE1 A:HIS398 2.7 12.6 1.0 CE1 A:HIS444 2.8 16.2 1.0 CD2 A:HIS444 2.9 10.4 1.0 CD2 A:HIS398 3.0 13.2 1.0 CE1 A:HIS137 3.4 31.9 0.4 CE1 A:HIS137 3.4 32.9 0.6 CU A:CU504 3.5 5.2 0.1 CD2 A:HIS95 3.6 16.9 1.0 CD2 A:HIS396 3.8 8.9 1.0 O A:HOH638 3.8 37.8 1.0 CG A:HIS137 3.8 19.3 0.6 CG A:HIS137 3.8 19.3 0.4 NE2 A:HIS95 3.8 19.5 1.0 ND1 A:HIS398 3.9 14.6 1.0 ND1 A:HIS444 3.9 22.2 1.0 CG A:HIS444 4.0 12.3 1.0 CG A:HIS398 4.0 19.8 1.0 ND1 A:HIS137 4.2 24.6 0.6 ND1 A:HIS137 4.2 24.2 0.4 NE2 A:HIS396 4.3 14.9 1.0 CG A:HIS95 4.4 16.5 1.0 CG2 A:VAL442 4.5 9.4 1.0 OE1 A:GLU451 4.5 21.9 0.5 OE2 A:GLU451 4.6 12.7 0.5 CE1 A:HIS95 4.6 11.8 1.0 CD A:GLU451 4.8 12.7 0.5 ND1 A:HIS95 4.9 10.5 1.0 CU A:CU502 5.0 18.6 1.0 CG A:HIS396 5.0 13.7 1.0

Copper binding site 2 out of 4 in the Crystal Structure of Native Laccase From Thermus Thermophilus HB27


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 Native Laccase From Thermus Thermophilus HB27 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu502 b:18.6 occ:1.00 ND1 A:HIS97 2.0 16.4 1.0 NE2 A:HIS446 2.1 19.4 1.0 NE2 A:HIS135 2.1 14.9 1.0 O1 A:OXY519 2.4 29.7 0.5 CE1 A:HIS97 2.9 15.8 1.0 CE1 A:HIS446 2.9 14.3 1.0 CD2 A:HIS135 3.0 8.6 1.0 O2 A:OXY519 3.0 19.3 0.5 CG A:HIS97 3.1 25.3 1.0 CE1 A:HIS135 3.1 15.4 1.0 CD2 A:HIS446 3.1 13.7 1.0 CB A:HIS97 3.5 20.4 1.0 CZ2 A:TRP133 3.6 15.8 1.0 CU A:CU504 3.8 5.2 0.1 CD2 A:HIS95 3.8 16.9 1.0 CE2 A:TRP133 4.0 10.7 1.0 NE2 A:HIS97 4.0 13.9 1.0 ND1 A:HIS446 4.1 14.1 1.0 CG A:HIS135 4.1 17.0 1.0 CD2 A:HIS97 4.1 11.8 1.0 ND1 A:HIS135 4.1 11.5 1.0 NE1 A:TRP133 4.2 15.7 1.0 CG A:HIS446 4.2 13.9 1.0 CH2 A:TRP133 4.2 10.4 1.0 NE2 A:HIS95 4.5 19.5 1.0 NE2 A:HIS396 4.6 14.9 1.0 CD2 A:HIS396 4.6 8.9 1.0 CA A:HIS97 4.7 14.2 1.0 O A:HOH638 4.8 37.8 1.0 CD2 A:TRP133 4.9 7.9 1.0 CG A:HIS95 4.9 16.5 1.0 CU A:CU501 5.0 19.4 0.5

Copper binding site 3 out of 4 in the Crystal Structure of Native Laccase From Thermus Thermophilus HB27


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 Native Laccase From Thermus Thermophilus HB27 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu503 b:23.0 occ:1.00 ND1 A:HIS450 2.1 12.3 1.0 ND1 A:HIS393 2.2 19.2 1.0 SG A:CYS445 2.2 19.1 1.0 CE1 A:HIS393 3.0 18.6 1.0 CE1 A:HIS450 3.1 17.1 1.0 CG A:HIS450 3.1 10.4 1.0 CB A:CYS445 3.3 20.3 1.0 CG A:HIS393 3.3 13.1 1.0 CB A:HIS450 3.4 9.9 1.0 SD A:MET455 3.6 24.2 0.8 SD A:MET455 3.6 23.7 0.1 CB A:HIS393 3.8 19.4 1.0 CB A:ILE447 4.0 10.7 1.0 CD1 A:ILE447 4.0 11.7 1.0 CA A:HIS393 4.0 15.8 1.0 NE2 A:HIS393 4.2 16.9 1.0 NE2 A:HIS450 4.2 11.4 1.0 CD2 A:HIS450 4.3 9.3 1.0 O A:ASP392 4.3 13.6 1.0 CD2 A:HIS393 4.4 11.1 1.0 CG1 A:ILE447 4.4 9.0 1.0 CD A:PRO394 4.6 9.5 1.0 CD A:PRO394 4.6 9.8 0.0 CA A:CYS445 4.7 9.3 1.0 CE A:MET455 4.7 15.3 0.8 O A:ILE447 4.7 18.8 1.0 CG2 A:ILE447 4.8 9.0 1.0 N A:ILE447 4.8 14.2 1.0 CE A:MET455 4.8 15.7 0.1 CA A:ILE447 4.9 16.2 1.0 CA A:HIS450 4.9 16.7 1.0 C A:HIS393 5.0 9.8 1.0

Copper binding site 4 out of 4 in the Crystal Structure of Native Laccase From Thermus Thermophilus HB27


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 Native Laccase From Thermus Thermophilus HB27 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu504 b:5.2 occ:0.09 NE2 A:HIS95 1.7 19.5 1.0 NE2 A:HIS396 1.7 14.9 1.0 CD2 A:HIS95 2.4 16.9 1.0 CD2 A:HIS396 2.5 8.9 1.0 O1 A:OXY519 2.6 29.7 0.5 CE1 A:HIS396 2.9 16.3 1.0 CE1 A:HIS95 2.9 11.8 1.0 CD2 A:HIS398 3.1 13.2 1.0 ND1 A:HIS97 3.2 16.4 1.0 NE2 A:HIS398 3.2 13.1 1.0 CG A:HIS97 3.5 25.3 1.0 CU A:CU501 3.5 19.4 0.5 O2 A:OXY519 3.6 19.3 0.5 CG A:HIS95 3.7 16.5 1.0 O A:HOH680 3.7 22.7 1.0 CG A:HIS396 3.7 13.7 1.0 CE1 A:HIS97 3.7 15.8 1.0 CU A:CU502 3.8 18.6 1.0 ND1 A:HIS396 3.8 17.3 1.0 ND1 A:HIS95 3.9 10.5 1.0 CG A:HIS398 3.9 19.8 1.0 CA A:HIS97 3.9 14.2 1.0 CB A:HIS97 3.9 20.4 1.0 CE1 A:HIS398 4.0 12.6 1.0 CD2 A:HIS97 4.1 11.8 1.0 NE2 A:HIS97 4.2 13.9 1.0 ND1 A:HIS398 4.3 14.6 1.0 N A:GLY98 4.5 13.5 1.0 NE2 A:HIS444 4.6 19.8 1.0 CA A:HIS398 4.7 10.8 1.0 C A:HIS97 4.7 19.9 1.0 CB A:HIS398 4.8 17.5 1.0 NE2 A:HIS446 4.8 19.4 1.0 CD2 A:HIS446 4.9 13.7 1.0 NE2 A:HIS135 4.9 14.9 1.0 N A:HIS97 4.9 9.5 1.0

A.Diaz-Vilchis, R.R.Ruiz-Arellano, E.Rosas-Benitez, V.Stojanoff, E.Rudino-Pinera. Preserving Metallic Sites Affected By Radiation Damage: the CUT2 Case in Thermus Thermophilus Multicopper Oxidase To Be Published.