Copper in PDB 5k7a: Crystal Structure of Laccase Fron Thermus Thermophilus HB27 (Sodium Nitrate 1.5 Min)

All present enzymatic activity of Crystal Structure of Laccase Fron Thermus Thermophilus HB27 (Sodium Nitrate 1.5 Min):
1.10.3.2;

The structure of Crystal Structure of Laccase Fron Thermus Thermophilus HB27 (Sodium Nitrate 1.5 Min), PDB code: 5k7a 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)	19.72 / 1.50
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	93.744, 110.332, 96.484, 90.00, 90.00, 90.00
R / Rfree (%)	16.8 / 19.1

The binding sites of Copper atom in the Crystal Structure of Laccase Fron Thermus Thermophilus HB27 (Sodium Nitrate 1.5 Min) (pdb code 5k7a). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 3 binding sites of Copper where determined in the Crystal Structure of Laccase Fron Thermus Thermophilus HB27 (Sodium Nitrate 1.5 Min), PDB code: 5k7a:
Jump to Copper binding site number: 1; 2; 3;

Copper binding site 1 out of 3 in the Crystal Structure of Laccase Fron Thermus Thermophilus HB27 (Sodium Nitrate 1.5 Min)


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 Laccase Fron Thermus Thermophilus HB27 (Sodium Nitrate 1.5 Min) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu501 b:11.6 occ:0.29 NE2 A:HIS398 1.7 5.3 1.0 NE2 A:HIS444 1.9 9.7 1.0 CE1 A:HIS137 2.5 14.2 0.3 CE1 A:HIS398 2.6 5.8 1.0 CD2 A:HIS444 2.8 5.5 1.0 ND1 A:HIS137 2.8 16.7 0.3 CD2 A:HIS398 2.8 5.6 1.0 CE1 A:HIS444 2.9 11.2 1.0 CE1 A:HIS137 2.9 13.1 0.7 ND1 A:HIS137 3.0 16.4 0.7 CD2 A:HIS95 3.5 9.8 1.0 CD2 A:HIS396 3.6 7.7 1.0 NE2 A:HIS137 3.6 23.6 0.3 NE2 A:HIS95 3.7 10.9 1.0 ND1 A:HIS398 3.7 7.9 1.0 O A:HOH630 3.8 16.1 1.0 NE2 A:HIS137 3.9 23.1 0.7 CG A:HIS398 3.9 5.3 1.0 CG A:HIS137 4.0 12.4 0.3 ND1 A:HIS444 4.0 7.1 1.0 CG A:HIS444 4.0 6.5 1.0 NE2 A:HIS396 4.0 9.2 1.0 CG A:HIS137 4.0 11.7 0.7 CG A:HIS95 4.2 7.3 1.0 CD2 A:HIS137 4.3 17.7 0.3 CE1 A:HIS95 4.4 9.3 1.0 CD2 A:HIS137 4.4 17.9 0.7 CG2 A:VAL442 4.5 7.7 1.0 OE2 A:GLU451 4.7 5.9 0.4 ND1 A:HIS95 4.7 9.3 1.0 CG A:HIS396 4.8 6.3 1.0 CB A:HIS137 4.9 9.8 0.7 CD A:GLU451 4.9 6.2 0.4 OE1 A:GLU451 5.0 12.7 0.4 CB A:HIS95 5.0 11.6 1.0 CU A:CU502 5.0 7.0 0.9 CB A:HIS137 5.0 10.0 0.3

Copper binding site 2 out of 3 in the Crystal Structure of Laccase Fron Thermus Thermophilus HB27 (Sodium Nitrate 1.5 Min)


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 Laccase Fron Thermus Thermophilus HB27 (Sodium Nitrate 1.5 Min) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu502 b:7.0 occ:0.92 ND1 A:HIS97 2.0 6.0 1.0 NE2 A:HIS135 2.0 6.3 1.0 NE2 A:HIS446 2.1 4.7 1.0 CE1 A:HIS97 2.9 5.5 1.0 CE1 A:HIS446 3.0 4.1 1.0 CE1 A:HIS135 3.0 8.6 1.0 CD2 A:HIS135 3.0 3.7 1.0 CG A:HIS97 3.0 7.4 1.0 CD2 A:HIS446 3.2 8.1 1.0 CB A:HIS97 3.4 4.5 1.0 CZ2 A:TRP133 3.6 5.3 1.0 CD2 A:HIS95 3.7 9.8 1.0 CE2 A:TRP133 3.9 4.2 1.0 NE2 A:HIS97 4.0 7.1 1.0 NE1 A:TRP133 4.0 3.7 1.0 ND1 A:HIS135 4.1 7.0 1.0 CD2 A:HIS97 4.1 5.9 1.0 ND1 A:HIS446 4.1 4.2 1.0 CG A:HIS135 4.1 5.5 1.0 CG A:HIS446 4.2 5.8 1.0 NE2 A:HIS95 4.3 10.9 1.0 CH2 A:TRP133 4.3 3.4 1.0 NE2 A:HIS396 4.4 9.2 1.0 CD2 A:HIS396 4.5 7.7 1.0 CA A:HIS97 4.7 5.6 1.0 CG A:HIS95 4.8 7.3 1.0 CD2 A:TRP133 4.8 4.0 1.0 O A:HOH630 5.0 16.1 1.0 CU A:CU501 5.0 11.6 0.3 CD1 A:TRP133 5.0 3.9 1.0

Copper binding site 3 out of 3 in the Crystal Structure of Laccase Fron Thermus Thermophilus HB27 (Sodium Nitrate 1.5 Min)


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 Laccase Fron Thermus Thermophilus HB27 (Sodium Nitrate 1.5 Min) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu503 b:6.9 occ:0.74 ND1 A:HIS393 2.1 8.3 1.0 SG A:CYS445 2.1 7.5 1.0 ND1 A:HIS450 2.1 7.5 1.0 CE1 A:HIS393 2.9 12.0 1.0 CG A:HIS450 3.1 5.8 1.0 CE1 A:HIS450 3.1 9.9 1.0 CG A:HIS393 3.2 8.4 1.0 CB A:CYS445 3.3 5.7 1.0 CB A:HIS450 3.4 6.5 1.0 SD A:MET455 3.4 5.5 0.3 CB A:HIS393 3.7 7.4 1.0 SD A:MET455 3.7 12.6 0.7 CE A:MET455 3.9 16.7 0.3 CD1 A:ILE447 4.0 8.6 1.0 CB A:ILE447 4.0 4.6 1.0 CA A:HIS393 4.1 7.3 1.0 NE2 A:HIS393 4.1 9.5 1.0 NE2 A:HIS450 4.2 7.5 1.0 CD2 A:HIS450 4.2 8.1 1.0 CD2 A:HIS393 4.3 7.5 1.0 CG1 A:ILE447 4.4 4.8 1.0 O A:ASP392 4.5 5.6 1.0 CE A:MET455 4.5 7.6 0.7 CD A:PRO394 4.6 5.6 1.0 CA A:CYS445 4.6 4.7 1.0 O A:ILE447 4.7 4.4 1.0 N A:ILE447 4.8 5.0 1.0 CG2 A:ILE447 4.8 7.0 1.0 CA A:HIS450 4.9 6.8 1.0 CG A:MET455 4.9 9.8 0.3 CA A:ILE447 4.9 6.0 1.0

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