Copper in PDB 5k5k: Crystal Structure of Laccasse From Thermus Thermophilus HB27 (Ascorbic Acid 10 Min)

All present enzymatic activity of Crystal Structure of Laccasse From Thermus Thermophilus HB27 (Ascorbic Acid 10 Min):
1.10.3.2;

The structure of Crystal Structure of Laccasse From Thermus Thermophilus HB27 (Ascorbic Acid 10 Min), PDB code: 5k5k 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)	19.63 / 1.80
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	93.440, 109.860, 96.050, 90.00, 90.00, 90.00
R / Rfree (%)	17.5 / 21.6

The binding sites of Copper atom in the Crystal Structure of Laccasse From Thermus Thermophilus HB27 (Ascorbic Acid 10 Min) (pdb code 5k5k). 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 Laccasse From Thermus Thermophilus HB27 (Ascorbic Acid 10 Min), PDB code: 5k5k:
Jump to Copper binding site number: 1; 2; 3;

Copper binding site 1 out of 3 in the Crystal Structure of Laccasse From Thermus Thermophilus HB27 (Ascorbic Acid 10 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 Laccasse From Thermus Thermophilus HB27 (Ascorbic Acid 10 Min) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu501 b:18.1 occ:0.23 NE2 A:HIS398 1.9 8.9 1.0 NE2 A:HIS444 2.0 7.4 1.0 NE2 A:HIS137 2.2 25.0 1.0 CD2 A:HIS137 2.4 21.4 1.0 CE1 A:HIS398 2.5 7.1 1.0 CD2 A:HIS444 2.9 12.7 1.0 CE1 A:HIS444 2.9 7.1 1.0 CD2 A:HIS398 3.1 7.7 1.0 CD2 A:HIS95 3.4 10.6 0.2 CE1 A:HIS137 3.4 37.3 1.0 NE2 A:HIS95 3.6 12.1 0.2 CG A:HIS137 3.6 21.4 1.0 CD2 A:HIS95 3.6 10.3 0.8 ND1 A:HIS398 3.8 8.6 1.0 NE2 A:HIS95 3.9 13.4 0.8 ND1 A:HIS444 4.0 7.3 1.0 CG A:HIS444 4.0 10.0 1.0 CD2 A:HIS396 4.0 11.1 1.0 CG A:HIS398 4.1 6.7 1.0 CG A:HIS95 4.1 12.2 0.2 ND1 A:HIS137 4.1 24.1 1.0 CG A:HIS95 4.2 11.7 0.8 CE1 A:HIS95 4.4 11.3 0.2 CG2 A:VAL442 4.4 7.8 1.0 OE2 A:GLU451 4.5 7.8 0.5 NE2 A:HIS396 4.5 12.0 1.0 ND1 A:HIS95 4.6 10.3 0.2 CE1 A:HIS95 4.6 9.6 0.8 OE1 A:GLU451 4.8 19.7 0.5 CD A:GLU451 4.8 8.7 0.5 CB A:HIS137 4.8 15.1 1.0 ND1 A:HIS95 4.8 9.8 0.8 CB A:HIS95 4.8 11.4 0.2 CB A:HIS95 4.9 11.3 0.8

Copper binding site 2 out of 3 in the Crystal Structure of Laccasse From Thermus Thermophilus HB27 (Ascorbic Acid 10 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 Laccasse From Thermus Thermophilus HB27 (Ascorbic Acid 10 Min) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu502 b:15.8 occ:1.00 ND1 A:HIS97 1.9 11.7 1.0 NE2 A:HIS446 2.1 7.4 1.0 NE2 A:HIS135 2.1 10.7 1.0 CE1 A:HIS97 2.9 17.4 1.0 CD2 A:HIS135 2.9 7.9 1.0 CE1 A:HIS446 2.9 4.4 1.0 CG A:HIS97 3.0 11.4 1.0 CD2 A:HIS446 3.2 10.2 1.0 CE1 A:HIS135 3.2 14.3 1.0 CB A:HIS97 3.4 8.0 1.0 CZ2 A:TRP133 3.5 10.0 1.0 CD2 A:HIS95 3.6 10.6 0.2 CD2 A:HIS95 3.7 10.3 0.8 CE2 A:TRP133 3.8 5.2 1.0 NE1 A:TRP133 3.9 7.5 1.0 NE2 A:HIS97 4.0 9.0 1.0 CD2 A:HIS97 4.1 10.9 1.0 NE2 A:HIS95 4.1 12.1 0.2 ND1 A:HIS446 4.1 7.1 1.0 CG A:HIS135 4.1 11.5 1.0 ND1 A:HIS135 4.2 10.5 1.0 CH2 A:TRP133 4.2 6.6 1.0 CG A:HIS446 4.2 10.8 1.0 NE2 A:HIS95 4.4 13.4 0.8 CD2 A:HIS396 4.4 11.1 1.0 NE2 A:HIS396 4.4 12.0 1.0 CA A:HIS97 4.7 9.0 1.0 CD2 A:TRP133 4.8 4.7 1.0 CG A:HIS95 4.8 12.2 0.2 CG A:HIS95 4.9 11.7 0.8 CD1 A:TRP133 4.9 5.3 1.0

Copper binding site 3 out of 3 in the Crystal Structure of Laccasse From Thermus Thermophilus HB27 (Ascorbic Acid 10 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 Laccasse From Thermus Thermophilus HB27 (Ascorbic Acid 10 Min) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu503 b:12.0 occ:0.74 ND1 A:HIS393 2.0 9.3 1.0 ND1 A:HIS450 2.1 9.2 1.0 SG A:CYS445 2.2 10.0 1.0 CE1 A:HIS393 2.9 13.4 1.0 CG A:HIS450 3.0 6.7 1.0 CE1 A:HIS450 3.0 12.7 1.0 CG A:HIS393 3.1 8.7 1.0 CB A:CYS445 3.2 8.2 1.0 CB A:HIS450 3.3 6.5 1.0 SD A:MET455 3.4 8.4 0.3 CB A:HIS393 3.6 7.5 1.0 SD A:MET455 3.7 15.8 0.7 CE A:MET455 3.8 9.3 0.3 CA A:HIS393 3.9 8.0 1.0 CB A:ILE447 4.0 9.2 1.0 NE2 A:HIS393 4.1 12.5 1.0 CD1 A:ILE447 4.1 10.9 1.0 NE2 A:HIS450 4.2 6.8 1.0 CD2 A:HIS450 4.2 7.3 1.0 CD2 A:HIS393 4.2 7.7 1.0 O A:ASP392 4.4 7.8 1.0 CE A:MET455 4.5 7.5 0.7 CG1 A:ILE447 4.5 8.0 1.0 CD A:PRO394 4.6 4.8 1.0 CA A:CYS445 4.6 6.2 1.0 O A:ILE447 4.7 8.8 1.0 CG2 A:ILE447 4.7 11.2 1.0 N A:ILE447 4.8 8.3 1.0 CA A:HIS450 4.9 9.2 1.0 CG A:MET455 4.9 11.8 0.3 C A:HIS393 4.9 10.2 1.0 CA A:ILE447 4.9 8.9 1.0 N A:HIS393 5.0 8.4 1.0 N A:PRO394 5.0 8.8 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.