Copper in PDB 2yaq: X-Ray Induced Reduction of Laccase From Thermus Thermophilus HB27 (75. 0-87.5 Percent Dose)

All present enzymatic activity of X-Ray Induced Reduction of Laccase From Thermus Thermophilus HB27 (75. 0-87.5 Percent Dose):
1.10.3.2;

The structure of X-Ray Induced Reduction of Laccase From Thermus Thermophilus HB27 (75. 0-87.5 Percent Dose), PDB code: 2yaq was solved by H.Serrano-Posada, E.Rudino-Pinera, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.70 / 1.80
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	93.715, 110.411, 96.430, 90.00, 90.00, 90.00
R / Rfree (%)	14.6 / 16.8

The binding sites of Copper atom in the X-Ray Induced Reduction of Laccase From Thermus Thermophilus HB27 (75. 0-87.5 Percent Dose) (pdb code 2yaq). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 3 binding sites of Copper where determined in the X-Ray Induced Reduction of Laccase From Thermus Thermophilus HB27 (75. 0-87.5 Percent Dose), PDB code: 2yaq:
Jump to Copper binding site number: 1; 2; 3;

Copper binding site 1 out of 3 in the X-Ray Induced Reduction of Laccase From Thermus Thermophilus HB27 (75. 0-87.5 Percent Dose)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of X-Ray Induced Reduction of Laccase From Thermus Thermophilus HB27 (75. 0-87.5 Percent Dose) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu1463 b:9.4 occ:0.97 ND1 A:HIS393 2.1 7.4 1.0 ND1 A:HIS450 2.1 8.0 1.0 SG A:CYS445 2.2 7.2 1.0 CE1 A:HIS393 2.9 10.4 1.0 CG A:HIS450 3.1 6.1 1.0 CE1 A:HIS450 3.1 10.8 1.0 CG A:HIS393 3.2 9.8 1.0 CB A:CYS445 3.3 9.3 1.0 CB A:HIS450 3.4 4.6 1.0 CB A:HIS393 3.6 10.5 1.0 SD A:MET455 3.6 16.2 1.0 CD1 A:ILE447 3.9 4.8 1.0 CB A:ILE447 4.0 5.0 1.0 CA A:HIS393 4.0 5.2 1.0 NE2 A:HIS393 4.1 8.7 1.0 NE2 A:HIS450 4.2 6.3 1.0 CD2 A:HIS450 4.2 8.4 1.0 CD2 A:HIS393 4.3 3.7 1.0 CG1 A:ILE447 4.4 4.5 1.0 O A:ASP392 4.5 6.7 1.0 CD A:PRO394 4.6 2.4 1.0 CE A:MET455 4.6 15.9 1.0 CA A:CYS445 4.6 6.5 1.0 O A:ILE447 4.7 6.1 1.0 CG2 A:ILE447 4.8 4.8 1.0 N A:ILE447 4.8 4.4 1.0 CA A:ILE447 4.9 5.4 1.0 CA A:HIS450 4.9 6.5 1.0 C A:HIS393 5.0 6.6 1.0

Copper binding site 2 out of 3 in the X-Ray Induced Reduction of Laccase From Thermus Thermophilus HB27 (75. 0-87.5 Percent Dose)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of X-Ray Induced Reduction of Laccase From Thermus Thermophilus HB27 (75. 0-87.5 Percent Dose) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu1464 b:10.0 occ:0.94 ND1 A:HIS97 2.0 4.8 1.0 NE2 A:HIS135 2.1 6.3 1.0 NE2 A:HIS446 2.1 6.4 1.0 O A:OH1482 2.7 23.7 0.5 CE1 A:HIS97 2.9 8.0 1.0 CE1 A:HIS446 3.0 6.1 1.0 HO A:OH1482 3.0 28.4 0.5 CG A:HIS97 3.0 6.5 1.0 CD2 A:HIS135 3.1 5.8 1.0 CE1 A:HIS135 3.1 9.1 1.0 CD2 A:HIS446 3.2 6.3 1.0 CB A:HIS97 3.4 8.8 1.0 CZ2 A:TRP133 3.5 3.8 1.0 CD2 A:HIS95 3.7 12.4 1.0 CE2 A:TRP133 3.9 5.5 1.0 NE1 A:TRP133 4.0 6.4 1.0 NE2 A:HIS97 4.0 6.6 1.0 CD2 A:HIS97 4.1 8.7 1.0 ND1 A:HIS446 4.2 5.2 1.0 ND1 A:HIS135 4.2 6.4 1.0 CG A:HIS135 4.2 4.5 1.0 CG A:HIS446 4.3 5.0 1.0 CH2 A:TRP133 4.3 6.3 1.0 NE2 A:HIS95 4.3 15.6 1.0 NE2 A:HIS396 4.4 9.4 1.0 CD2 A:HIS396 4.5 11.4 1.0 CA A:HIS97 4.7 5.1 1.0 CD2 A:TRP133 4.8 3.6 1.0 CG A:HIS95 4.9 8.4 1.0 O A:HOH2491 5.0 19.3 1.0

Copper binding site 3 out of 3 in the X-Ray Induced Reduction of Laccase From Thermus Thermophilus HB27 (75. 0-87.5 Percent Dose)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of X-Ray Induced Reduction of Laccase From Thermus Thermophilus HB27 (75. 0-87.5 Percent Dose) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu1465 b:16.7 occ:0.39 NE2 A:HIS398 1.8 3.6 1.0 NE2 A:HIS444 1.9 9.7 1.0 NE2 A:HIS137 2.1 13.9 0.4 O A:OH1482 2.5 23.7 0.5 CD2 A:HIS137 2.6 13.9 0.4 CE1 A:HIS398 2.6 6.1 1.0 CD2 A:HIS444 2.8 8.9 1.0 CD2 A:HIS398 2.9 7.7 1.0 CD2 A:HIS137 2.9 11.2 0.6 CE1 A:HIS444 3.0 9.0 1.0 HO A:OH1482 3.0 28.4 0.5 NE2 A:HIS137 3.0 18.8 0.6 CE1 A:HIS137 3.3 19.9 0.4 CD2 A:HIS396 3.6 11.4 1.0 CD2 A:HIS95 3.7 12.4 1.0 ND1 A:HIS398 3.8 7.5 1.0 NE2 A:HIS95 3.8 15.6 1.0 CG A:HIS137 3.8 12.0 0.4 O A:HOH2491 3.8 19.3 1.0 CG A:HIS137 3.9 10.9 0.6 CG A:HIS398 3.9 8.3 1.0 CG A:HIS444 4.0 8.6 1.0 ND1 A:HIS444 4.0 8.4 1.0 CE1 A:HIS137 4.0 19.6 0.6 NE2 A:HIS396 4.1 9.4 1.0 ND1 A:HIS137 4.2 17.0 0.4 CG A:HIS95 4.3 8.4 1.0 CG2 A:VAL442 4.4 4.5 1.0 ND1 A:HIS137 4.5 22.1 0.6 CE1 A:HIS95 4.5 14.8 1.0 OE1 A:GLU451 4.7 7.5 0.4 ND1 A:HIS95 4.8 10.2 1.0 OE2 A:GLU451 4.8 13.9 0.4 CG A:HIS396 4.9 5.9 1.0 CB A:HIS137 4.9 10.0 0.6 CD A:GLU451 4.9 9.6 0.4

H.Serrano-Posada, S.Centeno-Leija, S.P.Rojas-Trejo, C.Rodriguez-Almazan, V.Stojanoff, E.Rudino-Pinera. X-Ray-Induced Catalytic Active-Site Reduction of A Multicopper Oxidase: Structural Insights Into the Proton-Relay Mechanism and O2-Reduction States. Acta Crystallogr.,Sect.D V. 71 2396 2015.
ISSN: ISSN 0907-4449
PubMed: 26627648
DOI: 10.1107/S1399004715018714