Copper in PDB 5o4i: Crystal Structure of Mutant M54L/M64L/M96L of Two-Domain Laccase From Streptomyces Griseoflavus Dialyzed Against Solution Containing 0.25 Mm Copper Sulfate

All present enzymatic activity of Crystal Structure of Mutant M54L/M64L/M96L of Two-Domain Laccase From Streptomyces Griseoflavus Dialyzed Against Solution Containing 0.25 Mm Copper Sulfate:
1.10.3.2;

The structure of Crystal Structure of Mutant M54L/M64L/M96L of Two-Domain Laccase From Streptomyces Griseoflavus Dialyzed Against Solution Containing 0.25 Mm Copper Sulfate, PDB code: 5o4i was solved by A.G.Gabdulkhakov, T.V.Tishchenko, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 1.80
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	76.933, 94.931, 116.587, 90.08, 90.20, 91.65
R / Rfree (%)	17.7 / 22.2

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 20; Page 3, Binding sites: 21 - 30; Page 4, Binding sites: 31 - 40; Page 5, Binding sites: 41 - 45;

Binding sites:

The binding sites of Copper atom in the Crystal Structure of Mutant M54L/M64L/M96L of Two-Domain Laccase From Streptomyces Griseoflavus Dialyzed Against Solution Containing 0.25 Mm Copper Sulfate (pdb code 5o4i). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 45 binding sites of Copper where determined in the Crystal Structure of Mutant M54L/M64L/M96L of Two-Domain Laccase From Streptomyces Griseoflavus Dialyzed Against Solution Containing 0.25 Mm Copper Sulfate, PDB code: 5o4i:
Jump to Copper binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Copper binding site 1 out of 45 in the Crystal Structure of Mutant M54L/M64L/M96L of Two-Domain Laccase From Streptomyces Griseoflavus Dialyzed Against Solution Containing 0.25 Mm Copper Sulfate


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 Mutant M54L/M64L/M96L of Two-Domain Laccase From Streptomyces Griseoflavus Dialyzed Against Solution Containing 0.25 Mm Copper Sulfate within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu401 b:18.8 occ:1.00 ND1 A:HIS294 2.0 16.0 1.0 ND1 A:HIS232 2.1 18.5 1.0 SG A:CYS289 2.2 18.1 1.0 CG A:HIS294 3.0 17.2 1.0 CE1 A:HIS294 3.0 18.0 1.0 CE1 A:HIS232 3.0 14.7 1.0 CG A:HIS232 3.0 16.1 1.0 CB A:CYS289 3.2 16.1 1.0 CB A:HIS294 3.3 18.0 1.0 CB A:HIS232 3.4 15.8 1.0 SD A:MET299 3.5 20.2 1.0 CA A:HIS232 3.7 16.4 1.0 CG2 A:VAL291 4.0 20.5 1.0 CB A:VAL291 4.1 18.2 1.0 CD2 A:HIS294 4.1 18.3 1.0 NE2 A:HIS294 4.1 17.0 1.0 NE2 A:HIS232 4.1 16.4 1.0 CE A:MET299 4.2 22.0 1.0 CD2 A:HIS232 4.2 16.1 1.0 O A:TYR231 4.2 15.2 1.0 CA A:CYS289 4.5 15.8 1.0 N A:THR233 4.6 16.7 1.0 N A:HIS232 4.7 16.5 1.0 C A:HIS232 4.7 18.7 1.0 CA A:HIS294 4.8 19.1 1.0 C A:TYR231 4.8 15.8 1.0 CD2 A:PHE196 4.9 17.6 1.0 CG1 A:VAL291 4.9 15.8 1.0 N A:VAL291 5.0 17.6 1.0 CG A:MET299 5.0 20.6 1.0

Copper binding site 2 out of 45 in the Crystal Structure of Mutant M54L/M64L/M96L of Two-Domain Laccase From Streptomyces Griseoflavus Dialyzed Against Solution Containing 0.25 Mm Copper Sulfate


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 Mutant M54L/M64L/M96L of Two-Domain Laccase From Streptomyces Griseoflavus Dialyzed Against Solution Containing 0.25 Mm Copper Sulfate within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu402 b:27.8 occ:0.54 NE2 A:HIS237 2.2 23.9 1.0 NE2 A:HIS288 2.2 21.1 1.0 NE2 C:HIS159 2.3 20.0 1.0 O A:HOH517 2.3 23.0 1.0 CE1 A:HIS288 3.0 20.3 1.0 CE1 A:HIS237 3.0 27.1 1.0 CE1 C:HIS159 3.2 18.6 1.0 CD2 C:HIS159 3.2 18.6 1.0 CD2 A:HIS237 3.3 22.0 1.0 CD2 A:HIS288 3.3 21.0 1.0 O C:HOH559 3.6 25.1 1.0 CD2 A:HIS235 3.8 21.6 1.0 CU C:CU401 3.8 23.0 0.5 NE2 C:HIS103 3.9 34.9 1.0 CE1 C:HIS103 3.9 31.9 1.0 NE2 A:HIS235 4.1 22.6 1.0 ND1 A:HIS288 4.2 20.0 1.0 ND1 A:HIS237 4.2 23.2 1.0 ND1 C:HIS159 4.3 20.0 1.0 CG A:HIS237 4.4 21.6 1.0 CG C:HIS159 4.4 19.3 1.0 CG A:HIS288 4.4 18.5 1.0 ND1 C:HIS103 4.4 33.4 1.0 CD2 C:HIS103 4.5 32.5 1.0 NE2 A:HIS290 4.5 20.6 1.0 CU C:CU401 4.7 24.4 0.5 CD2 C:HIS165 4.7 25.9 1.0 SD A:MET286 4.8 41.6 1.0 CG C:HIS103 4.8 29.4 1.0 CD2 A:HIS290 4.8 19.0 1.0

Copper binding site 3 out of 45 in the Crystal Structure of Mutant M54L/M64L/M96L of Two-Domain Laccase From Streptomyces Griseoflavus Dialyzed Against Solution Containing 0.25 Mm Copper Sulfate


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 Mutant M54L/M64L/M96L of Two-Domain Laccase From Streptomyces Griseoflavus Dialyzed Against Solution Containing 0.25 Mm Copper Sulfate within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu403 b:22.5 occ:0.50 CU A:CU403 0.0 22.5 0.5 CU A:CU403 0.7 22.8 0.5 NE2 A:HIS105 1.9 18.1 1.0 NE2 B:HIS290 2.0 16.2 1.0 NE2 A:HIS157 2.1 18.6 1.0 O B:HOH562 2.6 23.3 1.0 CE1 A:HIS105 2.9 18.0 1.0 CE1 B:HIS290 2.9 14.5 1.0 CD2 B:HIS290 3.0 14.5 1.0 CD2 A:HIS105 3.0 18.0 1.0 CE1 A:HIS157 3.0 18.4 1.0 NE2 A:HIS103 3.1 26.6 1.0 CD2 A:HIS157 3.1 19.2 1.0 CD2 A:HIS103 3.4 24.1 1.0 ND1 A:HIS105 4.0 17.0 1.0 ND1 B:HIS290 4.0 13.2 1.0 NE2 B:HIS235 4.1 17.3 1.0 CG B:HIS290 4.1 14.3 1.0 CG A:HIS105 4.1 16.2 1.0 ND1 A:HIS157 4.1 17.9 1.0 CB A:ALA267 4.2 15.0 1.0 CG A:HIS157 4.2 17.1 1.0 CE1 A:HIS155 4.3 16.8 1.0 CE1 A:HIS103 4.3 26.2 1.0 CD2 B:HIS235 4.3 16.3 1.0 CU B:CU402 4.5 28.9 0.7 O A:HOH564 4.5 20.8 1.0 CE1 B:HIS235 4.7 15.9 1.0 CG A:HIS103 4.8 21.2 1.0

Copper binding site 4 out of 45 in the Crystal Structure of Mutant M54L/M64L/M96L of Two-Domain Laccase From Streptomyces Griseoflavus Dialyzed Against Solution Containing 0.25 Mm Copper Sulfate


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 Mutant M54L/M64L/M96L of Two-Domain Laccase From Streptomyces Griseoflavus Dialyzed Against Solution Containing 0.25 Mm Copper Sulfate within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu403 b:22.8 occ:0.50 CU A:CU403 0.0 22.8 0.5 CU A:CU403 0.7 22.5 0.5 O B:HOH562 2.0 23.3 1.0 NE2 B:HIS290 2.1 16.2 1.0 NE2 A:HIS105 2.2 18.1 1.0 NE2 A:HIS157 2.4 18.6 1.0 NE2 A:HIS103 2.6 26.6 1.0 CE1 A:HIS157 3.1 18.4 1.0 CD2 A:HIS103 3.1 24.1 1.0 CD2 B:HIS290 3.1 14.5 1.0 CE1 A:HIS105 3.1 18.0 1.0 CE1 B:HIS290 3.2 14.5 1.0 CD2 A:HIS105 3.2 18.0 1.0 CD2 A:HIS157 3.5 19.2 1.0 NE2 B:HIS235 3.7 17.3 1.0 CE1 A:HIS103 3.8 26.2 1.0 CU B:CU402 3.9 28.9 0.7 CD2 B:HIS235 4.0 16.3 1.0 ND1 B:HIS290 4.2 13.2 1.0 CG B:HIS290 4.2 14.3 1.0 O A:HOH564 4.2 20.8 1.0 ND1 A:HIS105 4.2 17.0 1.0 ND1 A:HIS157 4.3 17.9 1.0 CG A:HIS105 4.3 16.2 1.0 CG A:HIS103 4.3 21.2 1.0 CE1 B:HIS235 4.5 15.9 1.0 CG A:HIS157 4.5 17.1 1.0 ND1 A:HIS103 4.6 25.4 1.0 CB A:ALA267 4.7 15.0 1.0 CE1 B:HIS288 4.8 16.8 1.0 CD2 A:HIS159 4.8 17.3 1.0 CG B:HIS235 4.8 16.3 1.0 CE1 A:HIS155 4.9 16.8 1.0 NE2 B:HIS288 4.9 17.1 1.0 NE2 A:HIS159 5.0 17.9 1.0

Copper binding site 5 out of 45 in the Crystal Structure of Mutant M54L/M64L/M96L of Two-Domain Laccase From Streptomyces Griseoflavus Dialyzed Against Solution Containing 0.25 Mm Copper Sulfate


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 Mutant M54L/M64L/M96L of Two-Domain Laccase From Streptomyces Griseoflavus Dialyzed Against Solution Containing 0.25 Mm Copper Sulfate within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu401 b:15.7 occ:1.00 ND1 B:HIS232 2.0 13.3 1.0 ND1 B:HIS294 2.0 14.5 1.0 SG B:CYS289 2.2 15.2 1.0 CE1 B:HIS232 2.9 13.7 1.0 CG B:HIS294 3.0 16.1 1.0 CG B:HIS232 3.0 13.7 1.0 CE1 B:HIS294 3.0 15.7 1.0 CB B:CYS289 3.2 14.9 1.0 CB B:HIS294 3.3 15.5 1.0 CB B:HIS232 3.4 14.3 1.0 SD B:MET299 3.4 17.6 1.0 CA B:HIS232 3.7 14.8 1.0 CE B:MET299 4.0 16.7 1.0 NE2 B:HIS232 4.0 14.0 1.0 O B:TYR231 4.0 15.8 1.0 NE2 B:HIS294 4.1 16.6 1.0 CD2 B:HIS232 4.1 13.8 1.0 CD2 B:HIS294 4.1 17.3 1.0 CG2 B:VAL291 4.1 14.3 1.0 CB B:VAL291 4.1 13.8 1.0 CA B:CYS289 4.5 14.4 1.0 N B:THR233 4.6 14.5 1.0 N B:HIS232 4.7 15.7 1.0 C B:HIS232 4.8 15.7 1.0 CD2 B:PHE196 4.8 15.6 1.0 CA B:HIS294 4.8 16.1 1.0 C B:TYR231 4.8 16.5 1.0 CG B:MET299 4.9 18.4 1.0 CE2 B:PHE196 4.9 15.4 1.0 CG1 B:VAL291 5.0 13.6 1.0 N B:VAL291 5.0 14.4 1.0

Copper binding site 6 out of 45 in the Crystal Structure of Mutant M54L/M64L/M96L of Two-Domain Laccase From Streptomyces Griseoflavus Dialyzed Against Solution Containing 0.25 Mm Copper Sulfate


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 Mutant M54L/M64L/M96L of Two-Domain Laccase From Streptomyces Griseoflavus Dialyzed Against Solution Containing 0.25 Mm Copper Sulfate within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu402 b:28.9 occ:0.66 NE2 B:HIS237 2.0 19.4 1.0 O B:HOH562 2.0 23.3 1.0 NE2 A:HIS159 2.1 17.9 1.0 NE2 B:HIS288 2.2 17.1 1.0 CE1 B:HIS237 2.8 18.9 1.0 CD2 A:HIS159 3.1 17.3 1.0 CE1 B:HIS288 3.1 16.8 1.0 CE1 A:HIS159 3.2 19.0 1.0 CD2 B:HIS237 3.2 17.1 1.0 CD2 B:HIS288 3.3 19.7 1.0 O A:HOH564 3.7 20.8 1.0 NE2 A:HIS103 3.8 26.6 1.0 CU A:CU403 3.9 22.8 0.5 CE1 A:HIS103 3.9 26.2 1.0 CD2 B:HIS235 3.9 16.3 1.0 ND1 B:HIS237 3.9 21.3 1.0 CG B:HIS237 4.2 18.9 1.0 NE2 B:HIS235 4.2 17.3 1.0 CG A:HIS159 4.2 17.5 1.0 ND1 B:HIS288 4.2 17.3 1.0 ND1 A:HIS159 4.2 17.8 1.0 CG B:HIS288 4.4 16.7 1.0 CD2 A:HIS103 4.5 24.1 1.0 ND1 A:HIS103 4.5 25.4 1.0 CU A:CU403 4.5 22.5 0.5 NE2 B:HIS290 4.5 16.2 1.0 ND1 A:HIS165 4.8 22.2 1.0 SD B:MET286 4.8 37.3 1.0 CG A:HIS103 4.8 21.2 1.0 CD2 B:HIS290 4.9 14.5 1.0

Copper binding site 7 out of 45 in the Crystal Structure of Mutant M54L/M64L/M96L of Two-Domain Laccase From Streptomyces Griseoflavus Dialyzed Against Solution Containing 0.25 Mm Copper Sulfate


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 Mutant M54L/M64L/M96L of Two-Domain Laccase From Streptomyces Griseoflavus Dialyzed Against Solution Containing 0.25 Mm Copper Sulfate within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu403 b:23.6 occ:0.50 CU B:CU403 0.0 23.6 0.5 CU B:CU403 0.8 21.7 0.5 NE2 B:HIS105 1.9 21.4 1.0 NE2 C:HIS290 2.0 17.2 1.0 NE2 B:HIS157 2.1 14.2 1.0 O C:HOH523 2.6 23.5 1.0 CD2 B:HIS105 2.9 20.6 1.0 CE1 C:HIS290 3.0 17.4 1.0 CE1 B:HIS105 3.0 18.6 1.0 CD2 C:HIS290 3.0 14.7 1.0 CE1 B:HIS157 3.1 16.6 1.0 NE2 B:HIS103 3.1 26.4 1.0 CD2 B:HIS157 3.1 15.2 1.0 CD2 B:HIS103 3.5 27.4 1.0 CE1 B:HIS155 4.0 17.0 1.0 CG B:HIS105 4.0 18.1 1.0 ND1 B:HIS105 4.0 16.6 1.0 ND1 C:HIS290 4.1 14.4 1.0 CG C:HIS290 4.1 14.6 1.0 CB B:ALA267 4.2 14.6 1.0 ND1 B:HIS157 4.2 17.7 1.0 CG B:HIS157 4.2 16.0 1.0 CE1 B:HIS103 4.3 25.4 1.0 NE2 C:HIS235 4.3 18.3 1.0 CU C:CU403 4.5 27.8 0.7 CD2 C:HIS235 4.5 18.1 1.0 O B:HOH570 4.7 23.1 1.0 CG B:HIS103 4.8 25.2 1.0 ND1 B:HIS155 4.8 16.4 1.0 NE2 B:HIS155 4.8 16.4 1.0 CE1 C:HIS235 4.8 16.7 1.0

Copper binding site 8 out of 45 in the Crystal Structure of Mutant M54L/M64L/M96L of Two-Domain Laccase From Streptomyces Griseoflavus Dialyzed Against Solution Containing 0.25 Mm Copper Sulfate


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 Mutant M54L/M64L/M96L of Two-Domain Laccase From Streptomyces Griseoflavus Dialyzed Against Solution Containing 0.25 Mm Copper Sulfate within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu403 b:21.7 occ:0.50 CU B:CU403 0.0 21.7 0.5 CU B:CU403 0.8 23.6 0.5 O C:HOH523 1.9 23.5 1.0 NE2 C:HIS290 2.2 17.2 1.0 NE2 B:HIS105 2.3 21.4 1.0 NE2 B:HIS157 2.3 14.2 1.0 NE2 B:HIS103 2.6 26.4 1.0 CE1 B:HIS157 3.1 16.6 1.0 CD2 B:HIS103 3.1 27.4 1.0 CD2 C:HIS290 3.1 14.7 1.0 CD2 B:HIS105 3.2 20.6 1.0 CE1 C:HIS290 3.2 17.4 1.0 CE1 B:HIS105 3.3 18.6 1.0 CD2 B:HIS157 3.5 15.2 1.0 CE1 B:HIS103 3.7 25.4 1.0 CU C:CU403 3.8 27.8 0.7 NE2 C:HIS235 3.9 18.3 1.0 CD2 C:HIS235 4.1 18.1 1.0 ND1 B:HIS157 4.3 17.7 1.0 CG C:HIS290 4.3 14.6 1.0 ND1 C:HIS290 4.3 14.4 1.0 CG B:HIS103 4.3 25.2 1.0 CG B:HIS105 4.3 18.1 1.0 ND1 B:HIS105 4.3 16.6 1.0 O B:HOH570 4.4 23.1 1.0 CG B:HIS157 4.5 16.0 1.0 ND1 B:HIS103 4.6 27.4 1.0 CE1 C:HIS235 4.6 16.7 1.0 CE1 B:HIS155 4.8 17.0 1.0 CB B:ALA267 4.8 14.6 1.0 CE1 C:HIS288 4.8 17.7 1.0 CD2 B:HIS159 4.9 18.4 1.0 CG C:HIS235 4.9 15.8 1.0 NE2 C:HIS288 4.9 16.9 1.0

Copper binding site 9 out of 45 in the Crystal Structure of Mutant M54L/M64L/M96L of Two-Domain Laccase From Streptomyces Griseoflavus Dialyzed Against Solution Containing 0.25 Mm Copper Sulfate


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 Mutant M54L/M64L/M96L of Two-Domain Laccase From Streptomyces Griseoflavus Dialyzed Against Solution Containing 0.25 Mm Copper Sulfate within 5.0Å range: probe atom residue distance (Å) B Occ C:Cu401 b:24.4 occ:0.50 CU C:CU401 0.0 24.4 0.5 CU C:CU401 0.9 23.0 0.5 NE2 C:HIS105 2.0 16.6 1.0 NE2 A:HIS290 2.1 20.6 1.0 NE2 C:HIS157 2.2 17.5 1.0 O A:HOH517 2.6 23.0 1.0 CD2 C:HIS105 2.9 17.6 1.0 CE1 A:HIS290 2.9 20.9 1.0 CE1 C:HIS105 3.0 15.4 1.0 CD2 C:HIS157 3.1 18.4 1.0 CD2 A:HIS290 3.1 19.0 1.0 NE2 C:HIS103 3.1 34.9 1.0 CE1 C:HIS157 3.2 18.6 1.0 CD2 C:HIS103 3.4 32.5 1.0 CE1 C:HIS155 4.0 16.7 1.0 CG C:HIS105 4.0 16.8 1.0 CB C:ALA267 4.0 17.0 1.0 ND1 A:HIS290 4.0 18.6 1.0 ND1 C:HIS105 4.1 15.2 1.0 CG A:HIS290 4.2 17.9 1.0 CG C:HIS157 4.2 17.4 1.0 ND1 C:HIS157 4.3 18.5 1.0 NE2 A:HIS235 4.4 22.6 1.0 CE1 C:HIS103 4.4 31.9 1.0 CD2 A:HIS235 4.6 21.6 1.0 O C:HOH559 4.7 25.1 1.0 CU A:CU402 4.7 27.8 0.5 NE2 C:HIS155 4.8 17.1 1.0 CG C:HIS103 4.8 29.4 1.0 CE1 A:HIS235 4.8 23.1 1.0 ND1 C:HIS155 4.8 16.6 1.0

Copper binding site 10 out of 45 in the Crystal Structure of Mutant M54L/M64L/M96L of Two-Domain Laccase From Streptomyces Griseoflavus Dialyzed Against Solution Containing 0.25 Mm Copper Sulfate


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 10 of Crystal Structure of Mutant M54L/M64L/M96L of Two-Domain Laccase From Streptomyces Griseoflavus Dialyzed Against Solution Containing 0.25 Mm Copper Sulfate within 5.0Å range: probe atom residue distance (Å) B Occ C:Cu401 b:23.0 occ:0.50 CU C:CU401 0.0 23.0 0.5 CU C:CU401 0.9 24.4 0.5 O A:HOH517 1.7 23.0 1.0 NE2 A:HIS290 2.0 20.6 1.0 NE2 C:HIS157 2.4 17.5 1.0 NE2 C:HIS105 2.4 16.6 1.0 NE2 C:HIS103 2.7 34.9 1.0 CE1 A:HIS290 3.0 20.9 1.0 CD2 A:HIS290 3.1 19.0 1.0 CD2 C:HIS103 3.1 32.5 1.0 CE1 C:HIS157 3.1 18.6 1.0 CD2 C:HIS105 3.3 17.6 1.0 CE1 C:HIS105 3.4 15.4 1.0 CD2 C:HIS157 3.5 18.4 1.0 CE1 C:HIS103 3.8 31.9 1.0 CU A:CU402 3.8 27.8 0.5 NE2 A:HIS235 3.9 22.6 1.0 ND1 A:HIS290 4.1 18.6 1.0 O C:HOH559 4.1 25.1 1.0 CD2 A:HIS235 4.1 21.6 1.0 CG A:HIS290 4.2 17.9 1.0 CG C:HIS103 4.3 29.4 1.0 ND1 C:HIS157 4.3 18.5 1.0 ND1 C:HIS105 4.5 15.2 1.0 CG C:HIS105 4.5 16.8 1.0 CG C:HIS157 4.6 17.4 1.0 CE1 A:HIS235 4.6 23.1 1.0 CB C:ALA267 4.6 17.0 1.0 ND1 C:HIS103 4.7 33.4 1.0 CE1 A:HIS288 4.8 20.3 1.0 CE1 C:HIS155 4.8 16.7 1.0 CD2 C:HIS159 4.9 18.6 1.0 CG A:HIS235 4.9 21.2 1.0 NE2 C:HIS159 4.9 20.0 1.0 NE2 A:HIS288 5.0 21.1 1.0

A.G.Gabdulkhakov, O.S.Kostareva, I.A.Kolyadenko, A.O.Mikhaylina, L.I.Trubitsina, S.V.Tishchenko. Incorporation of Copper Ions Into T2/T3 Centers of Two-Domain Laccases. Mol.Biol.(Moscow) V. 52 29 2018.
ISSN: ISSN 0026-8984
PubMed: 29512633
DOI: 10.7868/S0026898418010056