Copper in PDB 4a68: Mutations in the Neighbourhood of Cota-Laccase Trinuclear Site: D116N Mutant

All present enzymatic activity of Mutations in the Neighbourhood of Cota-Laccase Trinuclear Site: D116N Mutant:
1.10.3.2;

The structure of Mutations in the Neighbourhood of Cota-Laccase Trinuclear Site: D116N Mutant, PDB code: 4a68 was solved by C.S.Silva, P.F.Lindley, I.Bento, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	87.94 / 2.00
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	101.548, 101.548, 136.717, 90.00, 90.00, 120.00
R / Rfree (%)	16.891 / 20.013

The binding sites of Copper atom in the Mutations in the Neighbourhood of Cota-Laccase Trinuclear Site: D116N Mutant (pdb code 4a68). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 4 binding sites of Copper where determined in the Mutations in the Neighbourhood of Cota-Laccase Trinuclear Site: D116N Mutant, PDB code: 4a68:
Jump to Copper binding site number: 1; 2; 3; 4;

Copper binding site 1 out of 4 in the Mutations in the Neighbourhood of Cota-Laccase Trinuclear Site: D116N Mutant


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Mutations in the Neighbourhood of Cota-Laccase Trinuclear Site: D116N Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu1511 b:15.8 occ:1.00 ND1 A:HIS497 2.0 15.7 1.0 ND1 A:HIS419 2.0 15.2 1.0 SG A:CYS492 2.2 12.3 1.0 CE1 A:HIS419 3.0 15.5 1.0 CE1 A:HIS497 3.0 14.3 1.0 CG A:HIS497 3.0 14.5 1.0 CG A:HIS419 3.0 15.0 1.0 CB A:CYS492 3.2 10.3 1.0 CB A:HIS497 3.3 12.7 1.0 SD A:MET502 3.4 13.8 1.0 CB A:HIS419 3.4 13.2 1.0 CD1 A:ILE494 4.0 14.0 1.0 CE A:MET502 4.0 12.1 1.0 CA A:HIS419 4.1 13.5 1.0 CB A:ILE494 4.1 11.6 1.0 NE2 A:HIS419 4.1 16.5 1.0 NE2 A:HIS497 4.1 14.4 1.0 CD2 A:HIS497 4.2 9.5 1.0 CD2 A:HIS419 4.2 15.6 1.0 CG1 A:ILE494 4.4 13.7 1.0 CA A:CYS492 4.6 10.9 1.0 CD A:PRO420 4.6 11.0 1.0 CD1 A:LEU386 4.6 17.2 1.0 O A:HOH2403 4.7 27.2 1.0 CG2 A:ILE494 4.9 10.8 1.0 CA A:HIS497 4.9 13.0 1.0 CG A:MET502 4.9 11.9 1.0 O A:THR418 4.9 15.2 1.0 N A:ILE494 4.9 11.5 1.0

Copper binding site 2 out of 4 in the Mutations in the Neighbourhood of Cota-Laccase Trinuclear Site: D116N Mutant


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Mutations in the Neighbourhood of Cota-Laccase Trinuclear Site: D116N Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu1512 b:16.8 occ:1.00 ND1 A:HIS107 2.0 12.0 1.0 NE2 A:HIS153 2.0 12.8 1.0 NE2 A:HIS493 2.0 11.9 1.0 O1 A:PER1516 2.8 24.4 1.0 O2 A:PER1516 2.9 25.3 1.0 CE1 A:HIS153 2.9 10.2 1.0 CE1 A:HIS107 2.9 9.9 1.0 CE1 A:HIS493 2.9 9.6 1.0 CG A:HIS107 3.0 9.6 1.0 CD2 A:HIS153 3.1 10.6 1.0 CD2 A:HIS493 3.1 11.7 1.0 CB A:HIS107 3.4 10.5 1.0 CZ2 A:TRP151 3.7 10.2 1.0 O A:HOH2209 3.9 28.9 1.0 CD2 A:HIS105 3.9 10.2 1.0 CE2 A:TRP151 4.0 10.5 1.0 ND1 A:HIS153 4.1 12.7 1.0 NE2 A:HIS107 4.1 9.0 1.0 ND1 A:HIS493 4.1 8.3 1.0 NE1 A:TRP151 4.1 9.3 1.0 CD2 A:HIS107 4.1 7.8 1.0 CG A:HIS153 4.2 9.8 1.0 CU A:CU1514 4.2 16.9 1.0 CG A:HIS493 4.2 10.1 1.0 CB A:ALA297 4.3 9.2 1.0 NE2 A:HIS105 4.4 12.6 1.0 CH2 A:TRP151 4.5 8.3 1.0 CA A:HIS107 4.5 10.5 1.0 NE2 A:HIS422 4.6 13.2 1.0 CU A:CU1513 4.6 18.2 1.0 CD2 A:HIS422 4.7 11.9 1.0 CD2 A:TRP151 5.0 9.6 1.0

Copper binding site 3 out of 4 in the Mutations in the Neighbourhood of Cota-Laccase Trinuclear Site: D116N Mutant


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Mutations in the Neighbourhood of Cota-Laccase Trinuclear Site: D116N Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu1513 b:18.2 occ:1.00 O1 A:PER1516 1.9 24.4 1.0 NE2 A:HIS424 2.0 13.9 1.0 NE2 A:HIS155 2.0 12.6 1.0 NE2 A:HIS491 2.0 11.9 1.0 O2 A:PER1516 2.4 25.3 1.0 CD2 A:HIS155 2.9 11.7 1.0 CE1 A:HIS424 2.9 14.4 1.0 CD2 A:HIS491 3.0 10.3 1.0 CE1 A:HIS491 3.0 10.7 1.0 CD2 A:HIS424 3.1 12.5 1.0 CE1 A:HIS155 3.1 13.9 1.0 O A:HOH2209 3.1 28.9 1.0 CD2 A:HIS422 3.7 11.9 1.0 CU A:CU1514 3.7 16.9 1.0 CD2 A:HIS105 3.9 10.2 1.0 NE2 A:HIS105 3.9 12.6 1.0 ND1 A:HIS491 4.1 12.3 1.0 ND1 A:HIS424 4.1 13.7 1.0 CG A:HIS155 4.1 12.8 1.0 CG A:HIS491 4.1 11.0 1.0 ND1 A:HIS155 4.2 11.2 1.0 NE2 A:HIS422 4.2 13.2 1.0 CG A:HIS424 4.2 13.2 1.0 CG2 A:VAL489 4.4 10.6 0.5 OE2 A:GLU498 4.5 16.1 1.0 CU A:CU1512 4.6 16.8 1.0 CG A:HIS105 4.6 10.6 1.0 NE2 A:HIS493 4.7 11.9 1.0 CE1 A:HIS105 4.7 10.7 1.0 CD2 A:HIS493 4.7 11.7 1.0 CE1 A:HIS153 4.9 10.2 1.0 CG A:HIS422 5.0 11.5 1.0 CG1 A:VAL489 5.0 11.1 0.5 OE1 A:GLU498 5.0 15.2 1.0

Copper binding site 4 out of 4 in the Mutations in the Neighbourhood of Cota-Laccase Trinuclear Site: D116N Mutant


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 4 of Mutations in the Neighbourhood of Cota-Laccase Trinuclear Site: D116N Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu1514 b:16.9 occ:1.00 O2 A:PER1516 2.0 25.3 1.0 NE2 A:HIS422 2.0 13.2 1.0 NE2 A:HIS105 2.0 12.6 1.0 O A:OH1515 2.1 13.5 1.0 CE1 A:HIS105 2.9 10.7 1.0 CE1 A:HIS422 2.9 10.8 1.0 CD2 A:HIS422 3.0 11.9 1.0 CD2 A:HIS105 3.1 10.2 1.0 CD2 A:HIS424 3.1 12.5 1.0 NE2 A:HIS424 3.3 13.9 1.0 O1 A:PER1516 3.4 24.4 1.0 ND1 A:HIS107 3.5 12.0 1.0 CG A:HIS424 3.7 13.2 1.0 CG A:HIS107 3.7 9.6 1.0 CU A:CU1513 3.7 18.2 1.0 CA A:HIS107 3.8 10.5 1.0 CE1 A:HIS424 3.9 14.4 1.0 CE1 A:HIS107 3.9 9.9 1.0 ND1 A:HIS105 4.0 11.8 1.0 N A:GLY108 4.0 11.3 1.0 ND1 A:HIS422 4.0 10.9 1.0 ND1 A:HIS424 4.1 13.7 1.0 CB A:HIS107 4.1 10.5 1.0 CG A:HIS422 4.1 11.5 1.0 CG A:HIS105 4.1 10.6 1.0 CD2 A:HIS107 4.2 7.8 1.0 CU A:CU1512 4.2 16.8 1.0 NE2 A:HIS107 4.3 9.0 1.0 CA A:HIS424 4.3 12.2 1.0 O A:HOH2141 4.3 15.9 1.0 C A:HIS107 4.4 10.9 1.0 CB A:HIS424 4.5 12.0 1.0 O A:HOH2404 4.5 9.4 1.0 N A:HIS107 4.8 9.7 1.0 O A:LEU423 4.9 12.1 1.0 N A:HIS424 4.9 12.9 1.0 O A:LEU106 4.9 10.0 1.0 NE2 A:HIS491 4.9 11.9 1.0

C.S.Silva, J.M.Damas, Z.Chen, V.Brissos, L.O.Martins, C.M.Soares, P.F.Lindley, I.Bento. The Role of ASP116 in the Reductive Cleavage of Dioxygen to Water in Cota Laccase: Assistance During the Proton Transfer Mechanism Acta Crystallogr.,Sect.D V. 68 186 2012.
ISSN: ISSN 0907-4449
PubMed: 22281748
DOI: 10.1107/S0907444911054503