Copper in PDB 4a66: Mutations in the Neighbourhood of Cota-Laccase Trinuclear Site: D116A Mutant

All present enzymatic activity of Mutations in the Neighbourhood of Cota-Laccase Trinuclear Site: D116A Mutant:
1.10.3.2;

The structure of Mutations in the Neighbourhood of Cota-Laccase Trinuclear Site: D116A Mutant, PDB code: 4a66 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)	19.99 / 1.95
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	101.683, 101.683, 136.611, 90.00, 90.00, 120.00
R / Rfree (%)	17.408 / 20.306

The binding sites of Copper atom in the Mutations in the Neighbourhood of Cota-Laccase Trinuclear Site: D116A Mutant (pdb code 4a66). 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: D116A Mutant, PDB code: 4a66:
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: D116A 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: D116A Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu1512 b:15.3 occ:1.00 ND1 A:HIS419 2.0 15.8 1.0 ND1 A:HIS497 2.0 15.6 1.0 SG A:CYS492 2.2 15.4 1.0 CE1 A:HIS419 2.9 15.9 1.0 CE1 A:HIS497 3.0 15.6 1.0 CG A:HIS497 3.0 15.5 1.0 CG A:HIS419 3.1 14.8 1.0 CB A:CYS492 3.3 12.1 1.0 SD A:MET502 3.3 16.9 1.0 CB A:HIS497 3.3 14.9 1.0 CB A:HIS419 3.5 13.8 1.0 CE A:MET502 3.8 14.0 1.0 CD1 A:ILE494 3.9 13.1 1.0 NE2 A:HIS419 4.1 16.2 1.0 CB A:ILE494 4.1 12.8 1.0 CA A:HIS419 4.1 14.5 1.0 NE2 A:HIS497 4.1 15.5 1.0 CD2 A:HIS497 4.1 13.0 1.0 CD2 A:HIS419 4.2 15.5 1.0 CG1 A:ILE494 4.4 13.5 1.0 CD1 A:LEU386 4.6 25.9 1.0 CD A:PRO420 4.6 14.3 1.0 CA A:CYS492 4.7 13.1 1.0 O A:HOH2394 4.7 24.6 1.0 CG A:MET502 4.8 13.8 1.0 CA A:HIS497 4.9 15.1 1.0 O A:THR418 4.9 16.4 1.0 CG2 A:ILE494 4.9 13.8 1.0 N A:ILE494 4.9 12.6 1.0

Copper binding site 2 out of 4 in the Mutations in the Neighbourhood of Cota-Laccase Trinuclear Site: D116A 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: D116A Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu1513 b:15.3 occ:1.00 ND1 A:HIS107 2.0 14.4 1.0 NE2 A:HIS153 2.0 13.5 1.0 NE2 A:HIS493 2.1 13.1 1.0 O2 A:PER1527 2.3 25.3 1.0 O1 A:PER1527 2.9 27.5 1.0 CE1 A:HIS107 2.9 14.0 1.0 CE1 A:HIS153 2.9 14.3 1.0 CE1 A:HIS493 3.0 12.0 1.0 CG A:HIS107 3.0 12.2 1.0 CD2 A:HIS153 3.1 12.7 1.0 CD2 A:HIS493 3.1 13.1 1.0 CB A:HIS107 3.4 11.0 1.0 CD2 A:HIS105 3.8 13.9 1.0 CZ2 A:TRP151 3.8 12.3 1.0 CU A:CU1515 4.0 17.1 1.0 NE2 A:HIS107 4.1 11.7 1.0 ND1 A:HIS153 4.1 13.4 1.0 ND1 A:HIS493 4.1 11.8 1.0 CE2 A:TRP151 4.1 11.6 1.0 CD2 A:HIS107 4.1 12.6 1.0 CG A:HIS153 4.2 11.2 1.0 NE1 A:TRP151 4.2 12.1 1.0 CG A:HIS493 4.2 11.8 1.0 O A:HOH2194 4.2 29.1 1.0 NE2 A:HIS105 4.3 16.1 1.0 CB A:ALA297 4.4 11.2 1.0 NE2 A:HIS422 4.5 13.6 1.0 CA A:HIS107 4.5 11.1 1.0 CD2 A:HIS422 4.6 13.6 1.0 CU A:CU1514 4.6 19.1 1.0 CH2 A:TRP151 4.6 12.5 1.0

Copper binding site 3 out of 4 in the Mutations in the Neighbourhood of Cota-Laccase Trinuclear Site: D116A 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: D116A Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu1514 b:19.1 occ:1.00 NE2 A:HIS424 2.0 15.6 1.0 NE2 A:HIS155 2.0 15.2 1.0 NE2 A:HIS491 2.0 14.7 1.0 O1 A:PER1527 2.1 27.5 1.0 O2 A:PER1527 2.3 25.3 1.0 CD2 A:HIS155 2.9 15.2 1.0 CE1 A:HIS424 3.0 15.6 1.0 CD2 A:HIS491 3.0 13.6 1.0 CD2 A:HIS424 3.0 10.8 1.0 CE1 A:HIS491 3.0 13.1 1.0 CE1 A:HIS155 3.1 15.7 1.0 CU A:CU1515 3.6 17.1 1.0 O A:HOH2194 3.7 29.1 1.0 NE2 A:HIS105 3.8 16.1 1.0 CD2 A:HIS422 3.8 13.6 1.0 CD2 A:HIS105 3.9 13.9 1.0 ND1 A:HIS491 4.1 13.2 1.0 CG A:HIS491 4.1 13.8 1.0 ND1 A:HIS424 4.1 12.4 1.0 CG A:HIS155 4.1 13.7 1.0 CG A:HIS424 4.1 13.5 1.0 ND1 A:HIS155 4.2 15.6 1.0 CG2 A:VAL489 4.2 14.5 0.3 NE2 A:HIS422 4.2 13.6 1.0 CE1 A:HIS105 4.4 13.3 1.0 CG A:HIS105 4.6 13.5 1.0 CU A:CU1513 4.6 15.3 1.0 OE2 A:GLU498 4.6 20.0 1.0 NE2 A:HIS493 4.8 13.1 1.0 ND1 A:HIS105 4.8 15.0 1.0 CD2 A:HIS493 4.8 13.1 1.0 CE1 A:HIS153 5.0 14.3 1.0

Copper binding site 4 out of 4 in the Mutations in the Neighbourhood of Cota-Laccase Trinuclear Site: D116A 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: D116A Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu1515 b:17.1 occ:1.00 NE2 A:HIS422 2.0 13.6 1.0 NE2 A:HIS105 2.0 16.1 1.0 O A:HOH2137 2.6 18.4 1.0 O2 A:PER1527 2.7 25.3 1.0 CE1 A:HIS105 2.9 13.3 1.0 CD2 A:HIS422 2.9 13.6 1.0 CE1 A:HIS422 3.0 14.0 1.0 CD2 A:HIS105 3.0 13.9 1.0 CD2 A:HIS424 3.1 10.8 1.0 NE2 A:HIS424 3.4 15.6 1.0 ND1 A:HIS107 3.4 14.4 1.0 CU A:CU1514 3.6 19.1 1.0 CG A:HIS107 3.7 12.2 1.0 CA A:HIS107 3.8 11.1 1.0 CG A:HIS424 3.8 13.5 1.0 CE1 A:HIS107 3.9 14.0 1.0 ND1 A:HIS105 4.0 15.0 1.0 CU A:CU1513 4.0 15.3 1.0 O1 A:PER1527 4.0 27.5 1.0 CG A:HIS422 4.1 13.8 1.0 ND1 A:HIS422 4.1 13.5 1.0 CB A:HIS107 4.1 11.0 1.0 CG A:HIS105 4.1 13.5 1.0 CE1 A:HIS424 4.1 15.6 1.0 CD2 A:HIS107 4.2 12.6 1.0 N A:GLY108 4.2 12.2 1.0 NE2 A:HIS107 4.3 11.7 1.0 ND1 A:HIS424 4.3 12.4 1.0 CA A:HIS424 4.4 14.3 1.0 O A:HOH2139 4.5 20.4 1.0 C A:HIS107 4.5 12.1 1.0 CB A:HIS424 4.6 14.5 1.0 O A:HOH2395 4.7 15.0 1.0 NE2 A:HIS491 4.8 14.7 1.0 N A:HIS107 4.8 10.5 1.0 N A:HIS424 4.9 14.9 1.0 O A:LEU423 4.9 14.6 1.0 O A:LEU106 4.9 10.5 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