Copper in PDB 4akp: Mutations in the Neighbourhood of Cota-Laccase Trinuclear Site:E498T Mutant

All present enzymatic activity of Mutations in the Neighbourhood of Cota-Laccase Trinuclear Site:E498T Mutant:
1.10.3.2;

The structure of Mutations in the Neighbourhood of Cota-Laccase Trinuclear Site:E498T Mutant, PDB code: 4akp was solved by C.S.Silva, Z.Chen, P.Durao, M.M.Pereira, S.Todorovic, P.Hildebrandt, L.O.Martins, P.F.Lindley, I.Bento, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	44.11 / 2.00
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	101.898, 101.898, 136.931, 90.00, 90.00, 120.00
R / Rfree (%)	17.671 / 21.497

The binding sites of Copper atom in the Mutations in the Neighbourhood of Cota-Laccase Trinuclear Site:E498T Mutant (pdb code 4akp). 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:E498T Mutant, PDB code: 4akp:
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:E498T 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:E498T Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu1512 b:22.2 occ:1.00 ND1 A:HIS497 2.0 20.4 1.0 ND1 A:HIS419 2.0 22.6 1.0 SG A:CYS492 2.3 20.4 1.0 CE1 A:HIS419 2.8 22.2 1.0 CE1 A:HIS497 3.0 21.7 1.0 CG A:HIS497 3.0 20.3 1.0 CG A:HIS419 3.1 22.4 1.0 CB A:CYS492 3.2 18.8 1.0 SD A:MET502 3.3 21.4 1.0 CB A:HIS497 3.3 20.5 1.0 CB A:HIS419 3.6 22.3 1.0 CE A:MET502 4.0 21.4 1.0 CD1 A:ILE494 4.0 19.1 1.0 NE2 A:HIS419 4.0 22.7 1.0 NE2 A:HIS497 4.1 20.2 1.0 CB A:ILE494 4.1 19.2 1.0 CD2 A:HIS497 4.1 19.4 1.0 CD2 A:HIS419 4.2 23.4 1.0 CA A:HIS419 4.2 21.9 1.0 CD2 A:LEU386 4.5 31.8 1.0 CG1 A:ILE494 4.5 18.9 1.0 O A:HOH2417 4.6 28.6 1.0 CA A:CYS492 4.7 18.8 1.0 CG A:MET502 4.8 20.0 1.0 CD A:PRO420 4.8 19.9 1.0 CA A:HIS497 4.9 20.5 1.0 CG2 A:ILE494 4.9 18.5 1.0 O A:THR418 4.9 24.2 1.0 N A:ILE494 5.0 18.8 1.0 O A:ILE494 5.0 19.6 1.0

Copper binding site 2 out of 4 in the Mutations in the Neighbourhood of Cota-Laccase Trinuclear Site:E498T 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:E498T Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu1513 b:21.0 occ:0.80 ND1 A:HIS107 2.0 21.2 1.0 NE2 A:HIS493 2.0 19.6 1.0 NE2 A:HIS153 2.0 18.2 1.0 O2 A:OXY1516 2.1 9.2 0.8 O1 A:OXY1516 2.2 15.0 0.8 CE1 A:HIS107 2.9 20.9 1.0 CE1 A:HIS153 2.9 17.4 1.0 CE1 A:HIS493 3.0 19.1 1.0 CD2 A:HIS493 3.0 18.5 1.0 CG A:HIS107 3.1 18.5 1.0 CD2 A:HIS153 3.1 15.0 1.0 CU A:CU1515 3.6 18.6 0.8 CB A:HIS107 3.6 16.7 1.0 CD2 A:HIS105 3.8 15.4 1.0 NE2 A:HIS107 4.0 20.7 1.0 ND1 A:HIS153 4.0 16.6 1.0 CZ2 A:TRP151 4.1 15.9 1.0 CU A:CU1514 4.1 18.8 0.8 ND1 A:HIS493 4.1 18.9 1.0 CG A:HIS493 4.2 18.3 1.0 CD2 A:HIS107 4.2 20.8 1.0 CG A:HIS153 4.2 15.7 1.0 CD2 A:HIS422 4.3 17.2 1.0 NE2 A:HIS105 4.3 14.8 1.0 NE2 A:HIS422 4.4 17.4 1.0 CE2 A:TRP151 4.4 16.4 1.0 NE1 A:TRP151 4.5 16.5 1.0 CB A:ALA297 4.7 16.2 1.0 CA A:HIS107 4.7 16.3 1.0 CH2 A:TRP151 4.8 16.0 1.0 CE1 A:HIS491 4.8 19.0 1.0 CD2 A:HIS155 4.9 19.0 1.0 NE2 A:HIS155 5.0 19.4 1.0

Copper binding site 3 out of 4 in the Mutations in the Neighbourhood of Cota-Laccase Trinuclear Site:E498T 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:E498T Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu1514 b:18.8 occ:0.80 NE2 A:HIS424 2.0 19.2 1.0 NE2 A:HIS491 2.0 19.9 1.0 NE2 A:HIS155 2.0 19.4 1.0 O2 A:OXY1516 2.1 9.2 0.8 O1 A:OXY1516 2.2 15.0 0.8 CE1 A:HIS424 2.9 18.0 1.0 CE1 A:HIS491 2.9 19.0 1.0 CD2 A:HIS155 3.0 19.0 1.0 CE1 A:HIS155 3.1 20.6 1.0 CD2 A:HIS491 3.1 19.3 1.0 CD2 A:HIS424 3.1 17.2 1.0 CU A:CU1515 3.5 18.6 0.8 CD2 A:HIS422 3.7 17.2 1.0 CD2 A:HIS105 3.9 15.4 1.0 NE2 A:HIS105 4.0 14.8 1.0 ND1 A:HIS491 4.0 18.8 1.0 ND1 A:HIS424 4.0 16.1 1.0 CU A:CU1513 4.1 21.0 0.8 CG A:HIS155 4.1 18.1 1.0 ND1 A:HIS155 4.1 20.0 1.0 CG A:HIS491 4.2 18.6 1.0 CG A:HIS424 4.2 16.8 1.0 NE2 A:HIS422 4.2 17.4 1.0 CG2 A:VAL489 4.2 17.1 0.5 NE2 A:HIS493 4.6 19.6 1.0 CG A:HIS105 4.6 14.6 1.0 CD2 A:HIS493 4.7 18.5 1.0 CE1 A:HIS105 4.7 14.3 1.0 CE1 A:HIS153 4.8 17.4 1.0 O A:HOH2162 4.8 33.8 1.0 CG A:HIS422 4.9 17.4 1.0

Copper binding site 4 out of 4 in the Mutations in the Neighbourhood of Cota-Laccase Trinuclear Site:E498T 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:E498T Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu1515 b:18.6 occ:0.80 NE2 A:HIS422 2.0 17.4 1.0 NE2 A:HIS105 2.0 14.8 1.0 O1 A:OXY1516 2.1 15.0 0.8 CD2 A:HIS422 2.8 17.2 1.0 CD2 A:HIS105 2.9 15.4 1.0 CE1 A:HIS105 3.0 14.3 1.0 CE1 A:HIS422 3.1 17.4 1.0 O2 A:OXY1516 3.2 9.2 0.8 ND1 A:HIS107 3.2 21.2 1.0 O A:HOH2142 3.2 18.5 1.0 NE2 A:HIS424 3.2 19.2 1.0 CD2 A:HIS424 3.3 17.2 1.0 CU A:CU1514 3.5 18.8 0.8 CG A:HIS107 3.5 18.5 1.0 CU A:CU1513 3.6 21.0 0.8 CE1 A:HIS107 3.6 20.9 1.0 CE1 A:HIS424 3.8 18.0 1.0 CA A:HIS107 3.8 16.3 1.0 CG A:HIS424 3.9 16.8 1.0 CB A:HIS107 3.9 16.7 1.0 CG A:HIS422 4.0 17.4 1.0 CG A:HIS105 4.0 14.6 1.0 CD2 A:HIS107 4.1 20.8 1.0 ND1 A:HIS105 4.1 14.7 1.0 ND1 A:HIS422 4.1 17.0 1.0 NE2 A:HIS107 4.1 20.7 1.0 ND1 A:HIS424 4.1 16.1 1.0 N A:GLY108 4.3 16.3 1.0 C A:HIS107 4.6 16.6 1.0 CA A:HIS424 4.7 17.7 1.0 N A:HIS107 4.8 15.9 1.0 NE2 A:HIS491 4.8 19.9 1.0 CB A:HIS424 4.8 17.4 1.0 NE2 A:HIS153 4.9 18.2 1.0 O A:HOH2145 5.0 17.2 1.0 NE2 A:HIS493 5.0 19.6 1.0 NE2 A:HIS155 5.0 19.4 1.0 O A:HOH2418 5.0 17.7 1.0

Z.Chen, P.Durao, C.S.Silva, M.M.Pereira, S.Todorovic, P.Hildebrandt, I.Bento, P.F.Lindley, L.O.Martins. The Role of GLU498 in the Dioxygen Reactivity of Cota-Laccase From Bacillus Subtilis. Dalton Trans V. 39 2875 2010.
ISSN: ISSN 1477-9226
PubMed: 20200715
DOI: 10.1039/B922734B