Copper in PDB 9njj: F195L/I200F/M298L Streptomyces Coelicolor Laccase

The structure of F195L/I200F/M298L Streptomyces Coelicolor Laccase, PDB code: 9njj was solved by J.-X.Wang, Y.Lu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	79.53 / 2.64
Space group	P 43 3 2
Cell size a, b, c (Å), α, β, γ (°)	177.832, 177.832, 177.832, 90, 90, 90
R / Rfree (%)	18.6 / 20.8

The binding sites of Copper atom in the F195L/I200F/M298L Streptomyces Coelicolor Laccase (pdb code 9njj). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 4 binding sites of Copper where determined in the F195L/I200F/M298L Streptomyces Coelicolor Laccase, PDB code: 9njj:
Jump to Copper binding site number: 1; 2; 3; 4;

Copper binding site 1 out of 4 in the F195L/I200F/M298L Streptomyces Coelicolor Laccase


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of F195L/I200F/M298L Streptomyces Coelicolor Laccase within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu401 b:62.9 occ:1.00 ND1 A:HIS293 2.1 53.1 1.0 ND1 A:HIS231 2.1 63.0 1.0 SG A:CYS288 2.2 58.0 1.0 O A:HOH536 2.7 57.7 0.5 CG A:HIS231 3.0 48.2 1.0 CE1 A:HIS293 3.0 56.0 1.0 CG A:HIS293 3.1 54.5 1.0 CB A:HIS231 3.2 45.1 1.0 CB A:CYS288 3.2 42.7 1.0 CE1 A:HIS231 3.2 52.1 1.0 CB A:HIS293 3.4 44.4 1.0 CA A:HIS231 3.7 42.1 1.0 CD1 A:LEU298 3.9 53.5 1.0 O A:TYR230 4.0 51.9 1.0 NE2 A:HIS293 4.2 52.6 1.0 CD2 A:HIS231 4.2 52.6 1.0 CG2 A:VAL290 4.2 41.2 1.0 CD2 A:HIS293 4.2 60.8 1.0 NE2 A:HIS231 4.2 58.9 1.0 CB A:VAL290 4.3 48.7 1.0 CD2 A:LEU195 4.4 55.3 0.7 CA A:CYS288 4.6 45.7 1.0 N A:HIS231 4.6 46.1 1.0 N A:THR232 4.6 43.3 1.0 C A:TYR230 4.7 50.2 1.0 C A:HIS231 4.8 45.9 1.0 CA A:HIS293 4.9 50.4 1.0 O A:HOH502 4.9 53.0 0.4

Copper binding site 2 out of 4 in the F195L/I200F/M298L Streptomyces Coelicolor Laccase


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of F195L/I200F/M298L Streptomyces Coelicolor Laccase within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu402 b:56.7 occ:1.00 NE2 A:HIS289 2.1 51.4 1.0 O A:OH405 2.5 32.8 1.0 CE1 A:HIS289 3.0 43.3 1.0 CD2 A:HIS289 3.1 45.2 1.0 CU A:CU404 3.8 50.8 0.3 ND1 A:HIS289 4.1 48.5 1.0 NE2 A:HIS234 4.1 50.1 1.0 CG A:HIS289 4.2 50.5 1.0 CD2 A:HIS234 4.2 43.8 1.0 CE1 A:HIS234 4.9 43.2 1.0 CU A:CU403 4.9 58.9 1.0 CG A:HIS234 5.0 45.5 1.0

Copper binding site 3 out of 4 in the F195L/I200F/M298L Streptomyces Coelicolor Laccase


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of F195L/I200F/M298L Streptomyces Coelicolor Laccase within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu403 b:58.9 occ:1.00 NE2 A:HIS236 2.1 45.5 1.0 NE2 A:HIS287 2.2 53.0 1.0 O A:OH405 2.4 32.8 1.0 CE1 A:HIS236 2.8 41.0 1.0 CE1 A:HIS287 3.0 47.1 1.0 CD2 A:HIS236 3.2 45.1 1.0 CD2 A:HIS287 3.3 45.1 1.0 ND1 A:HIS236 4.0 40.5 1.0 CD2 A:HIS234 4.1 43.8 1.0 CU A:CU404 4.1 50.8 0.3 ND1 A:HIS287 4.2 48.6 1.0 CG A:HIS236 4.2 38.2 1.0 CG A:HIS287 4.3 44.4 1.0 SD A:MET285 4.5 73.3 1.0 NE2 A:HIS234 4.5 50.1 1.0 CG A:MET285 4.6 54.8 1.0 NE2 A:HIS289 4.8 51.4 1.0 CU A:CU402 4.9 56.7 1.0 CD2 A:HIS289 5.0 45.2 1.0

Copper binding site 4 out of 4 in the F195L/I200F/M298L Streptomyces Coelicolor Laccase


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 4 of F195L/I200F/M298L Streptomyces Coelicolor Laccase within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu404 b:50.8 occ:0.34 NE2 A:HIS234 1.9 50.1 1.0 CE1 A:HIS234 2.8 43.2 1.0 CD2 A:HIS234 2.9 43.8 1.0 O A:OH405 3.1 32.8 1.0 CD2 A:HIS236 3.3 45.1 1.0 NE2 A:HIS236 3.5 45.5 1.0 CU A:CU402 3.8 56.7 1.0 ND1 A:HIS234 3.9 44.0 1.0 CG A:HIS236 4.0 38.2 1.0 CG A:HIS234 4.0 45.5 1.0 CE1 A:HIS236 4.1 41.0 1.0 CU A:CU403 4.1 58.9 1.0 ND1 A:HIS236 4.4 40.5 1.0 CA A:HIS236 4.5 40.8 1.0 CB A:HIS236 4.8 44.5 1.0 OD2 A:ASP259 4.8 44.7 1.0 O A:MET235 4.9 45.1 1.0 N A:HIS236 4.9 45.4 1.0

J.X.Wang, A.C.Vilbert, L.H.Williams, E.N.Mirts, C.Cui, Y.Lu. Unexpected Effect of An Axial Ligand Mutation in the Type 1 Copper Center in Small Laccase: Structure-Based Analyses and Engineering to Increase Reduction Potential and Activity Chem Sci 2025.
ISSN: ESSN 2041-6539
DOI: 10.1039/D5SC02177D