Copper in PDB 6klj: Crystal Structure of the Zea Mays Laccase 3 Complexed with Coniferyl

All present enzymatic activity of Crystal Structure of the Zea Mays Laccase 3 Complexed with Coniferyl:
1.10.3.2;

The structure of Crystal Structure of the Zea Mays Laccase 3 Complexed with Coniferyl, PDB code: 6klj was solved by T.Xie, Z.C.Liu, G.G.Wang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.94 / 2.00
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	111.848, 111.848, 208.185, 90.00, 90.00, 120.00
R / Rfree (%)	16.4 / 20.5

The binding sites of Copper atom in the Crystal Structure of the Zea Mays Laccase 3 Complexed with Coniferyl (pdb code 6klj). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 4 binding sites of Copper where determined in the Crystal Structure of the Zea Mays Laccase 3 Complexed with Coniferyl, PDB code: 6klj:
Jump to Copper binding site number: 1; 2; 3; 4;

Copper binding site 1 out of 4 in the Crystal Structure of the Zea Mays Laccase 3 Complexed with Coniferyl


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 the Zea Mays Laccase 3 Complexed with Coniferyl within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu601 b:18.3 occ:1.00 ND1 A:HIS519 2.1 18.6 1.0 ND1 A:HIS451 2.1 17.4 1.0 SG A:CYS514 2.2 16.1 1.0 CE1 A:HIS519 3.0 20.9 1.0 CE1 A:HIS451 3.1 20.2 1.0 CG A:HIS451 3.1 17.9 1.0 CG A:HIS519 3.1 15.8 1.0 SD A:MET524 3.1 18.2 1.0 CB A:CYS514 3.2 15.6 1.0 CB A:HIS451 3.4 18.5 1.0 CB A:HIS519 3.5 15.7 1.0 CD2 A:PHE516 3.5 19.2 1.0 CE A:MET524 3.7 17.2 1.0 CA A:HIS451 4.0 19.9 1.0 NE2 A:HIS519 4.1 18.1 1.0 CB A:PHE516 4.1 17.2 1.0 NE2 A:HIS451 4.2 19.4 1.0 CD2 A:HIS519 4.2 19.4 1.0 CG A:PHE516 4.2 18.9 1.0 CD2 A:HIS451 4.2 19.6 1.0 CE2 A:PHE516 4.3 20.2 1.0 CD A:PRO452 4.6 17.4 1.0 CA A:CYS514 4.6 16.1 1.0 CG A:MET524 4.8 19.4 1.0 C A:HIS451 4.9 19.6 1.0 CA A:HIS519 5.0 17.6 1.0

Copper binding site 2 out of 4 in the Crystal Structure of the Zea Mays Laccase 3 Complexed with Coniferyl


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 the Zea Mays Laccase 3 Complexed with Coniferyl within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu602 b:20.6 occ:1.00 NE2 A:HIS454 1.9 17.4 1.0 NE2 A:HIS59 2.0 17.0 1.0 O A:HOH947 2.4 18.6 1.0 CD2 A:HIS454 2.9 15.3 1.0 CE1 A:HIS59 2.9 17.2 1.0 CE1 A:HIS454 3.0 16.3 1.0 O1 A:OXY616 3.0 28.4 1.0 CD2 A:HIS59 3.0 17.6 1.0 CD2 A:HIS456 3.3 13.9 1.0 NE2 A:HIS456 3.4 17.0 1.0 ND1 A:HIS61 3.5 18.3 1.0 CG A:HIS61 3.7 18.1 1.0 CG A:HIS456 3.8 17.2 1.0 CE1 A:HIS456 3.8 16.5 1.0 CA A:HIS61 3.8 18.9 1.0 CU A:CU603 3.8 22.6 1.0 CU A:CU604 3.9 22.8 1.0 ND1 A:HIS456 4.0 15.4 1.0 CE1 A:HIS61 4.0 15.4 1.0 N A:GLY62 4.0 18.6 1.0 CB A:HIS61 4.0 17.4 1.0 ND1 A:HIS454 4.0 15.3 1.0 ND1 A:HIS59 4.1 15.7 1.0 CG A:HIS454 4.1 18.2 1.0 CG A:HIS59 4.1 17.7 1.0 O2 A:OXY616 4.2 27.4 1.0 CD2 A:HIS61 4.4 16.7 1.0 C A:HIS61 4.5 16.6 1.0 NE2 A:HIS61 4.5 17.8 1.0 CA A:HIS456 4.5 17.9 1.0 O A:HOH904 4.6 18.4 1.0 CB A:HIS456 4.6 16.3 1.0 O A:HOH817 4.7 16.5 1.0 N A:HIS61 4.9 16.6 1.0 N A:HIS456 4.9 16.9 1.0

Copper binding site 3 out of 4 in the Crystal Structure of the Zea Mays Laccase 3 Complexed with Coniferyl


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 the Zea Mays Laccase 3 Complexed with Coniferyl within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu603 b:22.6 occ:1.00 NE2 A:HIS456 2.0 17.0 1.0 NE2 A:HIS513 2.1 18.6 1.0 O2 A:OXY616 2.1 27.4 1.0 O1 A:OXY616 2.1 28.4 1.0 NE2 A:HIS106 2.2 15.2 1.0 CE1 A:HIS456 2.9 16.5 1.0 CE1 A:HIS513 2.9 21.1 1.0 CD2 A:HIS106 3.0 16.6 1.0 CD2 A:HIS513 3.1 18.3 1.0 CD2 A:HIS456 3.1 13.9 1.0 CE1 A:HIS106 3.2 19.2 1.0 CD2 A:HIS454 3.7 15.3 1.0 CU A:CU602 3.8 20.6 1.0 ND1 A:HIS456 4.1 15.4 1.0 ND1 A:HIS513 4.1 19.2 1.0 CG A:HIS513 4.2 16.9 1.0 CG A:HIS456 4.2 17.2 1.0 CG A:HIS106 4.2 17.7 1.0 NE2 A:HIS454 4.2 17.4 1.0 O3 A:GOL615 4.2 23.3 1.0 ND1 A:HIS106 4.3 18.9 1.0 CD2 A:HIS59 4.3 17.6 1.0 NE2 A:HIS59 4.3 17.0 1.0 CD2 A:PHE511 4.3 16.7 1.0 CU A:CU604 4.4 22.8 1.0 C3 A:GOL615 4.4 29.8 1.0 CE1 A:HIS104 4.7 18.8 1.0 NE2 A:HIS515 4.8 18.8 1.0 CG A:HIS454 4.9 18.2 1.0 CD2 A:HIS515 5.0 17.9 1.0 CE1 A:HIS59 5.0 17.2 1.0 CG A:HIS59 5.0 17.7 1.0 CE2 A:PHE511 5.0 19.8 1.0

Copper binding site 4 out of 4 in the Crystal Structure of the Zea Mays Laccase 3 Complexed with Coniferyl


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 the Zea Mays Laccase 3 Complexed with Coniferyl within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu604 b:22.8 occ:1.00 ND1 A:HIS61 2.0 18.3 1.0 NE2 A:HIS515 2.1 18.8 1.0 NE2 A:HIS104 2.2 18.8 1.0 O1 A:OXY616 2.2 28.4 1.0 O2 A:OXY616 2.7 27.4 1.0 CE1 A:HIS61 2.9 15.4 1.0 CE1 A:HIS515 3.0 18.6 1.0 CG A:HIS61 3.1 18.1 1.0 CE1 A:HIS104 3.2 18.8 1.0 CD2 A:HIS104 3.2 18.2 1.0 CD2 A:HIS515 3.2 17.9 1.0 CB A:HIS61 3.5 17.4 1.0 CZ2 A:TRP102 3.8 16.0 1.0 CU A:CU602 3.9 20.6 1.0 NE2 A:HIS61 4.0 17.8 1.0 CD2 A:HIS59 4.0 17.6 1.0 CD2 A:HIS61 4.1 16.7 1.0 ND1 A:HIS515 4.2 17.9 1.0 CD2 A:HIS454 4.2 15.3 1.0 NE2 A:HIS454 4.2 17.4 1.0 ND1 A:HIS104 4.3 17.8 1.0 CG A:HIS515 4.3 19.2 1.0 CE2 A:TRP102 4.3 18.4 1.0 CG A:HIS104 4.3 15.5 1.0 CU A:CU603 4.4 22.6 1.0 NE2 A:HIS59 4.4 17.0 1.0 CH2 A:TRP102 4.5 16.6 1.0 NE1 A:TRP102 4.5 18.7 1.0 CA A:HIS61 4.6 18.9 1.0 O3 A:GOL615 4.7 23.3 1.0 CA A:GLY242 4.7 15.4 1.0

T.Xie, Z.C.Liu, G.G.Wang. Crystal Structure of Zea Mays Laccase 3 Complexed with Coniferyl at 2.0 Angstroms Resolution To Be Published.