Copper in PDB 6syy: Crystal Structure of Mcoa Multicopper Oxidase From the Hyperthermophile Aquifex Aeolicus

The structure of Crystal Structure of Mcoa Multicopper Oxidase From the Hyperthermophile Aquifex Aeolicus, PDB code: 6syy was solved by P.T.Borges, V.Brissos, T.N.Cordeiro, L.O.Martins, C.Frazao, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.66 / 1.79
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	52.920, 98.927, 98.589, 90.00, 90.00, 90.00
R / Rfree (%)	19.2 / 19.2

The binding sites of Copper atom in the Crystal Structure of Mcoa Multicopper Oxidase From the Hyperthermophile Aquifex Aeolicus (pdb code 6syy). 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 Mcoa Multicopper Oxidase From the Hyperthermophile Aquifex Aeolicus, PDB code: 6syy:
Jump to Copper binding site number: 1; 2; 3; 4;

Copper binding site 1 out of 4 in the Crystal Structure of Mcoa Multicopper Oxidase From the Hyperthermophile Aquifex Aeolicus


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 Mcoa Multicopper Oxidase From the Hyperthermophile Aquifex Aeolicus within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu701 b:24.3 occ:0.65 ND1 A:HIS514 2.0 22.1 1.0 SG A:CYS509 2.0 31.2 1.0 ND1 A:HIS451 2.2 30.6 1.0 CE A:MET519 2.6 36.6 0.4 CE1 A:HIS514 3.0 30.4 1.0 CB A:CYS509 3.0 35.8 1.0 CG A:HIS514 3.0 27.6 1.0 CE1 A:HIS451 3.1 30.3 1.0 CG A:HIS451 3.2 26.3 1.0 SD A:MET519 3.2 24.9 0.6 CB A:HIS514 3.3 22.3 1.0 CB A:HIS451 3.5 29.1 1.0 SD A:MET519 3.8 47.8 0.4 CE A:MET519 3.9 21.6 0.6 CA A:HIS451 4.0 23.6 1.0 CD1 A:ILE511 4.0 21.9 1.0 NE2 A:HIS514 4.1 23.6 1.0 CB A:ILE511 4.1 26.2 1.0 CD2 A:HIS514 4.1 23.2 1.0 NE2 A:HIS451 4.2 33.9 1.0 CD2 A:HIS451 4.3 34.1 1.0 O A:TYR450 4.3 28.4 1.0 CG1 A:ILE511 4.4 21.6 1.0 CA A:CYS509 4.4 25.0 1.0 CG A:MET519 4.6 27.7 0.6 CD A:PRO452 4.7 38.6 1.0 N A:ILE511 4.8 24.0 1.0 CA A:HIS514 4.8 32.7 1.0 CG2 A:ILE511 4.9 22.0 1.0 C A:HIS451 4.9 25.9 1.0 N A:HIS451 5.0 26.4 1.0 CD2 A:PHE407 5.0 29.6 1.0 C A:CYS509 5.0 31.1 1.0

Copper binding site 2 out of 4 in the Crystal Structure of Mcoa Multicopper Oxidase From the Hyperthermophile Aquifex Aeolicus


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 Mcoa Multicopper Oxidase From the Hyperthermophile Aquifex Aeolicus within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu702 b:34.8 occ:0.60 NE2 A:HIS161 2.0 53.4 1.0 NE2 A:HIS456 2.1 34.1 1.0 O A:O705 2.1 29.0 0.6 NE2 A:HIS508 2.2 40.1 1.0 CE1 A:HIS456 2.7 41.9 1.0 CD2 A:HIS161 2.9 35.4 1.0 CU A:CU703 2.9 42.6 0.4 CE1 A:HIS508 3.0 49.1 1.0 CE1 A:HIS161 3.1 59.8 1.0 CD2 A:HIS508 3.2 34.8 1.0 CD2 A:HIS456 3.3 50.3 1.0 CD2 A:HIS118 3.7 37.8 1.0 CD2 A:HIS454 3.7 35.0 1.0 NE2 A:HIS118 3.8 68.6 1.0 ND1 A:HIS456 3.9 39.2 1.0 CG A:HIS161 4.1 35.0 1.0 ND1 A:HIS508 4.1 30.0 1.0 ND1 A:HIS161 4.1 40.4 1.0 NE2 A:HIS454 4.2 29.1 1.0 CG A:HIS508 4.2 34.1 1.0 CG A:HIS456 4.2 42.5 1.0 CG A:HIS118 4.4 57.3 1.0 CD1 A:LEU506 4.5 39.5 1.0 CU A:CU704 4.5 38.8 0.6 CE1 A:HIS118 4.6 55.1 1.0 CE1 A:HIS159 4.8 31.7 1.0 ND1 A:HIS118 4.9 43.7 1.0 CG A:HIS454 4.9 30.1 1.0

Copper binding site 3 out of 4 in the Crystal Structure of Mcoa Multicopper Oxidase From the Hyperthermophile Aquifex Aeolicus


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 Mcoa Multicopper Oxidase From the Hyperthermophile Aquifex Aeolicus within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu703 b:42.6 occ:0.39 NE2 A:HIS454 2.1 29.1 1.0 NE2 A:HIS118 2.2 68.6 1.0 O A:O705 2.5 29.0 0.6 CD2 A:HIS454 2.6 35.0 1.0 CD2 A:HIS118 2.7 37.8 1.0 NE2 A:HIS456 2.9 34.1 1.0 CU A:CU702 2.9 34.8 0.6 ND1 A:HIS120 3.2 35.5 1.0 CD2 A:HIS456 3.3 50.3 1.0 CE1 A:HIS454 3.3 34.1 1.0 CG A:HIS120 3.3 34.8 1.0 CE1 A:HIS118 3.4 55.1 1.0 CU A:CU704 3.6 38.8 0.6 CE1 A:HIS456 3.6 41.9 1.0 CE1 A:HIS120 3.6 48.5 1.0 O A:HOH921 3.7 45.0 1.0 CG A:HIS454 3.8 30.1 1.0 CD2 A:HIS120 3.8 37.9 1.0 CB A:HIS120 3.8 26.8 1.0 CA A:HIS120 3.9 29.3 1.0 NE2 A:HIS120 3.9 33.4 1.0 CG A:HIS118 3.9 57.3 1.0 ND1 A:HIS454 4.1 35.0 1.0 CG A:HIS456 4.1 42.5 1.0 NE2 A:HIS508 4.2 40.1 1.0 ND1 A:HIS456 4.3 39.2 1.0 ND1 A:HIS118 4.3 43.7 1.0 NE2 A:HIS159 4.6 48.3 1.0 NE2 A:HIS161 4.6 53.4 1.0 N A:GLY121 4.7 33.5 1.0 CD2 A:HIS161 4.8 35.4 1.0 C A:HIS120 4.8 42.8 1.0 CE1 A:HIS508 4.9 49.1 1.0 CD2 A:HIS510 4.9 31.2 1.0 N A:HIS120 4.9 30.0 1.0 NE2 A:HIS510 5.0 35.6 1.0

Copper binding site 4 out of 4 in the Crystal Structure of Mcoa Multicopper Oxidase From the Hyperthermophile Aquifex Aeolicus


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 Mcoa Multicopper Oxidase From the Hyperthermophile Aquifex Aeolicus within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu704 b:38.8 occ:0.60 NE2 A:HIS159 1.8 48.3 1.0 ND1 A:HIS120 2.0 35.5 1.0 NE2 A:HIS510 2.3 35.6 1.0 O A:O705 2.4 29.0 0.6 CE1 A:HIS159 2.8 31.7 1.0 CE1 A:HIS120 2.8 48.5 1.0 CD2 A:HIS159 2.8 41.5 1.0 CG A:HIS120 3.1 34.8 1.0 CD2 A:HIS510 3.2 31.2 1.0 CE1 A:HIS510 3.3 34.8 1.0 CB A:HIS120 3.5 26.8 1.0 CU A:CU703 3.6 42.6 0.4 ND1 A:HIS159 3.9 37.1 1.0 CG A:HIS159 3.9 30.3 1.0 NE2 A:HIS120 4.0 33.4 1.0 CD2 A:HIS118 4.1 37.8 1.0 CD2 A:HIS120 4.1 37.9 1.0 CD2 A:PHE157 4.2 36.2 1.0 CE2 A:PHE157 4.2 28.3 1.0 CG A:HIS510 4.4 40.5 1.0 ND1 A:HIS510 4.4 30.4 1.0 CU A:CU702 4.5 34.8 0.6 NE2 A:HIS118 4.8 68.6 1.0 CD2 A:HIS454 4.8 35.0 1.0 CA A:HIS120 4.8 29.3 1.0 NE2 A:HIS454 4.9 29.1 1.0

P.T.Borges, V.Brissos, T.N.Cordeiro, L.O.Martins, C.Frazao. The Methionine-Rich Loop of Multicopper Oxidase Mcoa Follows Open-to-Close Transitions with A Role in Enzyme Catalysis Acs Catalysis 2020.
ISSN: ESSN 2155-5435
DOI: 10.1021/ACSCATAL.0C01623