Copper in PDB 3nsy: The Multi-Copper Oxidase Cueo with Six Met to Ser Mutations (M358S, M361S,M362S,M364S,M366S,M368S)

The structure of The Multi-Copper Oxidase Cueo with Six Met to Ser Mutations (M358S, M361S,M362S,M364S,M366S,M368S), PDB code: 3nsy was solved by S.A.Roberts, W.R.Montfort, S.K.Singh, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.00 / 2.10
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	50.052, 91.259, 53.979, 90.00, 102.34, 90.00
R / Rfree (%)	17 / 22.7

The binding sites of Copper atom in the The Multi-Copper Oxidase Cueo with Six Met to Ser Mutations (M358S, M361S,M362S,M364S,M366S,M368S) (pdb code 3nsy). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 6 binding sites of Copper where determined in the The Multi-Copper Oxidase Cueo with Six Met to Ser Mutations (M358S, M361S,M362S,M364S,M366S,M368S), PDB code: 3nsy:
Jump to Copper binding site number: 1; 2; 3; 4; 5; 6;

Copper binding site 1 out of 6 in the The Multi-Copper Oxidase Cueo with Six Met to Ser Mutations (M358S, M361S,M362S,M364S,M366S,M368S)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of The Multi-Copper Oxidase Cueo with Six Met to Ser Mutations (M358S, M361S,M362S,M364S,M366S,M368S) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu604 b:32.8 occ:1.00 ND1 A:HIS505 2.0 37.0 1.0 ND1 A:HIS443 2.1 33.6 1.0 SG A:CYS500 2.2 33.7 1.0 CE1 A:HIS505 3.0 37.2 1.0 CG A:HIS505 3.0 36.4 1.0 CE1 A:HIS443 3.1 34.6 1.0 CG A:HIS443 3.1 35.2 1.0 CB A:CYS500 3.3 32.9 1.0 CB A:HIS505 3.4 36.6 1.0 SD A:MET510 3.5 34.5 1.0 CB A:HIS443 3.5 35.7 1.0 CA A:HIS443 3.8 35.9 1.0 O A:LEU442 3.8 39.0 1.0 CB A:LEU502 4.1 30.8 1.0 NE2 A:HIS505 4.1 37.0 1.0 CD2 A:HIS505 4.1 36.5 1.0 NE2 A:HIS443 4.2 34.6 1.0 CE A:MET510 4.2 35.2 1.0 CD2 A:HIS443 4.3 34.6 1.0 N A:HIS443 4.5 36.7 1.0 C A:LEU442 4.5 38.5 1.0 CD1 A:LEU502 4.5 32.7 1.0 CA A:CYS500 4.7 32.6 1.0 CG A:LEU502 4.8 31.8 1.0 CA A:HIS505 4.9 36.4 1.0 CG A:MET510 5.0 35.3 1.0 O A:LEU502 5.0 29.0 1.0 C A:HIS443 5.0 35.0 1.0

Copper binding site 2 out of 6 in the The Multi-Copper Oxidase Cueo with Six Met to Ser Mutations (M358S, M361S,M362S,M364S,M366S,M368S)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of The Multi-Copper Oxidase Cueo with Six Met to Ser Mutations (M358S, M361S,M362S,M364S,M366S,M368S) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu601 b:45.7 occ:0.50 NE2 A:HIS446 1.9 38.2 1.0 NE2 A:HIS101 1.9 34.6 1.0 CE1 A:HIS101 2.8 35.3 1.0 CD2 A:HIS446 2.8 35.8 1.0 O A:HOH17 2.9 43.4 1.0 CE1 A:HIS446 3.0 37.5 1.0 O1 A:C2O602 3.0 35.5 1.0 NE2 A:HIS448 3.0 35.4 1.0 CD2 A:HIS448 3.0 34.8 1.0 CD2 A:HIS101 3.0 35.4 1.0 CU2 A:C2O602 3.3 39.7 1.0 ND1 A:HIS103 3.6 30.5 1.0 CG A:HIS103 3.6 31.9 1.0 CE1 A:HIS448 3.6 37.3 1.0 CA A:HIS103 3.7 33.2 1.0 CG A:HIS448 3.7 36.4 1.0 CB A:HIS103 3.8 33.0 1.0 CU3 A:C2O602 3.9 27.9 1.0 ND1 A:HIS101 3.9 34.5 1.0 CG A:HIS446 3.9 35.3 1.0 ND1 A:HIS448 4.0 36.4 1.0 ND1 A:HIS446 4.0 37.3 1.0 CG A:HIS101 4.1 34.8 1.0 CE1 A:HIS103 4.2 31.9 1.0 CD2 A:HIS103 4.2 32.6 1.0 N A:GLY104 4.4 34.5 1.0 NE2 A:HIS103 4.5 32.2 1.0 C A:HIS103 4.6 33.6 1.0 CA A:HIS448 4.6 36.1 1.0 N A:HIS103 4.6 33.1 1.0 CB A:HIS448 4.6 36.2 1.0 O A:HOH565 4.8 37.3 1.0 O A:HOH9 4.8 42.0 1.0 NE2 A:HIS499 4.9 34.8 1.0 NE2 A:HIS143 4.9 40.8 1.0 O A:TRP102 4.9 33.2 1.0

Copper binding site 3 out of 6 in the The Multi-Copper Oxidase Cueo with Six Met to Ser Mutations (M358S, M361S,M362S,M364S,M366S,M368S)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of The Multi-Copper Oxidase Cueo with Six Met to Ser Mutations (M358S, M361S,M362S,M364S,M366S,M368S) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu602 b:39.7 occ:1.00 CU2 A:C2O602 0.0 39.7 1.0 O1 A:C2O602 1.9 35.5 1.0 NE2 A:HIS499 2.0 34.8 1.0 NE2 A:HIS448 2.1 35.4 1.0 NE2 A:HIS143 2.2 40.8 1.0 CE1 A:HIS499 2.9 34.2 1.0 CE1 A:HIS448 3.0 37.3 1.0 CD2 A:HIS499 3.1 33.6 1.0 CD2 A:HIS143 3.1 40.6 1.0 CD2 A:HIS448 3.1 34.8 1.0 CE1 A:HIS143 3.2 39.0 1.0 CD2 A:HIS446 3.2 35.8 1.0 CU A:CU601 3.3 45.7 0.5 CU3 A:C2O602 3.7 27.9 1.0 NE2 A:HIS446 3.8 38.2 1.0 NE2 A:HIS101 3.8 34.6 1.0 CD2 A:HIS101 4.0 35.4 1.0 ND1 A:HIS499 4.1 35.8 1.0 CG A:HIS499 4.2 34.5 1.0 ND1 A:HIS448 4.2 36.4 1.0 CG A:HIS448 4.2 36.4 1.0 CG A:HIS143 4.3 39.4 1.0 ND1 A:HIS143 4.3 40.1 1.0 CG A:HIS446 4.4 35.3 1.0 CD2 A:HIS501 4.5 31.8 1.0 CE1 A:HIS141 4.6 31.8 1.0 NE2 A:HIS501 4.6 30.9 1.0 CE1 A:HIS101 4.6 35.3 1.0 NE2 A:HIS141 4.8 31.1 1.0 CG A:HIS101 4.8 34.8 1.0 CB A:MET497 4.9 38.9 1.0 ND1 A:HIS103 4.9 30.5 1.0

Copper binding site 4 out of 6 in the The Multi-Copper Oxidase Cueo with Six Met to Ser Mutations (M358S, M361S,M362S,M364S,M366S,M368S)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 4 of The Multi-Copper Oxidase Cueo with Six Met to Ser Mutations (M358S, M361S,M362S,M364S,M366S,M368S) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu602 b:27.9 occ:1.00 CU3 A:C2O602 0.0 27.9 1.0 O1 A:C2O602 1.9 35.5 1.0 NE2 A:HIS141 2.0 31.1 1.0 ND1 A:HIS103 2.1 30.5 1.0 NE2 A:HIS501 2.2 30.9 1.0 CE1 A:HIS141 2.8 31.8 1.0 CE1 A:HIS103 3.0 31.9 1.0 CD2 A:HIS501 3.1 31.8 1.0 CD2 A:HIS141 3.2 29.1 1.0 CG A:HIS103 3.2 31.9 1.0 CE1 A:HIS501 3.2 31.8 1.0 CB A:HIS103 3.6 33.0 1.0 CU2 A:C2O602 3.7 39.7 1.0 CU A:CU601 3.9 45.7 0.5 CZ2 A:TRP139 4.0 29.7 1.0 ND1 A:HIS141 4.0 30.5 1.0 CD2 A:HIS101 4.0 35.4 1.0 CD2 A:HIS446 4.1 35.8 1.0 NE2 A:HIS103 4.1 32.2 1.0 NE2 A:HIS446 4.2 38.2 1.0 CG A:HIS141 4.2 30.3 1.0 CG A:HIS501 4.3 31.7 1.0 CD2 A:HIS103 4.3 32.6 1.0 NE2 A:HIS101 4.3 34.6 1.0 ND1 A:HIS501 4.3 30.2 1.0 CE2 A:TRP139 4.4 28.2 1.0 NE1 A:TRP139 4.5 30.9 1.0 CH2 A:TRP139 4.7 29.8 1.0 CA A:HIS103 4.8 33.2 1.0 CE1 A:HIS499 4.8 34.2 1.0 NE2 A:HIS499 4.9 34.8 1.0 CG A:HIS446 4.9 35.3 1.0 NE2 A:HIS143 4.9 40.8 1.0

Copper binding site 5 out of 6 in the The Multi-Copper Oxidase Cueo with Six Met to Ser Mutations (M358S, M361S,M362S,M364S,M366S,M368S)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 5 of The Multi-Copper Oxidase Cueo with Six Met to Ser Mutations (M358S, M361S,M362S,M364S,M366S,M368S) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu605 b:32.4 occ:0.50 OD1 A:ASP360 2.0 49.8 1.0 OD2 A:ASP439 2.1 47.2 1.0 SD A:MET441 2.2 45.7 1.0 SD A:MET355 2.3 47.3 1.0 CE A:MET355 2.9 43.9 1.0 CG A:ASP360 2.9 49.5 1.0 CE A:MET441 2.9 43.9 1.0 CG A:ASP439 3.0 44.9 1.0 OD1 A:ASP439 3.1 45.4 1.0 OD2 A:ASP360 3.2 52.5 1.0 CG A:MET441 3.2 43.1 1.0 CG A:MET355 3.4 43.2 1.0 CB A:MET441 3.7 42.6 1.0 CB A:MET355 3.7 41.8 1.0 O A:HOH733 3.8 38.7 1.0 N A:MET441 4.2 43.4 1.0 CB A:ASP360 4.3 48.4 1.0 CB A:ASP439 4.4 43.7 1.0 O A:HOH696 4.5 54.1 1.0 CA A:MET441 4.6 42.5 1.0 N A:MET440 4.6 45.0 1.0 CA A:ASP360 4.8 48.0 1.0 CA A:ASP439 4.9 43.6 1.0

Copper binding site 6 out of 6 in the The Multi-Copper Oxidase Cueo with Six Met to Ser Mutations (M358S, M361S,M362S,M364S,M366S,M368S)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 6 of The Multi-Copper Oxidase Cueo with Six Met to Ser Mutations (M358S, M361S,M362S,M364S,M366S,M368S) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu606 b:45.3 occ:0.50 ND1 A:HIS488 2.1 48.1 1.0 O A:HOH813 2.2 46.6 1.0 O A:HOH804 2.3 65.5 1.0 CG A:HIS488 3.0 47.7 1.0 CE1 A:HIS488 3.1 49.4 1.0 CB A:HIS488 3.2 47.4 1.0 CA A:HIS488 3.7 47.4 1.0 O A:ASN487 4.0 46.5 1.0 CG A:PRO108 4.1 41.5 1.0 CD2 A:HIS488 4.2 47.8 1.0 NE2 A:HIS488 4.2 47.9 1.0 N A:HIS488 4.5 46.9 1.0 C A:ASN487 4.6 46.4 1.0 CD A:PRO108 4.6 40.5 1.0 N A:ASP489 4.7 48.6 1.0 C A:HIS488 4.8 48.0 1.0 O A:HOH591 4.9 45.8 1.0

S.K.Singh, S.A.Roberts, S.F.Mcdevitt, A.Weichsel, G.F.Wildner, G.B.Grass, C.Rensing, W.R.Montfort. Crystal Structures of Multicopper Oxidase Cueo Bound to Copper(I) and Silver(I): Functional Role of A Methionine-Rich Sequence. J. Biol. Chem. V. 286 37849 2011.
ISSN: ESSN 1083-351X
PubMed: 21903583
DOI: 10.1074/JBC.M111.293589