Copper in PDB 8z59: The X-Ray Crystal Structure of Multicopper Oxidase From Sulfurimonas Sp.

The structure of The X-Ray Crystal Structure of Multicopper Oxidase From Sulfurimonas Sp., PDB code: 8z59 was solved by Y.Wang, H.Qian, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.52 / 2.58
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	86.636, 103.389, 131.906, 104.86, 103.96, 98.35
R / Rfree (%)	19.1 / 24

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 20; Page 3, Binding sites: 21 - 30; Page 4, Binding sites: 31 - 32;

Binding sites:

The binding sites of Copper atom in the The X-Ray Crystal Structure of Multicopper Oxidase From Sulfurimonas Sp. (pdb code 8z59). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 32 binding sites of Copper where determined in the The X-Ray Crystal Structure of Multicopper Oxidase From Sulfurimonas Sp., PDB code: 8z59:
Jump to Copper binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Copper binding site 1 out of 32 in the The X-Ray Crystal Structure of Multicopper Oxidase From Sulfurimonas Sp.


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of The X-Ray Crystal Structure of Multicopper Oxidase From Sulfurimonas Sp. within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu601 b:51.1 occ:0.64 NE2 A:HIS429 2.0 39.4 1.0 NE2 A:HIS477 2.0 39.8 1.0 NE2 A:HIS166 2.2 39.3 1.0 CE1 A:HIS477 2.6 38.0 1.0 CE1 A:HIS429 2.8 37.7 1.0 CD2 A:HIS166 3.0 38.1 1.0 CD2 A:HIS429 3.1 38.6 1.0 CE1 A:HIS166 3.3 42.1 1.0 CD2 A:HIS477 3.3 39.1 1.0 CU A:CU603 3.7 39.0 0.5 CD2 A:HIS427 3.8 32.2 1.0 ND1 A:HIS477 3.9 39.8 1.0 ND1 A:HIS429 4.0 39.3 1.0 CG2 A:VAL475 4.1 35.7 1.0 CG A:HIS166 4.2 34.6 1.0 CG A:HIS477 4.2 39.9 1.0 CG A:HIS429 4.2 38.2 1.0 NE2 A:HIS427 4.2 37.5 1.0 ND1 A:HIS166 4.3 39.8 1.0 NE2 A:HIS479 4.4 36.9 1.0 CD2 A:HIS479 4.4 38.7 1.0 CD2 A:HIS124 4.4 28.9 1.0 NE2 A:HIS124 4.5 33.2 1.0 CU A:CU602 4.5 32.7 0.6 OE2 A:GLU484 4.5 53.9 1.0 CG A:HIS124 4.8 28.7 1.0 CE1 A:HIS164 4.8 32.6 1.0 CE1 A:HIS124 4.9 29.9 1.0

Copper binding site 2 out of 32 in the The X-Ray Crystal Structure of Multicopper Oxidase From Sulfurimonas Sp.


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of The X-Ray Crystal Structure of Multicopper Oxidase From Sulfurimonas Sp. within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu602 b:32.7 occ:0.58 ND1 A:HIS126 1.8 31.0 1.0 NE2 A:HIS164 2.0 27.9 1.0 NE2 A:HIS479 2.2 36.9 1.0 CE1 A:HIS126 2.7 36.8 1.0 CE1 A:HIS164 2.9 32.6 1.0 CG A:HIS126 3.0 33.6 1.0 CE1 A:HIS479 3.0 33.8 1.0 CD2 A:HIS164 3.1 28.5 1.0 CD2 A:HIS479 3.2 38.7 1.0 CB A:HIS126 3.5 27.8 1.0 CZ2 A:TRP162 3.5 30.7 1.0 NE2 A:HIS126 3.8 35.4 1.0 CU A:CU603 4.0 39.0 0.5 CE2 A:TRP162 4.0 29.7 1.0 CD2 A:HIS126 4.0 33.6 1.0 ND1 A:HIS164 4.0 27.4 1.0 CD2 A:HIS124 4.1 28.9 1.0 ND1 A:HIS479 4.1 38.4 1.0 CH2 A:TRP162 4.2 30.4 1.0 CG A:HIS164 4.2 26.5 1.0 NE1 A:TRP162 4.2 28.9 1.0 CG A:HIS479 4.3 40.9 1.0 CU A:CU601 4.5 51.1 0.6 CB A:ALA298 4.6 28.0 1.0 NE2 A:HIS124 4.6 33.2 1.0 NE2 A:HIS427 4.6 37.5 1.0 CD2 A:HIS427 4.6 32.2 1.0 CA A:HIS126 4.7 30.4 1.0 CD2 A:TRP162 4.9 28.6 1.0

Copper binding site 3 out of 32 in the The X-Ray Crystal Structure of Multicopper Oxidase From Sulfurimonas Sp.


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of The X-Ray Crystal Structure of Multicopper Oxidase From Sulfurimonas Sp. within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu603 b:39.0 occ:0.48 NE2 A:HIS427 1.8 37.5 1.0 NE2 A:HIS124 2.1 33.2 1.0 CD2 A:HIS427 2.7 32.2 1.0 CE1 A:HIS427 2.8 36.4 1.0 CD2 A:HIS429 2.9 38.6 1.0 CD2 A:HIS124 2.9 28.9 1.0 CE1 A:HIS124 2.9 29.9 1.0 NE2 A:HIS429 3.0 39.4 1.0 ND1 A:HIS126 3.2 31.0 1.0 CE1 A:HIS126 3.5 36.8 1.0 CG A:HIS429 3.6 38.2 1.0 CG A:HIS126 3.6 33.6 1.0 CU A:CU601 3.7 51.1 0.6 CE1 A:HIS429 3.7 37.7 1.0 CG A:HIS427 3.9 40.7 1.0 ND1 A:HIS427 3.9 38.6 1.0 ND1 A:HIS124 3.9 31.9 1.0 CG A:HIS124 3.9 28.7 1.0 CU A:CU602 4.0 32.7 0.6 CA A:HIS126 4.0 30.4 1.0 ND1 A:HIS429 4.1 39.3 1.0 NE2 A:HIS126 4.1 35.4 1.0 CB A:HIS126 4.1 27.8 1.0 CD2 A:HIS126 4.1 33.6 1.0 CA A:HIS429 4.5 32.6 1.0 CB A:HIS429 4.6 32.9 1.0 N A:GLY127 4.6 33.6 1.0 O A:MET428 4.8 32.0 1.0 C A:HIS126 4.8 32.5 1.0 N A:HIS429 4.9 33.2 1.0 NE2 A:HIS477 5.0 39.8 1.0

Copper binding site 4 out of 32 in the The X-Ray Crystal Structure of Multicopper Oxidase From Sulfurimonas Sp.


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 4 of The X-Ray Crystal Structure of Multicopper Oxidase From Sulfurimonas Sp. within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu604 b:63.4 occ:1.00 ND1 A:HIS424 1.9 45.7 1.0 SG A:CYS478 2.1 72.8 1.0 ND1 A:HIS483 2.2 48.1 1.0 CE1 A:HIS424 2.6 48.1 1.0 CE1 A:HIS483 3.1 48.3 1.0 CG A:HIS424 3.1 38.4 1.0 CB A:CYS478 3.1 32.6 1.0 CG A:HIS483 3.2 44.5 1.0 SD A:MET488 3.5 40.5 1.0 CB A:ILE480 3.6 37.2 1.0 CG1 A:ILE480 3.6 44.0 1.0 CB A:HIS483 3.6 46.3 1.0 CB A:HIS424 3.7 33.1 1.0 NE2 A:HIS424 3.8 38.3 1.0 CD2 A:HIS424 4.0 39.4 1.0 CA A:HIS424 4.1 36.5 1.0 NE2 A:HIS483 4.3 41.9 1.0 CD2 A:HIS483 4.4 41.7 1.0 CG2 A:ILE480 4.4 38.8 1.0 CE A:MET488 4.4 43.8 1.0 CA A:CYS478 4.5 40.0 1.0 O A:ALA423 4.6 31.2 1.0 N A:ILE480 4.6 40.7 1.0 CA A:ILE480 4.7 39.6 1.0 CD A:PRO425 4.8 36.5 1.0 O A:ILE480 4.9 41.1 1.0 CD1 A:ILE480 5.0 41.1 1.0

Copper binding site 5 out of 32 in the The X-Ray Crystal Structure of Multicopper Oxidase From Sulfurimonas Sp.


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 5 of The X-Ray Crystal Structure of Multicopper Oxidase From Sulfurimonas Sp. within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu601 b:56.6 occ:0.58 NE2 B:HIS166 2.0 42.4 1.0 NE2 B:HIS477 2.1 37.5 1.0 NE2 B:HIS429 2.1 37.9 1.0 CE1 B:HIS477 2.6 33.7 1.0 CD2 B:HIS166 2.9 36.4 1.0 CE1 B:HIS429 3.0 38.2 1.0 CE1 B:HIS166 3.1 43.7 1.0 CD2 B:HIS429 3.2 40.1 1.0 CD2 B:HIS477 3.3 32.5 1.0 CD2 B:HIS427 3.8 36.8 1.0 ND1 B:HIS477 3.8 35.9 1.0 CU B:CU603 4.0 41.9 0.5 CG2 B:VAL475 4.0 44.7 1.0 CG B:HIS166 4.1 38.0 1.0 ND1 B:HIS166 4.1 41.7 1.0 ND1 B:HIS429 4.1 38.9 1.0 CG B:HIS477 4.2 34.0 1.0 NE2 B:HIS427 4.2 39.4 1.0 CG B:HIS429 4.3 40.2 1.0 CD2 B:HIS124 4.4 37.3 1.0 OE1 B:GLU484 4.4 52.9 1.0 NE2 B:HIS124 4.4 40.1 1.0 NE2 B:HIS479 4.5 33.3 1.0 CU B:CU602 4.5 34.6 0.6 CD2 B:HIS479 4.6 28.8 1.0 CE1 B:HIS164 4.7 35.1 1.0 CG B:HIS124 4.8 33.4 1.0 CE1 B:HIS124 4.8 38.5 1.0 CD B:GLU484 5.0 46.6 1.0

Copper binding site 6 out of 32 in the The X-Ray Crystal Structure of Multicopper Oxidase From Sulfurimonas Sp.


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 6 of The X-Ray Crystal Structure of Multicopper Oxidase From Sulfurimonas Sp. within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu602 b:34.6 occ:0.61 ND1 B:HIS126 1.8 34.9 1.0 NE2 B:HIS164 2.0 34.5 1.0 NE2 B:HIS479 2.2 33.3 1.0 CE1 B:HIS126 2.5 38.6 1.0 CE1 B:HIS164 2.9 35.1 1.0 CG B:HIS126 3.0 34.7 1.0 CD2 B:HIS164 3.0 32.2 1.0 CE1 B:HIS479 3.0 28.2 1.0 CD2 B:HIS479 3.3 28.8 1.0 CZ2 B:TRP162 3.5 29.1 1.0 CB B:HIS126 3.6 33.9 1.0 NE2 B:HIS126 3.8 40.9 1.0 CD2 B:HIS124 3.8 37.3 1.0 CU B:CU603 3.8 41.9 0.5 CD2 B:HIS126 4.0 37.1 1.0 CE2 B:TRP162 4.0 32.8 1.0 ND1 B:HIS164 4.0 26.9 1.0 CG B:HIS164 4.1 29.6 1.0 ND1 B:HIS479 4.2 31.2 1.0 CH2 B:TRP162 4.2 30.2 1.0 NE1 B:TRP162 4.3 33.4 1.0 NE2 B:HIS124 4.3 40.1 1.0 CG B:HIS479 4.3 37.4 1.0 CU B:CU601 4.5 56.6 0.6 CD2 B:HIS427 4.5 36.8 1.0 NE2 B:HIS427 4.5 39.4 1.0 CB B:ALA298 4.7 28.4 1.0 CA B:HIS126 4.8 34.0 1.0

Copper binding site 7 out of 32 in the The X-Ray Crystal Structure of Multicopper Oxidase From Sulfurimonas Sp.


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 7 of The X-Ray Crystal Structure of Multicopper Oxidase From Sulfurimonas Sp. within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu603 b:41.9 occ:0.48 NE2 B:HIS427 1.8 39.4 1.0 NE2 B:HIS124 1.9 40.1 1.0 CE1 B:HIS427 2.7 37.7 1.0 CE1 B:HIS124 2.8 38.5 1.0 CD2 B:HIS427 2.9 36.8 1.0 CD2 B:HIS124 2.9 37.3 1.0 ND1 B:HIS126 3.2 34.9 1.0 CD2 B:HIS429 3.2 40.1 1.0 CG B:HIS126 3.3 34.7 1.0 NE2 B:HIS429 3.4 37.9 1.0 CE1 B:HIS126 3.4 38.6 1.0 CD2 B:HIS126 3.7 37.1 1.0 NE2 B:HIS126 3.7 40.9 1.0 ND1 B:HIS427 3.8 38.3 1.0 CA B:HIS126 3.8 34.0 1.0 CU B:CU602 3.8 34.6 0.6 ND1 B:HIS124 3.9 35.4 1.0 CG B:HIS427 3.9 38.4 1.0 CB B:HIS126 3.9 33.9 1.0 CU B:CU601 4.0 56.6 0.6 CG B:HIS124 4.0 33.4 1.0 CG B:HIS429 4.0 40.2 1.0 CE1 B:HIS429 4.2 38.2 1.0 N B:GLY127 4.4 33.7 1.0 ND1 B:HIS429 4.5 38.9 1.0 C B:HIS126 4.6 35.5 1.0 CA B:HIS429 4.7 36.6 1.0 O B:MET428 4.8 37.6 1.0 N B:HIS126 4.8 32.7 1.0 CB B:HIS429 4.8 40.9 1.0 N B:HIS429 4.9 35.1 1.0 C B:MET428 5.0 41.2 1.0

Copper binding site 8 out of 32 in the The X-Ray Crystal Structure of Multicopper Oxidase From Sulfurimonas Sp.


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 8 of The X-Ray Crystal Structure of Multicopper Oxidase From Sulfurimonas Sp. within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu604 b:63.4 occ:1.00 ND1 B:HIS424 1.9 49.2 1.0 ND1 B:HIS483 1.9 46.7 1.0 SG B:CYS478 2.1 41.4 1.0 CE1 B:HIS424 2.6 44.1 1.0 CE1 B:HIS483 2.9 46.6 1.0 CG B:HIS483 2.9 45.4 1.0 CG B:HIS424 3.1 42.7 1.0 CB B:CYS478 3.1 35.0 1.0 SD B:MET488 3.2 41.5 1.0 CB B:HIS483 3.3 44.2 1.0 CG1 B:ILE480 3.5 45.3 1.0 CB B:HIS424 3.7 34.4 1.0 CB B:ILE480 3.7 41.1 1.0 NE2 B:HIS424 3.7 36.9 1.0 NE2 B:HIS483 4.0 44.4 1.0 CD2 B:HIS424 4.0 38.9 1.0 CD2 B:HIS483 4.0 43.4 1.0 CE B:MET488 4.1 43.5 1.0 CA B:HIS424 4.1 34.0 1.0 CA B:CYS478 4.5 35.8 1.0 CG2 B:ILE480 4.6 39.6 1.0 N B:ILE480 4.7 35.8 1.0 O B:ALA423 4.7 31.6 1.0 CA B:ILE480 4.8 37.9 1.0 CA B:HIS483 4.8 42.9 1.0 CD B:PRO425 4.8 37.3 1.0 CD1 B:ILE480 4.9 41.8 1.0 CG B:MET488 4.9 36.3 1.0

Copper binding site 9 out of 32 in the The X-Ray Crystal Structure of Multicopper Oxidase From Sulfurimonas Sp.


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 9 of The X-Ray Crystal Structure of Multicopper Oxidase From Sulfurimonas Sp. within 5.0Å range: probe atom residue distance (Å) B Occ C:Cu601 b:52.5 occ:0.67 NE2 C:HIS166 2.0 44.8 1.0 NE2 C:HIS429 2.2 42.5 1.0 NE2 C:HIS477 2.2 42.0 1.0 CE1 C:HIS477 2.8 36.7 1.0 CD2 C:HIS166 2.8 41.5 1.0 CE1 C:HIS429 2.9 39.6 1.0 CE1 C:HIS166 3.1 46.2 1.0 CD2 C:HIS429 3.3 41.8 1.0 CD2 C:HIS477 3.4 41.0 1.0 CD2 C:HIS427 3.7 36.7 1.0 CU C:CU603 3.9 38.2 0.4 ND1 C:HIS477 4.0 37.8 1.0 CG C:HIS166 4.0 38.5 1.0 CD2 C:HIS124 4.1 34.4 1.0 NE2 C:HIS427 4.1 40.3 1.0 ND1 C:HIS166 4.1 43.5 1.0 ND1 C:HIS429 4.1 40.0 1.0 NE2 C:HIS124 4.2 36.6 1.0 CU C:CU602 4.2 36.4 0.6 OE2 C:GLU484 4.3 52.8 1.0 CG C:HIS477 4.3 42.5 1.0 CG2 C:VAL475 4.3 42.8 1.0 NE2 C:HIS479 4.4 41.0 1.0 CG C:HIS429 4.4 40.7 1.0 CD2 C:HIS479 4.4 35.4 1.0 CE1 C:HIS164 4.6 32.5 1.0 CG C:HIS124 4.7 34.3 1.0 CE1 C:HIS124 4.8 35.8 1.0 CG C:HIS427 5.0 37.1 1.0

Copper binding site 10 out of 32 in the The X-Ray Crystal Structure of Multicopper Oxidase From Sulfurimonas Sp.


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 10 of The X-Ray Crystal Structure of Multicopper Oxidase From Sulfurimonas Sp. within 5.0Å range: probe atom residue distance (Å) B Occ C:Cu602 b:36.4 occ:0.57 ND1 C:HIS126 1.8 30.9 1.0 NE2 C:HIS164 2.1 30.7 1.0 NE2 C:HIS479 2.2 41.0 1.0 CE1 C:HIS126 2.4 36.3 1.0 CE1 C:HIS164 2.9 32.5 1.0 CE1 C:HIS479 3.1 36.4 1.0 CG C:HIS126 3.1 34.0 1.0 CD2 C:HIS479 3.2 35.4 1.0 CD2 C:HIS164 3.2 28.9 1.0 NE2 C:HIS126 3.7 32.7 1.0 CU C:CU603 3.7 38.2 0.4 CZ2 C:TRP162 3.7 31.8 1.0 CB C:HIS126 3.8 27.9 1.0 CD2 C:HIS124 4.0 34.4 1.0 CD2 C:HIS126 4.0 34.6 1.0 ND1 C:HIS164 4.0 28.6 1.0 ND1 C:HIS479 4.2 38.6 1.0 CU C:CU601 4.2 52.5 0.7 CG C:HIS164 4.2 30.3 1.0 CE2 C:TRP162 4.2 29.2 1.0 CG C:HIS479 4.3 36.3 1.0 CH2 C:TRP162 4.3 33.6 1.0 CD2 C:HIS427 4.4 36.7 1.0 NE2 C:HIS427 4.4 40.3 1.0 NE1 C:TRP162 4.5 28.7 1.0 NE2 C:HIS124 4.5 36.6 1.0 CB C:ALA298 4.7 29.3 1.0 CA C:HIS126 4.9 29.6 1.0

Y.Wang, H.Qian. The X-Ray Crystal Structure of Multicopper Oxidase From Sulfurimonas Sp. To Be Published.