Copper in PDB 8ucp: Komagataella Pastoris Cytochrome C Oxidase in Complex with Human VMAT2 and Serotonin

The structure of Komagataella Pastoris Cytochrome C Oxidase in Complex with Human VMAT2 and Serotonin also contains other interesting chemical elements:

Iron	(Fe)	2 atoms
Zinc	(Zn)	1 atom

The binding sites of Copper atom in the Komagataella Pastoris Cytochrome C Oxidase in Complex with Human VMAT2 and Serotonin (pdb code 8ucp). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 3 binding sites of Copper where determined in the Komagataella Pastoris Cytochrome C Oxidase in Complex with Human VMAT2 and Serotonin, PDB code: 8ucp:
Jump to Copper binding site number: 1; 2; 3;

Copper binding site 1 out of 3 in the Komagataella Pastoris Cytochrome C Oxidase in Complex with Human VMAT2 and Serotonin


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Komagataella Pastoris Cytochrome C Oxidase in Complex with Human VMAT2 and Serotonin within 5.0Å range: probe atom residue distance (Å) B Occ a:Cu601 b:42.3 occ:1.00 NE2 a:HIS293 2.0 32.8 1.0 ND1 a:HIS243 2.0 32.9 1.0 NE2 a:HIS292 2.1 34.1 1.0 CD2 a:HIS293 2.5 32.8 1.0 CE1 a:HIS243 2.7 32.9 1.0 CE1 a:HIS292 2.9 34.1 1.0 CD2 a:HIS292 3.0 34.1 1.0 CG a:HIS243 3.2 32.9 1.0 CE1 a:HIS293 3.3 32.8 1.0 CHA a:HEA603 3.6 34.5 1.0 CB a:HIS243 3.8 32.9 1.0 CG a:HIS293 3.8 32.8 1.0 C1A a:HEA603 3.9 34.5 1.0 NE2 a:HIS243 3.9 32.9 1.0 ND1 a:HIS292 4.0 34.1 1.0 CG a:HIS292 4.0 34.1 1.0 CD2 a:HIS243 4.1 32.9 1.0 ND1 a:HIS293 4.1 32.8 1.0 NA a:HEA603 4.3 34.5 1.0 C2A a:HEA603 4.4 34.5 1.0 CA a:HIS243 4.5 32.9 1.0 C4D a:HEA603 4.6 34.5 1.0 FE a:HEA603 4.7 34.5 1.0 CAA a:HEA603 4.8 34.5 1.0 O a:VAL289 4.9 33.9 1.0

Copper binding site 2 out of 3 in the Komagataella Pastoris Cytochrome C Oxidase in Complex with Human VMAT2 and Serotonin


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Komagataella Pastoris Cytochrome C Oxidase in Complex with Human VMAT2 and Serotonin within 5.0Å range: probe atom residue distance (Å) B Occ b:Cu301 b:55.8 occ:1.00 CU1 b:CUA301 0.0 55.8 1.0 CU2 b:CUA301 1.7 55.8 1.0 CE b:MET230 3.0 37.1 1.0 SG b:CYS219 3.0 39.8 1.0 SG b:CYS223 3.1 39.3 1.0 CD2 b:HIS227 3.2 36.7 1.0 O b:GLU221 3.2 38.8 1.0 CB b:CYS223 3.5 39.3 1.0 ND1 b:HIS184 3.6 36.7 1.0 CB b:CYS219 3.9 39.8 1.0 NE2 b:HIS227 3.9 36.7 1.0 CG b:HIS227 4.0 36.7 1.0 CE1 b:HIS184 4.1 36.7 1.0 N b:CYS223 4.1 39.3 1.0 CA b:HIS227 4.3 36.7 1.0 SD b:MET230 4.4 37.1 1.0 C b:GLU221 4.4 38.8 1.0 CA b:CYS223 4.4 39.3 1.0 CB b:HIS227 4.4 36.7 1.0 O b:HIS227 4.5 36.7 1.0 CG b:HIS184 4.6 36.7 1.0 C b:LEU222 4.7 37.0 1.0 CE1 b:HIS227 4.9 36.7 1.0 ND1 b:HIS227 5.0 36.7 1.0 C b:HIS227 5.0 36.7 1.0

Copper binding site 3 out of 3 in the Komagataella Pastoris Cytochrome C Oxidase in Complex with Human VMAT2 and Serotonin


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Komagataella Pastoris Cytochrome C Oxidase in Complex with Human VMAT2 and Serotonin within 5.0Å range: probe atom residue distance (Å) B Occ b:Cu301 b:55.8 occ:1.00 CU2 b:CUA301 0.0 55.8 1.0 CU1 b:CUA301 1.7 55.8 1.0 CE b:MET230 2.8 37.1 1.0 CB b:CYS223 2.9 39.3 1.0 CE1 b:HIS184 3.1 36.7 1.0 SG b:CYS223 3.1 39.3 1.0 ND1 b:HIS184 3.2 36.7 1.0 SD b:MET230 3.7 37.1 1.0 O b:GLN121 3.7 38.5 1.0 CD1 b:TRP122 4.0 37.3 1.0 CA b:CYS223 4.1 39.3 1.0 NE2 b:HIS184 4.2 36.7 1.0 NE1 b:TRP122 4.3 37.3 1.0 CD2 b:HIS227 4.4 36.7 1.0 N b:CYS223 4.4 39.3 1.0 CG b:HIS184 4.4 36.7 1.0 CA b:HIS227 4.4 36.7 1.0 SG b:CYS219 4.4 39.8 1.0 O b:MET226 4.4 36.4 1.0 CG b:MET230 4.5 37.1 1.0 O b:GLU221 4.6 38.8 1.0 C b:CYS223 4.7 39.3 1.0 CB b:HIS227 4.8 36.7 1.0 CG b:HIS227 4.9 36.7 1.0 CD2 b:HIS184 4.9 36.7 1.0 C b:GLN121 4.9 38.5 1.0

J.Ye, B.Liu, W.Li. Komagataella Pastoris Cytochrome C Oxidase in Complex with Human VMAT2 and Serotonin To Be Published.