Copper in PDB 1cyx: Quinol Oxidase (Periplasmic Fragment of Subunit II with Engineered Cu-A Binding Site)(Cyoa)

The structure of Quinol Oxidase (Periplasmic Fragment of Subunit II with Engineered Cu-A Binding Site)(Cyoa), PDB code: 1cyx was solved by M.Wilmanns, P.Lappalainen, M.Kelly, E.Sauer-Eriksson, M.Saraste, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	6.00 / 2.30
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	46.000, 98.200, 39.900, 90.00, 90.00, 90.00
R / Rfree (%)	19.6 / 31.6

The binding sites of Copper atom in the Quinol Oxidase (Periplasmic Fragment of Subunit II with Engineered Cu-A Binding Site)(Cyoa) (pdb code 1cyx). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Quinol Oxidase (Periplasmic Fragment of Subunit II with Engineered Cu-A Binding Site)(Cyoa), PDB code: 1cyx:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in the Quinol Oxidase (Periplasmic Fragment of Subunit II with Engineered Cu-A Binding Site)(Cyoa)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Quinol Oxidase (Periplasmic Fragment of Subunit II with Engineered Cu-A Binding Site)(Cyoa) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu316 b:15.6 occ:1.00 CU1 A:CUA316 0.0 15.6 1.0 ND1 A:HIS215 1.7 11.7 1.0 SG A:CYS207 2.2 13.9 1.0 SG A:CYS211 2.2 13.4 1.0 O A:GLU209 2.3 21.9 1.0 CE1 A:HIS215 2.5 8.6 1.0 CU2 A:CUA316 2.5 17.5 1.0 CG A:HIS215 3.0 13.4 1.0 C A:GLU209 3.4 19.0 1.0 CB A:CYS207 3.5 17.6 1.0 CB A:CYS211 3.5 14.3 1.0 N A:CYS211 3.5 17.1 1.0 CB A:HIS215 3.6 17.1 1.0 NE2 A:HIS215 3.7 12.6 1.0 O A:CYS207 3.7 18.0 1.0 CA A:HIS215 3.9 19.2 1.0 CD2 A:HIS215 4.0 12.0 1.0 CA A:ILE210 4.0 16.9 1.0 C A:ILE210 4.0 18.1 1.0 N A:GLU209 4.1 20.3 1.0 N A:ILE210 4.1 17.5 1.0 CA A:CYS211 4.2 15.8 1.0 ND1 A:HIS172 4.2 6.4 1.0 C A:CYS207 4.2 20.3 1.0 CA A:GLU209 4.4 19.6 1.0 O A:HIS215 4.5 14.1 1.0 CA A:CYS207 4.5 18.2 1.0 C A:HIS215 4.6 16.6 1.0 SD A:MET218 4.7 13.6 1.0 CE1 A:HIS172 4.9 2.9 1.0 O A:ILE210 4.9 17.2 1.0

Copper binding site 2 out of 2 in the Quinol Oxidase (Periplasmic Fragment of Subunit II with Engineered Cu-A Binding Site)(Cyoa)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Quinol Oxidase (Periplasmic Fragment of Subunit II with Engineered Cu-A Binding Site)(Cyoa) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu316 b:17.5 occ:1.00 CU2 A:CUA316 0.0 17.5 1.0 ND1 A:HIS172 1.8 6.4 1.0 SG A:CYS207 2.1 13.9 1.0 SG A:CYS211 2.3 13.4 1.0 CU1 A:CUA316 2.5 15.6 1.0 CE1 A:HIS172 2.7 2.9 1.0 CG A:HIS172 3.0 7.6 1.0 SD A:MET218 3.0 13.6 1.0 CB A:CYS211 3.1 14.3 1.0 CB A:CYS207 3.4 17.6 1.0 CB A:HIS172 3.5 8.2 1.0 O A:GLU209 3.7 21.9 1.0 NE2 A:HIS172 3.9 5.8 1.0 CD2 A:HIS172 4.0 6.3 1.0 CE A:MET218 4.1 6.8 1.0 CA A:HIS172 4.1 10.8 1.0 ND1 A:HIS215 4.2 11.7 1.0 CG A:MET218 4.3 9.2 1.0 CA A:CYS211 4.5 15.8 1.0 N A:CYS211 4.6 17.1 1.0 CA A:CYS207 4.7 18.2 1.0 O A:MET171 4.7 11.3 1.0 CB A:MET218 4.8 7.3 1.0 CE1 A:HIS215 4.8 8.6 1.0 N A:SER173 4.9 10.2 1.0 C A:GLU209 4.9 19.0 1.0

M.Wilmanns, P.Lappalainen, M.Kelly, E.Sauer-Eriksson, M.Saraste. Crystal Structure of the Membrane-Exposed Domain From A Respiratory Quinol Oxidase Complex with An Engineered Dinuclear Copper Center. Proc.Natl.Acad.Sci.Usa V. 92 11955 1995.
ISSN: ISSN 0027-8424
PubMed: 8618822
DOI: 10.1073/PNAS.92.26.11955