Copper in PDB 1x9l: Solution Structure of Cui-DR1885 From Deinococcus Radiodurans

The binding sites of Copper atom in the Solution Structure of Cui-DR1885 From Deinococcus Radiodurans (pdb code 1x9l). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total only one binding site of Copper was determined in the Solution Structure of Cui-DR1885 From Deinococcus Radiodurans, PDB code: 1x9l:

Copper binding site 1 out of 1 in the Solution Structure of Cui-DR1885 From Deinococcus Radiodurans


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Solution Structure of Cui-DR1885 From Deinococcus Radiodurans within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu150 b:10.0 occ:1.00 NE2 A:HIS108 2.1 10.0 1.0 SD A:MET110 2.4 10.0 1.0 SD A:MET75 2.4 10.0 1.0 SD A:MET86 2.5 10.0 1.0 CE1 A:HIS108 2.9 10.0 1.0 HE1 A:HIS108 2.9 10.0 1.0 HG3 A:MET110 2.9 10.0 1.0 HE3 A:MET86 3.0 10.0 1.0 CG A:MET110 3.1 10.0 1.0 CE A:MET86 3.1 10.0 1.0 HE2 A:MET86 3.2 10.0 1.0 HG2 A:MET75 3.2 10.0 1.0 HG2 A:MET110 3.2 10.0 1.0 CG A:MET75 3.3 10.0 1.0 HG2 A:MET86 3.3 10.0 1.0 CD2 A:HIS108 3.4 10.0 1.0 HE2 A:MET110 3.4 10.0 1.0 CE A:MET110 3.5 10.0 1.0 HB3 A:MET75 3.5 10.0 1.0 CG A:MET86 3.6 10.0 1.0 HE1 A:MET75 3.6 10.0 1.0 CE A:MET75 3.6 10.0 1.0 CB A:MET75 3.8 10.0 1.0 HE3 A:MET110 3.8 10.0 1.0 HD2 A:HIS108 3.8 10.0 1.0 HB2 A:MET75 3.9 10.0 1.0 HE2 A:MET75 4.0 10.0 1.0 ND1 A:HIS108 4.1 10.0 1.0 HE1 A:MET86 4.2 10.0 1.0 HG3 A:MET86 4.2 10.0 1.0 HG3 A:MET75 4.2 10.0 1.0 O A:ARG104 4.3 10.0 1.0 CG A:HIS108 4.4 10.0 1.0 HE1 A:MET110 4.4 10.0 1.0 HE3 A:MET75 4.5 10.0 1.0 CB A:MET110 4.6 10.0 1.0 O A:MET86 4.8 10.0 1.0 HA A:MET86 4.8 10.0 1.0 CB A:MET86 4.8 10.0 1.0 HB2 A:MET110 4.9 10.0 1.0 HA A:ASP105 4.9 10.0 1.0 HD1 A:HIS108 5.0 10.0 1.0 C A:MET86 5.0 10.0 1.0

L.Banci, I.Bertini, S.Ciofi-Baffoni, E.Katsari, N.Katsaros, K.Kubicek. A Copper(I) Protein Possibly Involved in the Assembly of Cua Center of Bacterial Cytochrome C Oxidase. Proc.Natl.Acad.Sci.Usa V. 102 3994 2005.
ISSN: ISSN 0027-8424
PubMed: 15753304
DOI: 10.1073/PNAS.0406150102