Copper in PDB 7r0h: Structural Basis of Ion Uptake in Copper-Transporting P1B-Type Atpases

The structure of Structural Basis of Ion Uptake in Copper-Transporting P1B-Type Atpases, PDB code: 7r0h was solved by N.Salustros, C.Groenberg, K.Wang, P.Gourdon, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.93 / 3.31
Space group	F 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	130.122, 151.115, 219.211, 90, 90, 90
R / Rfree (%)	21.4 / 25.1

The binding sites of Copper atom in the Structural Basis of Ion Uptake in Copper-Transporting P1B-Type Atpases (pdb code 7r0h). 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 Structural Basis of Ion Uptake in Copper-Transporting P1B-Type Atpases, PDB code: 7r0h:

Copper binding site 1 out of 1 in the Structural Basis of Ion Uptake in Copper-Transporting P1B-Type Atpases


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Structural Basis of Ion Uptake in Copper-Transporting P1B-Type Atpases within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu801 b:358.8 occ:1.00 SG A:CYS382 2.5 148.0 1.0 CB A:CYS382 2.5 151.9 1.0 CB A:CYS380 2.7 151.2 1.0 O A:CYS380 3.3 147.7 1.0 CE2 A:TYR162 3.5 124.6 1.0 CA A:CYS382 3.6 142.2 1.0 C A:CYS380 3.7 150.6 1.0 CA A:CYS380 3.8 152.2 1.0 SG A:CYS380 3.9 142.6 1.0 CE A:MET158 3.9 147.5 1.0 N A:CYS382 4.0 140.8 1.0 OH A:TYR162 4.0 128.6 1.0 CZ A:TYR162 4.2 119.6 1.0 CD2 A:TYR162 4.4 117.9 1.0 CG A:MET158 4.4 149.5 1.0 C A:PRO381 4.4 141.8 1.0 N A:PRO381 4.5 144.4 1.0 SD A:MET158 4.7 156.4 1.0 N A:CYS380 4.7 151.3 1.0 O A:PRO381 4.8 138.6 1.0 CG A:MET711 5.0 129.1 1.0 C A:CYS382 5.0 128.6 1.0

N.Salustros, C.Gronberg, N.S.Abeyrathna, P.Lyu, F.Oradd, K.Wang, M.Andersson, G.Meloni, P.Gourdon. Structural Basis of Ion Uptake in Copper-Transporting P 1B -Type Atpases. Nat Commun V. 13 5121 2022.
ISSN: ESSN 2041-1723
PubMed: 36045128
DOI: 10.1038/S41467-022-32751-W