Copper in PDB 7otd: Oxytocin uc(Nmr) Solution Structure

The binding sites of Copper atom in the Oxytocin uc(Nmr) Solution Structure (pdb code 7otd). 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 Oxytocin uc(Nmr) Solution Structure, PDB code: 7otd:

Copper binding site 1 out of 1 in the Oxytocin uc(Nmr) Solution Structure


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Oxytocin uc(Nmr) Solution Structure within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu101 b:0.0 occ:1.00 N A:TYR2 1.9 0.0 1.0 N A:ILE3 1.9 0.0 1.0 N A:CYS1 1.9 0.0 1.0 N A:GLN4 2.0 0.0 1.0 C A:CYS1 2.5 0.0 1.0 H2 A:CYS1 2.5 0.0 1.0 H1 A:CYS1 2.5 0.0 1.0 C A:TYR2 2.7 0.0 1.0 CA A:CYS1 2.7 0.0 1.0 C A:ILE3 2.8 0.0 1.0 HB2 A:GLN4 2.8 0.0 1.0 H A:ASN5 2.8 0.0 1.0 CA A:TYR2 2.9 0.0 1.0 CA A:ILE3 2.9 0.0 1.0 HG22 A:ILE3 3.0 0.0 1.0 CA A:GLN4 3.0 0.0 1.0 HD2 A:TYR2 3.2 0.0 1.0 N A:ASN5 3.3 0.0 1.0 C A:GLN4 3.4 0.0 1.0 HB2 A:CYS1 3.4 0.0 1.0 O A:CYS1 3.4 0.0 1.0 CB A:GLN4 3.4 0.0 1.0 CD2 A:TYR2 3.5 0.0 1.0 HA A:CYS1 3.5 0.0 1.0 HA A:TYR2 3.6 0.0 1.0 HA A:ILE3 3.6 0.0 1.0 CB A:CYS1 3.7 0.0 1.0 O A:TYR2 3.8 0.0 1.0 CG A:TYR2 3.8 0.0 1.0 CG2 A:ILE3 3.9 0.0 1.0 O A:ILE3 3.9 0.0 1.0 HA A:GLN4 3.9 0.0 1.0 CB A:TYR2 4.0 0.0 1.0 CB A:ILE3 4.0 0.0 1.0 H A:CYS6 4.0 0.0 1.0 HA A:ASN5 4.1 0.0 1.0 CE2 A:TYR2 4.1 0.0 1.0 HB3 A:GLN4 4.1 0.0 1.0 HG3 A:GLN4 4.2 0.0 1.0 CA A:ASN5 4.3 0.0 1.0 HB3 A:CYS1 4.3 0.0 1.0 O A:GLN4 4.3 0.0 1.0 HG23 A:ILE3 4.3 0.0 1.0 HE2 A:TYR2 4.4 0.0 1.0 HB A:ILE3 4.4 0.0 1.0 HB2 A:TYR2 4.5 0.0 1.0 CG A:GLN4 4.5 0.0 1.0 HG21 A:ILE3 4.6 0.0 1.0 SG A:CYS6 4.8 0.0 1.0 HB3 A:TYR2 4.8 0.0 1.0 CD1 A:TYR2 4.8 0.0 1.0 N A:CYS6 4.8 0.0 1.0

I.Alshanski, D.E.Shalev, S.Yitzchaik, M.Hurevich. Determining the Structure and Binding Mechanism of Oxytocin-Cu 2+ Complex Using Paramagnetic Relaxation Enhancement uc(Nmr) Analysis. J.Biol.Inorg.Chem. V. 26 809 2021.
ISSN: ESSN 1432-1327
PubMed: 34459989
DOI: 10.1007/S00775-021-01897-1