Cadmium in PDB 8ghj: Crystal Structure of Human AQP2 T125M Mutant

The structure of Crystal Structure of Human AQP2 T125M Mutant, PDB code: 8ghj was solved by S.Horsefield, C.J.Hagstroemer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.50 / 3.90
Space group	P 42
Cell size a, b, c (Å), α, β, γ (°)	118.31, 118.31, 90.4, 90, 90, 90
R / Rfree (%)	28.8 / 31.3

The binding sites of Cadmium atom in the Crystal Structure of Human AQP2 T125M Mutant (pdb code 8ghj). This binding sites where shown within 5.0 Angstroms radius around Cadmium atom.
In total 2 binding sites of Cadmium where determined in the Crystal Structure of Human AQP2 T125M Mutant, PDB code: 8ghj:
Jump to Cadmium binding site number: 1; 2;

Cadmium binding site 1 out of 2 in the Crystal Structure of Human AQP2 T125M Mutant


Mono view


Stereo pair view

A full contact list of Cadmium with other atoms in the Cd binding site number 1 of Crystal Structure of Human AQP2 T125M Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Cd301 b:181.7 occ:0.00 OE1 D:GLN57 3.0 204.7 1.0 OE2 A:GLU155 3.4 192.2 1.0 OE1 A:GLU155 3.5 177.7 1.0 CB D:ALA161 3.7 177.9 1.0 CD A:GLU155 3.8 178.5 1.0 N D:ALA161 3.9 169.9 1.0 CA D:THR159 4.0 173.8 1.0 CB A:THR159 4.0 181.5 1.0 CD D:GLN57 4.1 213.4 1.0 N D:LEU162 4.1 167.8 1.0 OG1 A:THR159 4.1 193.8 1.0 C D:THR159 4.1 180.9 1.0 CG D:LEU162 4.2 160.2 1.0 OG A:SER163 4.3 178.4 1.0 CA D:ALA161 4.3 168.5 1.0 N D:PRO160 4.3 188.3 1.0 CD D:PRO160 4.3 186.1 1.0 CD1 D:LEU162 4.4 167.2 1.0 CB D:THR159 4.5 171.5 1.0 NE2 D:GLN57 4.5 213.8 1.0 O D:THR159 4.7 179.4 1.0 CG2 A:THR159 4.7 171.3 1.0 C D:ALA161 4.7 171.4 1.0 O D:GLY158 4.8 181.7 1.0 C D:PRO160 4.9 175.9 1.0 CB D:LEU162 4.9 165.0 1.0

Cadmium binding site 2 out of 2 in the Crystal Structure of Human AQP2 T125M Mutant


Mono view


Stereo pair view

A full contact list of Cadmium with other atoms in the Cd binding site number 2 of Crystal Structure of Human AQP2 T125M Mutant within 5.0Å range: probe atom residue distance (Å) B Occ D:Cd301 b:212.8 occ:0.00 O D:GLU155 4.7 242.4 1.0

C.J.Hagstromer, J.Hyld Steffen, S.Kreida, T.Al-Jubair, A.Frick, P.Gourdon, S.Tornroth-Horsefield. Structural and Functional Analysis of Aquaporin-2 Mutants Involved in Nephrogenic Diabetes Insipidus. Sci Rep V. 13 14674 2023.
ISSN: ESSN 2045-2322
PubMed: 37674034
DOI: 10.1038/S41598-023-41616-1