Magnesium in PDB 7pdf: Focus Refinement of Soluble Domain of Adenylyl Cyclase 9 in Complex with Gs Protein Alpha Subunit and Mant-Gtp

The binding sites of Magnesium atom in the Focus Refinement of Soluble Domain of Adenylyl Cyclase 9 in Complex with Gs Protein Alpha Subunit and Mant-Gtp (pdb code 7pdf). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Focus Refinement of Soluble Domain of Adenylyl Cyclase 9 in Complex with Gs Protein Alpha Subunit and Mant-Gtp, PDB code: 7pdf:

Magnesium binding site 1 out of 1 in the Focus Refinement of Soluble Domain of Adenylyl Cyclase 9 in Complex with Gs Protein Alpha Subunit and Mant-Gtp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Focus Refinement of Soluble Domain of Adenylyl Cyclase 9 in Complex with Gs Protein Alpha Subunit and Mant-Gtp within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg502 b:69.1 occ:1.00 O2G B:GSP501 1.9 72.9 1.0 O2B B:GSP501 1.9 72.9 1.0 O1B B:GSP501 2.2 72.9 1.0 PB B:GSP501 2.2 72.9 1.0 PG B:GSP501 2.4 72.9 1.0 OG1 B:THR204 2.4 61.0 1.0 O3G B:GSP501 2.5 72.9 1.0 OG B:SER54 2.6 61.3 1.0 O3B B:GSP501 2.7 72.9 1.0 CB B:THR204 3.1 61.0 1.0 O3A B:GSP501 3.8 72.9 1.0 CB B:SER54 3.9 61.3 1.0 N B:SER54 4.0 61.3 1.0 CE B:LYS53 4.0 54.6 1.0 S1G B:GSP501 4.0 72.9 1.0 CG2 B:THR204 4.1 61.0 1.0 O B:VAL224 4.1 50.5 1.0 N B:THR204 4.2 61.0 1.0 CA B:THR204 4.3 61.0 1.0 OD1 B:ASP223 4.4 55.6 1.0 CB B:LYS53 4.5 54.6 1.0 CA B:SER54 4.6 61.3 1.0 O2A B:GSP501 4.6 72.9 1.0 PA B:GSP501 4.7 72.9 1.0 CA B:GLY225 4.7 51.8 1.0 CD B:LYS53 4.9 54.6 1.0 NZ B:LYS53 4.9 54.6 1.0 O1A B:GSP501 4.9 72.9 1.0 C B:VAL224 4.9 50.5 1.0 N B:LYS53 4.9 54.6 1.0 C B:LYS53 5.0 54.6 1.0

C.Qi, P.Lavriha, V.Mehta, B.Khanppnavar, I.Mohammed, Y.Li, M.Lazaratos, J.V.Schaefer, B.Dreier, A.Pluckthun, A.N.Bondar, C.W.Dessauer, V.M.Korkhov. Structural Basis of Adenylyl Cyclase 9 Activation. Nat Commun V. 13 1045 2022.
ISSN: ESSN 2041-1723
PubMed: 35210418
DOI: 10.1038/S41467-022-28685-Y