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Magnesium in PDB 3g82: Complex of Gs-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Mant-Itp and Mn

Enzymatic activity of Complex of Gs-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Mant-Itp and Mn

All present enzymatic activity of Complex of Gs-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Mant-Itp and Mn:
4.6.1.1;

Protein crystallography data

The structure of Complex of Gs-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Mant-Itp and Mn, PDB code: 3g82 was solved by M.Huebner, T.-C.Mou, S.R.Sprang, R.Seifert, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 15.00 / 3.11
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 117.637, 133.423, 70.642, 90.00, 90.00, 90.00
R / Rfree (%) 23.7 / 29.4

Other elements in 3g82:

The structure of Complex of Gs-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Mant-Itp and Mn also contains other interesting chemical elements:

Manganese (Mn) 2 atoms
Chlorine (Cl) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Complex of Gs-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Mant-Itp and Mn (pdb code 3g82). 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 Complex of Gs-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Mant-Itp and Mn, PDB code: 3g82:

Magnesium binding site 1 out of 1 in 3g82

Go back to Magnesium Binding Sites List in 3g82
Magnesium binding site 1 out of 1 in the Complex of Gs-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Mant-Itp and Mn


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Complex of Gs-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Mant-Itp and Mn within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg396

b:11.8
occ:1.00
 O2G C:GSP395 1.7 34.8 1.0
OG1 C:THR204 2.1 38.0 1.0
OG C:SER54 2.5 17.7 1.0
O2B C:GSP395 2.5 25.4 1.0
PG C:GSP395 2.9 36.9 1.0
CB C:THR204 2.9 36.2 1.0
O3B C:GSP395 3.3 31.2 1.0
CB C:SER54 3.4 27.1 1.0
PB C:GSP395 3.5 26.6 1.0
O3G C:GSP395 3.7 37.0 1.0
N C:THR204 3.8 39.0 1.0
CA C:THR204 4.0 37.4 1.0
CG2 C:THR204 4.0 37.4 1.0
N C:SER54 4.1 22.6 1.0
OD2 C:ASP223 4.1 54.2 1.0
CA C:SER54 4.3 25.9 1.0
S1G C:GSP395 4.3 37.5 1.0
O C:VAL202 4.4 34.9 1.0
O3A C:GSP395 4.5 26.6 1.0
O2A C:GSP395 4.5 22.9 1.0
OD1 C:ASP223 4.5 54.0 1.0
O1B C:GSP395 4.6 20.3 1.0
O C:VAL224 4.8 39.2 1.0
CG C:ASP223 4.8 50.6 1.0
C C:LEU203 4.8 40.5 1.0
PA C:GSP395 4.8 26.7 1.0
O1A C:GSP395 4.8 24.1 1.0

Reference:

M.Huebner, J.Geduhn, C.Pinto, T.-C.Mou, B.Konig, S.R.Sprang, R.Seifert. 2',3'-(O)-(N-Methyl)Anthraniloyl-Inosine 5'-Triphosphate Is the Most Potent Adenylyl Cyclase 1 and 5 Inhibitor Known So Far and Effectively Promotes Catalytic Subunit Assembly in the Absence of Forskolin To Be Published.
Page generated: Sun Aug 10 21:34:10 2025

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