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Magnesium in PDB 3c15: Complex of Gs-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Pyrophosphate and Mg

Enzymatic activity of Complex of Gs-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Pyrophosphate and Mg

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

Protein crystallography data

The structure of Complex of Gs-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Pyrophosphate and Mg, PDB code: 3c15 was solved by T.-C.Mou, S.R.Sprang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 24.49 / 2.78
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 117.510, 133.080, 70.108, 90.00, 90.00, 90.00
R / Rfree (%) 23.7 / 29.1

Other elements in 3c15:

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

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 Pyrophosphate and Mg (pdb code 3c15). 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 Pyrophosphate and Mg, PDB code: 3c15:

Magnesium binding site 1 out of 1 in 3c15

Go back to Magnesium Binding Sites List in 3c15
Magnesium binding site 1 out of 1 in the Complex of Gs-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Pyrophosphate and Mg


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 Pyrophosphate and Mg within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg29

b:67.5
occ:1.00
 O3 A:POP1 1.8 71.9 1.0
OD2 A:ASP440 1.8 78.0 1.0
OD2 A:ASP396 2.3 93.2 1.0
O A:ILE397 2.5 63.9 1.0
P1 A:POP1 3.0 71.2 1.0
CG A:ASP440 3.0 75.3 1.0
O1 A:POP1 3.2 72.6 1.0
CG A:ASP396 3.2 89.8 1.0
O A:HOH30 3.2 67.5 1.0
OD1 A:ASP396 3.5 95.8 1.0
CB A:PHE400 3.6 86.4 1.0
C A:ILE397 3.6 69.3 1.0
OD1 A:ASP440 3.7 74.8 1.0
O6 A:POP1 3.7 71.6 1.0
O2 A:POP1 3.9 72.2 1.0
N A:ILE397 4.0 66.5 1.0
O A:POP1 4.1 70.9 1.0
O5 A:POP1 4.1 71.8 1.0
CB A:ASP440 4.2 68.8 1.0
P2 A:POP1 4.2 69.6 1.0
CA A:ILE397 4.3 64.3 1.0
CG A:PHE400 4.4 93.0 1.0
CB A:ASP396 4.5 78.7 1.0
N A:PHE400 4.6 82.3 1.0
CD2 A:PHE400 4.6 92.6 1.0
N A:GLU398 4.7 76.0 1.0
CB A:ILE397 4.7 61.0 1.0
CA A:PHE400 4.7 82.3 1.0
C A:ASP396 4.9 70.0 1.0
CA A:GLU398 4.9 83.8 1.0
NH1 A:ARG484 5.0 95.2 1.0

Reference:

T.C.Mou, N.Masada, D.M.Cooper, S.R.Sprang. Structural Basis For Inhibition of Mammalian Adenylyl Cyclase By Calcium. Biochemistry V. 48 3387 2009.
ISSN: ISSN 0006-2960
PubMed: 19243146
DOI: 10.1021/BI802122K
Page generated: Sun Aug 10 17:59:11 2025

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