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Manganese 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:

Magnesium (Mg) 1 atom
Chlorine (Cl) 1 atom

Manganese Binding Sites:

The binding sites of Manganese 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 Manganese atom.
In total 2 binding sites of Manganese where determined in the Complex of Gs-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Mant-Itp and Mn, PDB code: 3g82:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in 3g82

Go back to Manganese Binding Sites List in 3g82
Manganese binding site 1 out of 2 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 Manganese with other atoms in the Mn 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
A:Mn581

b:33.0
occ:1.00
O2A A:MI3100 2.3 39.2 1.0
OD1 A:ASP440 2.4 62.2 1.0
O3B A:MI3100 2.8 37.4 1.0
OD1 A:ASP396 2.9 49.3 1.0
PA A:MI3100 3.3 39.5 1.0
O5' A:MI3100 3.4 40.2 1.0
CG A:ASP440 3.6 59.2 1.0
CG A:ASP396 3.8 47.4 1.0
CB A:CYS441 3.9 48.3 1.0
OD2 A:ASP440 4.0 62.1 1.0
O A:LEU438 4.1 48.8 1.0
OD2 A:ASP396 4.2 42.6 1.0
PB A:MI3100 4.2 37.1 1.0
N A:CYS441 4.3 49.4 1.0
O1A A:MI3100 4.3 38.1 1.0
O3A A:MI3100 4.6 39.5 1.0
O4' A:MI3100 4.6 41.0 1.0
CA A:CYS441 4.6 48.6 1.0
C A:ASP440 4.7 49.8 1.0
MN A:MN582 4.7 37.9 1.0
C8 A:MI3100 4.7 41.8 1.0
N A:ASP440 4.8 54.4 1.0
CB A:ASP440 4.8 56.0 1.0
C5' A:MI3100 4.8 40.8 1.0
CA A:ASP440 5.0 52.5 1.0

Manganese binding site 2 out of 2 in 3g82

Go back to Manganese Binding Sites List in 3g82
Manganese binding site 2 out of 2 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 Manganese with other atoms in the Mn binding site number 2 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
A:Mn582

b:37.9
occ:1.00
OD2 A:ASP440 1.9 62.1 1.0
OD2 A:ASP396 2.1 42.6 1.0
O A:ILE397 2.2 49.1 1.0
O1B A:MI3100 2.3 37.4 1.0
O3B A:MI3100 2.7 37.4 1.0
O2G A:MI3100 2.8 37.8 1.0
CG A:ASP396 3.0 47.4 1.0
PB A:MI3100 3.1 37.1 1.0
CG A:ASP440 3.1 59.2 1.0
C A:ILE397 3.3 52.6 1.0
OD1 A:ASP396 3.4 49.3 1.0
PG A:MI3100 3.4 37.8 1.0
N A:ILE397 3.6 50.7 1.0
OD1 A:ASP440 3.6 62.2 1.0
CA A:ILE397 3.7 51.2 1.0
CB A:PHE400 3.9 63.6 1.0
CB A:ILE397 3.9 51.0 1.0
O2B A:MI3100 4.0 37.7 1.0
O3G A:MI3100 4.1 37.5 1.0
O1A A:MI3100 4.2 38.1 1.0
CB A:ASP396 4.3 46.6 1.0
CB A:ASP440 4.3 56.0 1.0
C A:ASP396 4.4 48.0 1.0
N A:GLU398 4.5 58.3 1.0
N A:PHE400 4.5 63.1 1.0
MN A:MN581 4.7 33.0 1.0
O5' A:MI3100 4.8 40.2 1.0
CG2 A:ILE397 4.8 51.6 1.0
CA A:ASP396 4.8 46.4 1.0
CA A:PHE400 4.9 61.9 1.0
O1G A:MI3100 4.9 37.8 1.0
CG A:PHE400 4.9 66.5 1.0
PA A:MI3100 4.9 39.5 1.0
CA A:GLU398 4.9 64.0 1.0
N A:GLY399 5.0 63.9 1.0
O2A A:MI3100 5.0 39.2 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: Sat Oct 5 16:22:40 2024

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