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Manganese in PDB 1tl7: Complex of Gs- with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with 2'(3')-O-(N- Methylanthraniloyl)-Guanosine 5'-Triphosphate and Mn

Enzymatic activity of Complex of Gs- with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with 2'(3')-O-(N- Methylanthraniloyl)-Guanosine 5'-Triphosphate and Mn

All present enzymatic activity of Complex of Gs- with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with 2'(3')-O-(N- Methylanthraniloyl)-Guanosine 5'-Triphosphate and Mn:
4.6.1.1;

Protein crystallography data

The structure of Complex of Gs- with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with 2'(3')-O-(N- Methylanthraniloyl)-Guanosine 5'-Triphosphate and Mn, PDB code: 1tl7 was solved by T.C.Mou, A.Gille, R.J.Seifert, S.R.Sprang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 14.99 / 2.80
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 118.230, 133.600, 70.350, 90.00, 90.00, 90.00
R / Rfree (%) 25.4 / 29.8

Other elements in 1tl7:

The structure of Complex of Gs- with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with 2'(3')-O-(N- Methylanthraniloyl)-Guanosine 5'-Triphosphate 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- with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with 2'(3')-O-(N- Methylanthraniloyl)-Guanosine 5'-Triphosphate and Mn (pdb code 1tl7). 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- with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with 2'(3')-O-(N- Methylanthraniloyl)-Guanosine 5'-Triphosphate and Mn, PDB code: 1tl7:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in 1tl7

Go back to Manganese Binding Sites List in 1tl7
Manganese binding site 1 out of 2 in the Complex of Gs- with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with 2'(3')-O-(N- Methylanthraniloyl)-Guanosine 5'-Triphosphate 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- with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with 2'(3')-O-(N- Methylanthraniloyl)-Guanosine 5'-Triphosphate and Mn within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn581

b:33.0
occ:1.00
 O3B A:ONM100 2.2 54.3 1.0
OD1 A:ASP440 2.4 62.2 1.0
O2A A:ONM100 2.6 62.9 1.0
OD1 A:ASP396 2.7 49.3 1.0
CG A:ASP440 3.4 59.2 1.0
OD2 A:ASP396 3.5 42.6 1.0
CG A:ASP396 3.5 47.4 1.0
OD2 A:ASP440 3.6 62.1 1.0
PA A:ONM100 3.7 65.0 1.0
PB A:ONM100 3.7 59.3 1.0
C5' A:ONM100 3.8 51.3 1.0
O2B A:ONM100 4.0 55.7 1.0
O5' A:ONM100 4.1 60.8 1.0
MN A:MN582 4.2 37.9 1.0
O1A A:ONM100 4.2 62.5 1.0
O A:LEU438 4.3 48.8 1.0
CB A:CYS441 4.4 48.3 1.0
C8 A:ONM100 4.5 54.7 1.0
N A:CYS441 4.6 49.4 1.0
N A:ASP440 4.6 54.4 1.0
O1B A:ONM100 4.7 59.6 1.0
C A:ASP440 4.7 49.8 1.0
CB A:ASP440 4.7 56.0 1.0
O4' A:ONM100 4.8 44.8 1.0
CA A:ASP440 4.9 52.5 1.0
CB A:ASP396 4.9 46.6 1.0
C4' A:ONM100 5.0 45.0 1.0

Manganese binding site 2 out of 2 in 1tl7

Go back to Manganese Binding Sites List in 1tl7
Manganese binding site 2 out of 2 in the Complex of Gs- with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with 2'(3')-O-(N- Methylanthraniloyl)-Guanosine 5'-Triphosphate 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- with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with 2'(3')-O-(N- Methylanthraniloyl)-Guanosine 5'-Triphosphate and Mn within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn582

b:37.9
occ:1.00
 OD2 A:ASP396 2.3 42.6 1.0
O1B A:ONM100 2.3 59.6 1.0
OD2 A:ASP440 2.4 62.1 1.0
O A:ILE397 2.4 49.1 1.0
O3B A:ONM100 2.6 54.3 1.0
PB A:ONM100 2.9 59.3 1.0
CG A:ASP396 3.0 47.4 1.0
O1G A:ONM100 3.2 60.2 1.0
C A:ILE397 3.3 52.6 1.0
N A:ILE397 3.4 50.7 1.0
CG A:ASP440 3.4 59.2 1.0
O2B A:ONM100 3.4 55.7 1.0
OD1 A:ASP396 3.5 49.3 1.0
PG A:ONM100 3.6 61.4 1.0
CA A:ILE397 3.7 51.2 1.0
CB A:PHE400 3.9 63.6 1.0
CB A:ASP396 3.9 46.6 1.0
CB A:ILE397 4.0 51.0 1.0
OD1 A:ASP440 4.0 62.2 1.0
MN A:MN581 4.2 33.0 1.0
C A:ASP396 4.2 48.0 1.0
N A:PHE400 4.3 63.1 1.0
O3G A:ONM100 4.4 45.2 1.0
O1A A:ONM100 4.4 62.5 1.0
CB A:ASP440 4.4 56.0 1.0
N A:GLU398 4.5 58.3 1.0
CA A:ASP396 4.6 46.4 1.0
N A:GLY399 4.6 63.9 1.0
NH1 A:ARG484 4.7 68.8 1.0
CA A:PHE400 4.7 61.9 1.0
O2G A:ONM100 4.8 62.8 1.0
CG2 A:ILE397 4.8 51.6 1.0
CG A:PHE400 4.9 66.5 1.0
O A:ASP440 5.0 45.7 1.0

Reference:

T.C.Mou, A.Gille, D.A.Fancy, R.Seifert, S.R.Sprang. Structural Basis For the Inhibition of Mammalian Membrane Adenylyl Cyclase By 2 '(3')-O-(N-Methylanthraniloyl)-Guanosine 5 '-Triphosphate. J.Biol.Chem. V. 280 7253 2005.
ISSN: ISSN 0021-9258
PubMed: 15591060
DOI: 10.1074/JBC.M409076200
Page generated: Sat Oct 5 12:35:13 2024

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