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Magnesium in PDB 1cul: Complex of Gs-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with 2',5'-Dideoxy-Adenosine 3'- Triphosphate and Mg

Enzymatic activity of Complex of Gs-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with 2',5'-Dideoxy-Adenosine 3'- Triphosphate and Mg

All present enzymatic activity of Complex of Gs-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with 2',5'-Dideoxy-Adenosine 3'- Triphosphate 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 2',5'-Dideoxy-Adenosine 3'- Triphosphate and Mg, PDB code: 1cul was solved by J.J.G.Tesmer, C.A.Dessauer, R.K.Sunahara, R.A.Johnson, A.G.Gilman, S.R.Sprang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 15.00 / 2.40
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 118.200, 133.600, 70.600, 90.00, 90.00, 90.00
R / Rfree (%) 21.6 / 26.3

Other elements in 1cul:

The structure of Complex of Gs-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with 2',5'-Dideoxy-Adenosine 3'- Triphosphate and Mg also contains other interesting chemical elements:

Chlorine (Cl) 2 atoms

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 2',5'-Dideoxy-Adenosine 3'- Triphosphate and Mg (pdb code 1cul). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the Complex of Gs-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with 2',5'-Dideoxy-Adenosine 3'- Triphosphate and Mg, PDB code: 1cul:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in 1cul

Go back to Magnesium Binding Sites List in 1cul
Magnesium binding site 1 out of 3 in the Complex of Gs-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with 2',5'-Dideoxy-Adenosine 3'- Triphosphate 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 2',5'-Dideoxy-Adenosine 3'- Triphosphate and Mg within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1006

b:50.9
occ:1.00
 O A:ILE397 2.0 57.6 1.0
OD1 A:ASP440 2.0 53.2 1.0
OD1 A:ASP396 2.3 66.0 1.0
O2B A:3PO1003 2.3 95.1 1.0
O2G A:3PO1003 2.6 100.0 1.0
CG A:ASP396 3.2 62.7 1.0
C A:ILE397 3.2 55.6 1.0
CG A:ASP440 3.3 54.0 1.0
PB A:3PO1003 3.4 95.1 1.0
OD2 A:ASP396 3.4 66.7 1.0
MG A:MG1007 3.4 70.1 1.0
O3B A:3PO1003 3.6 98.5 1.0
O5' A:3PO1003 3.6 91.2 0.5
O3A A:3PO1003 3.6 93.6 1.0
PG A:3PO1003 3.7 100.0 1.0
CB A:PHE400 3.9 53.6 1.0
N A:ILE397 3.9 52.1 1.0
OD2 A:ASP440 4.0 53.4 1.0
O1A A:3PO1003 4.0 91.9 0.5
PA A:3PO1003 4.1 92.0 0.5
CA A:ILE397 4.1 53.2 1.0
N A:GLU398 4.2 57.5 1.0
N A:PHE400 4.2 54.3 1.0
CB A:ASP440 4.3 49.2 1.0
CA A:GLU398 4.3 59.8 1.0
C A:ASP396 4.5 54.1 1.0
N A:GLY399 4.5 57.4 1.0
CB A:ASP396 4.5 59.9 1.0
C A:GLU398 4.5 58.9 1.0
CB A:ILE397 4.6 52.5 1.0
O1G A:3PO1003 4.6 97.8 1.0
O3G A:3PO1003 4.7 100.0 1.0
CA A:PHE400 4.7 54.0 1.0
O1B A:3PO1003 4.8 94.7 1.0
CA A:ASP396 5.0 54.2 1.0

Magnesium binding site 2 out of 3 in 1cul

Go back to Magnesium Binding Sites List in 1cul
Magnesium binding site 2 out of 3 in the Complex of Gs-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with 2',5'-Dideoxy-Adenosine 3'- Triphosphate and Mg


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Complex of Gs-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with 2',5'-Dideoxy-Adenosine 3'- Triphosphate and Mg within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1007

b:70.1
occ:1.00
 O5' A:3PO1003 1.9 91.2 0.5
O1P B:1031082 2.0 49.6 0.5
O1A A:3PO1003 2.1 91.9 0.5
PA A:3PO1003 2.5 92.0 0.5
OD2 A:ASP440 2.6 53.4 1.0
P B:1031082 2.9 49.6 0.5
OD2 A:ASP396 3.0 66.7 1.0
OD1 A:ASP440 3.0 53.2 1.0
CG A:ASP440 3.2 54.0 1.0
O2P B:1031082 3.3 48.4 0.5
MG A:MG1006 3.4 50.9 1.0
O3A A:3PO1003 3.5 93.6 1.0
O3' B:1031082 3.6 48.0 1.0
O2A A:3PO1003 3.6 92.0 0.5
C3' B:1031082 3.7 41.4 1.0
O2B A:3PO1003 3.8 95.1 1.0
C2' B:1031082 3.9 40.0 1.0
CG A:ASP396 3.9 62.7 1.0
OD1 A:ASP396 4.1 66.0 1.0
O3P B:1031082 4.2 47.5 0.5
PB A:3PO1003 4.3 95.1 1.0
O2G A:3PO1003 4.6 100.0 1.0
CB A:ASP440 4.7 49.2 1.0
CB A:CYS441 4.9 50.6 1.0

Magnesium binding site 3 out of 3 in 1cul

Go back to Magnesium Binding Sites List in 1cul
Magnesium binding site 3 out of 3 in the Complex of Gs-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with 2',5'-Dideoxy-Adenosine 3'- Triphosphate and Mg


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Complex of Gs-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with 2',5'-Dideoxy-Adenosine 3'- Triphosphate and Mg within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg396

b:39.0
occ:1.00
 O2B C:GSP395 1.9 36.0 1.0
O2G C:GSP395 2.0 48.3 1.0
O C:HOH409 2.1 46.7 1.0
O C:HOH405 2.2 37.5 1.0
OG1 C:THR204 2.2 45.7 1.0
OG C:SER54 2.5 41.2 1.0
PB C:GSP395 3.0 35.6 1.0
PG C:GSP395 3.0 46.3 1.0
O3B C:GSP395 3.1 43.1 1.0
CB C:THR204 3.2 43.8 1.0
CB C:SER54 3.3 32.4 1.0
N C:SER54 3.8 27.4 1.0
O3G C:GSP395 3.9 45.8 1.0
O3A C:GSP395 4.0 34.1 1.0
O1B C:GSP395 4.1 31.6 1.0
CG2 C:THR204 4.1 40.8 1.0
CA C:SER54 4.1 32.3 1.0
N C:THR204 4.2 48.3 1.0
O2A C:GSP395 4.2 26.0 1.0
CA C:THR204 4.3 48.3 1.0
OD2 C:ASP223 4.4 43.6 1.0
OD1 C:ASP223 4.4 46.0 1.0
O C:HOH427 4.5 60.4 1.0
PA C:GSP395 4.5 29.7 1.0
S1G C:GSP395 4.5 53.5 1.0
O C:VAL224 4.5 37.5 1.0
O1A C:GSP395 4.6 31.6 1.0
O C:VAL202 4.7 45.4 1.0
CE C:LYS53 4.8 23.6 1.0
CB C:LYS53 4.8 24.4 1.0
CG C:ASP223 4.8 43.6 1.0
C C:LYS53 4.9 27.7 1.0

Reference:

J.J.Tesmer, C.W.Dessauer, R.K.Sunahara, L.D.Murray, R.A.Johnson, A.G.Gilman, S.R.Sprang. Molecular Basis For P-Site Inhibition of Adenylyl Cyclase. Biochemistry V. 39 14464 2000.
ISSN: ISSN 0006-2960
PubMed: 11087399
DOI: 10.1021/BI0015562
Page generated: Mon Dec 14 05:49:09 2020

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