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Magnesium in PDB 1cs4: Complex of Gs-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with 2'-Deoxy-Adenosine 3'- Monophosphate, Pyrophosphate and Mg

Enzymatic activity of Complex of Gs-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with 2'-Deoxy-Adenosine 3'- Monophosphate, Pyrophosphate and Mg

All present enzymatic activity of Complex of Gs-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with 2'-Deoxy-Adenosine 3'- Monophosphate, 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 2'-Deoxy-Adenosine 3'- Monophosphate, Pyrophosphate and Mg, PDB code: 1cs4 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 / 2.50
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 118.500, 134.500, 71.300, 90.00, 90.00, 90.00
R / Rfree (%) 21.6 / 26.4

Other elements in 1cs4:

The structure of Complex of Gs-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with 2'-Deoxy-Adenosine 3'- Monophosphate, 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 2'-Deoxy-Adenosine 3'- Monophosphate, Pyrophosphate and Mg (pdb code 1cs4). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Complex of Gs-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with 2'-Deoxy-Adenosine 3'- Monophosphate, Pyrophosphate and Mg, PDB code: 1cs4:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 1cs4

Go back to Magnesium Binding Sites List in 1cs4
Magnesium binding site 1 out of 2 in the Complex of Gs-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with 2'-Deoxy-Adenosine 3'- Monophosphate, 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 2'-Deoxy-Adenosine 3'- Monophosphate, Pyrophosphate and Mg within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg581

b:46.5
occ:1.00
 O A:ILE397 2.2 59.1 1.0
OD1 A:ASP440 2.3 57.1 1.0
OD1 A:ASP396 2.4 65.5 1.0
O2 A:POP1005 2.4 55.4 1.0
O5 A:POP1005 2.7 56.2 1.0
O1P B:1011082 2.8 56.6 1.0
CG A:ASP396 3.2 61.4 1.0
C A:ILE397 3.4 60.1 1.0
OD2 A:ASP396 3.5 63.7 1.0
P1 A:POP1005 3.5 57.4 1.0
CG A:ASP440 3.5 55.3 1.0
O3 A:POP1005 3.7 55.1 1.0
P2 A:POP1005 3.8 59.7 1.0
CB A:PHE400 3.8 59.2 1.0
O A:POP1005 3.9 57.3 1.0
P B:1011082 4.0 57.1 1.0
N A:ILE397 4.1 57.1 1.0
N A:PHE400 4.1 58.0 1.0
OD2 A:ASP440 4.1 52.5 1.0
O3P B:1011082 4.2 57.1 1.0
CA A:ILE397 4.2 59.5 1.0
O4 A:POP1005 4.2 55.0 1.0
N A:GLU398 4.4 60.2 1.0
N A:GLY399 4.4 57.6 1.0
CB A:ILE397 4.5 60.8 1.0
CA A:GLU398 4.6 62.1 1.0
CB A:ASP396 4.6 57.5 1.0
C A:ASP396 4.6 55.1 1.0
CA A:PHE400 4.6 58.1 1.0
CB A:ASP440 4.7 51.4 1.0
NH2 A:ARG484 4.7 54.1 1.0
C A:GLU398 4.8 60.6 1.0
O2P B:1011082 4.8 59.0 1.0
O1 A:POP1005 4.8 54.9 1.0
CG A:PHE400 5.0 58.5 1.0

Magnesium binding site 2 out of 2 in 1cs4

Go back to Magnesium Binding Sites List in 1cs4
Magnesium binding site 2 out of 2 in the Complex of Gs-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with 2'-Deoxy-Adenosine 3'- Monophosphate, Pyrophosphate 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'-Deoxy-Adenosine 3'- Monophosphate, Pyrophosphate and Mg within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg396

b:42.9
occ:1.00
 O2B C:GSP1000 1.9 35.6 1.0
O2G C:GSP1000 2.0 53.0 1.0
O C:HOH1007 2.1 31.9 1.0
OG1 C:THR204 2.1 53.4 1.0
O C:HOH1010 2.2 68.2 1.0
OG C:SER54 2.2 43.5 1.0
PG C:GSP1000 3.1 49.3 1.0
PB C:GSP1000 3.1 35.5 1.0
CB C:THR204 3.1 52.2 1.0
CB C:SER54 3.2 35.6 1.0
O3B C:GSP1000 3.2 40.3 1.0
N C:SER54 3.8 34.1 1.0
O3G C:GSP1000 3.9 48.7 1.0
O3A C:GSP1000 4.0 36.4 1.0
CA C:SER54 4.1 36.6 1.0
CG2 C:THR204 4.1 51.7 1.0
N C:THR204 4.1 54.9 1.0
O1B C:GSP1000 4.2 40.2 1.0
O2A C:GSP1000 4.2 34.4 1.0
OD2 C:ASP223 4.2 52.6 1.0
CA C:THR204 4.2 56.0 1.0
PA C:GSP1000 4.4 29.4 1.0
OD1 C:ASP223 4.5 56.4 1.0
O1A C:GSP1000 4.6 32.2 1.0
O C:VAL202 4.6 49.1 1.0
O C:HOH1032 4.7 52.1 1.0
S1G C:GSP1000 4.7 56.6 1.0
CG C:ASP223 4.8 54.1 1.0
O C:VAL224 4.8 48.3 1.0
C C:LYS53 4.9 32.8 1.0
CB C:LYS53 4.9 28.5 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: Tue Aug 13 02:31:48 2024

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