Atomistry » Magnesium » PDB 1c5u-1cxz » 1cul
Atomistry »
  Magnesium »
    PDB 1c5u-1cxz »
      1cul »

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: Tue Aug 13 02:32:01 2024

Last articles

Ca in 2WRA
Ca in 2WQZ
Ca in 2WQS
Ca in 2WQ8
Ca in 2WQD
Ca in 2WOY
Ca in 2WQ5
Ca in 2WPM
Ca in 2WPK
Ca in 2WPJ
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy