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Magnesium in PDB 1cjk: Complex of Gs-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Adenosine 5'-(Alpha Thio)-Triphosphate (Rp), Mg, and Mn

Enzymatic activity of Complex of Gs-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Adenosine 5'-(Alpha Thio)-Triphosphate (Rp), Mg, and Mn

All present enzymatic activity of Complex of Gs-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Adenosine 5'-(Alpha Thio)-Triphosphate (Rp), Mg, 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 Adenosine 5'-(Alpha Thio)-Triphosphate (Rp), Mg, and Mn, PDB code: 1cjk was solved by J.J.G.Tesmer, S.R.Sprang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 15.00 / 3.00
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 118.900, 134.900, 72.200, 90.00, 90.00, 90.00
R / Rfree (%) 22 / 26.6

Other elements in 1cjk:

The structure of Complex of Gs-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Adenosine 5'-(Alpha Thio)-Triphosphate (Rp), Mg, and Mn also contains other interesting chemical elements:

Manganese (Mn) 1 atom
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 Adenosine 5'-(Alpha Thio)-Triphosphate (Rp), Mg, and Mn (pdb code 1cjk). 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 Adenosine 5'-(Alpha Thio)-Triphosphate (Rp), Mg, and Mn, PDB code: 1cjk:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 1cjk

Go back to Magnesium Binding Sites List in 1cjk
Magnesium binding site 1 out of 2 in the Complex of Gs-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Adenosine 5'-(Alpha Thio)-Triphosphate (Rp), Mg, and Mn


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 Adenosine 5'-(Alpha Thio)-Triphosphate (Rp), Mg, and Mn within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg581

b:29.5
occ:1.00
 OD1 A:ASP440 2.1 34.8 1.0
O5' A:TAT801 2.4 42.4 1.0
OD1 A:ASP396 2.5 36.7 1.0
O A:HOH53 2.6 43.3 1.0
S1G A:TAT801 2.7 43.2 1.0
CG A:ASP440 3.1 34.7 1.0
C5' A:TAT801 3.2 46.0 1.0
OD2 A:ASP440 3.4 30.2 1.0
PA A:TAT801 3.5 39.4 1.0
MN A:MN582 3.6 18.4 1.0
CG A:ASP396 3.7 36.6 1.0
C3' A:TAT801 4.0 51.4 1.0
C4' A:TAT801 4.1 49.5 1.0
OD2 A:ASP396 4.1 36.6 1.0
CB A:CYS441 4.2 37.4 1.0
C2' A:TAT801 4.3 50.0 1.0
N A:CYS441 4.3 35.6 1.0
O A:LEU438 4.4 32.9 1.0
O3A A:TAT801 4.4 41.9 1.0
CB A:ASP440 4.5 33.1 1.0
O2A A:TAT801 4.6 39.9 1.0
N A:ASP440 4.6 32.3 1.0
C A:ASP440 4.7 34.3 1.0
CA A:CYS441 4.8 35.6 1.0
CA A:ASP440 4.9 32.9 1.0
CB A:ASP396 4.9 34.9 1.0
O4' A:TAT801 4.9 49.8 1.0
O1A A:TAT801 4.9 41.1 1.0
O2B A:TAT801 5.0 41.6 1.0

Magnesium binding site 2 out of 2 in 1cjk

Go back to Magnesium Binding Sites List in 1cjk
Magnesium binding site 2 out of 2 in the Complex of Gs-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Adenosine 5'-(Alpha Thio)-Triphosphate (Rp), Mg, and Mn


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 Adenosine 5'-(Alpha Thio)-Triphosphate (Rp), Mg, and Mn within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg403

b:11.8
occ:1.00
 O2G C:GSP405 1.7 34.8 1.0
O C:HOH412 2.0 12.0 1.0
O C:HOH409 2.0 29.7 1.0
OG1 C:THR204 2.1 45.5 1.0
OG C:SER54 2.4 24.0 1.0
O2B C:GSP405 2.5 25.4 1.0
CB C:THR204 2.9 46.3 1.0
PG C:GSP405 2.9 36.9 1.0
O3B C:GSP405 3.3 31.2 1.0
PB C:GSP405 3.5 26.6 1.0
CB C:SER54 3.6 26.1 1.0
O3G C:GSP405 3.7 37.0 1.0
N C:THR204 3.9 48.5 1.0
CG2 C:THR204 3.9 44.3 1.0
CA C:THR204 4.0 50.0 1.0
OD2 C:ASP223 4.1 51.2 1.0
O C:VAL202 4.3 41.0 1.0
S1G C:GSP405 4.3 37.5 1.0
N C:SER54 4.4 24.6 1.0
O3A C:GSP405 4.5 26.6 1.0
O2A C:GSP405 4.5 22.9 1.0
CA C:SER54 4.6 25.8 1.0
O1B C:GSP405 4.6 20.3 1.0
OD1 C:ASP223 4.7 50.0 1.0
O C:VAL224 4.7 39.2 1.0
C C:LEU203 4.7 46.3 1.0
PA C:GSP405 4.8 26.7 1.0
CG C:ASP223 4.8 50.6 1.0
O1A C:GSP405 4.8 24.1 1.0

Reference:

J.J.Tesmer, R.K.Sunahara, R.A.Johnson, G.Gosselin, A.G.Gilman, S.R.Sprang. Two-Metal-Ion Catalysis in Adenylyl Cyclase. Science V. 285 756 1999.
ISSN: ISSN 0036-8075
PubMed: 10427002
DOI: 10.1126/SCIENCE.285.5428.756
Page generated: Tue Aug 13 02:29:05 2024

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