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Magnesium in PDB 1cjt: Complex of Gs-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Beta-L-2',3'-Dideoxyatp, Mn, and Mg

Enzymatic activity of Complex of Gs-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Beta-L-2',3'-Dideoxyatp, Mn, and Mg

All present enzymatic activity of Complex of Gs-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Beta-L-2',3'-Dideoxyatp, Mn, 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 Beta-L-2',3'-Dideoxyatp, Mn, and Mg, PDB code: 1cjt 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 / 2.80
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 118.200, 134.200, 71.300, 90.00, 90.00, 90.00
R / Rfree (%) 20.6 / 25.2

Other elements in 1cjt:

The structure of Complex of Gs-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Beta-L-2',3'-Dideoxyatp, Mn, and Mg 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 Beta-L-2',3'-Dideoxyatp, Mn, and Mg (pdb code 1cjt). 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 Beta-L-2',3'-Dideoxyatp, Mn, and Mg, PDB code: 1cjt:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 1cjt

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

b:51.2
occ:1.00
 OD1 A:ASP440 2.0 38.1 1.0
O2A A:DAD102 2.1 35.7 1.0
OD1 A:ASP396 2.4 40.5 1.0
O A:HOH57 2.9 33.1 1.0
CG A:ASP440 3.0 38.0 1.0
CG A:ASP396 3.2 35.4 1.0
OD2 A:ASP396 3.2 33.9 1.0
OD2 A:ASP440 3.3 36.2 1.0
MN A:MN582 3.3 26.1 1.0
PA A:DAD102 3.4 33.9 1.0
C5' A:DAD102 3.5 35.3 1.0
O5' A:DAD102 3.9 38.8 1.0
C4' A:DAD102 4.0 35.3 1.0
O4' A:DAD102 4.1 33.5 1.0
O1A A:DAD102 4.2 37.2 1.0
CB A:CYS441 4.3 37.1 1.0
N A:CYS441 4.3 35.8 1.0
CB A:ASP440 4.4 33.1 1.0
O3A A:DAD102 4.4 33.9 1.0
O2G A:DAD102 4.6 38.3 1.0
C A:ASP440 4.6 36.3 1.0
O A:LEU438 4.6 27.5 1.0
CB A:ASP396 4.6 34.7 1.0
O1B A:DAD102 4.6 31.4 1.0
CA A:CYS441 4.7 35.9 1.0
N A:ASP440 4.7 34.4 1.0
CA A:ASP440 4.8 34.1 1.0

Magnesium binding site 2 out of 2 in 1cjt

Go back to Magnesium Binding Sites List in 1cjt
Magnesium binding site 2 out of 2 in the Complex of Gs-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Beta-L-2',3'-Dideoxyatp, Mn, 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 Beta-L-2',3'-Dideoxyatp, Mn, and Mg within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg403

b:3.5
occ:1.00
 O2B C:GSP405 1.9 23.2 1.0
O2G C:GSP405 1.9 27.0 1.0
O C:HOH412 2.0 2.0 1.0
O C:HOH415 2.1 31.6 1.0
OG C:SER54 2.1 24.4 1.0
OG1 C:THR204 2.2 32.7 1.0
PG C:GSP405 3.0 30.5 1.0
PB C:GSP405 3.0 22.1 1.0
O3B C:GSP405 3.0 23.3 1.0
CB C:THR204 3.2 32.4 1.0
CB C:SER54 3.2 25.6 1.0
N C:SER54 3.9 21.6 1.0
O3A C:GSP405 3.9 25.1 1.0
O3G C:GSP405 3.9 28.2 1.0
O2A C:GSP405 4.0 24.1 1.0
N C:THR204 4.1 34.9 1.0
O1B C:GSP405 4.1 19.2 1.0
CA C:SER54 4.1 25.4 1.0
CG2 C:THR204 4.2 30.8 1.0
CA C:THR204 4.2 36.3 1.0
PA C:GSP405 4.3 28.8 1.0
OD2 C:ASP223 4.3 39.3 1.0
O1A C:GSP405 4.4 28.5 1.0
S1G C:GSP405 4.4 36.2 1.0
OD1 C:ASP223 4.5 44.1 1.0
O C:VAL202 4.6 26.7 1.0
O C:VAL224 4.7 32.5 1.0
CG C:ASP223 4.9 41.8 1.0
CB C:LYS53 4.9 21.8 1.0
C C:LYS53 5.0 21.0 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 02:29:07 2024

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