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Magnesium in PDB 1azs: Complex of Gs-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase

Enzymatic activity of Complex of Gs-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase

All present enzymatic activity of Complex of Gs-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase:
4.6.1.1;

Protein crystallography data

The structure of Complex of Gs-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase, PDB code: 1azs 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 / 2.30
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 119.000, 134.050, 70.650, 90.00, 90.00, 90.00
R / Rfree (%) 21.9 / 28.2

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Complex of Gs-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase (pdb code 1azs). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Complex of Gs-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase, PDB code: 1azs:

Magnesium binding site 1 out of 1 in 1azs

Go back to Magnesium Binding Sites List in 1azs
Magnesium binding site 1 out of 1 in the Complex of Gs-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase


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 within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg403

b:28.9
occ:1.00
O C:HOH406 1.7 25.1 1.0
OG1 C:THR204 1.8 34.0 1.0
OG C:SER54 1.8 36.6 1.0
O2G C:GSP404 2.0 34.0 1.0
O C:HOH405 2.1 23.8 1.0
O2B C:GSP404 2.4 29.3 1.0
CB C:THR204 2.8 32.4 1.0
CB C:SER54 3.1 31.6 1.0
PG C:GSP404 3.3 38.3 1.0
PB C:GSP404 3.5 30.9 1.0
O3B C:GSP404 3.6 31.6 1.0
OD2 C:ASP223 3.8 65.5 1.0
N C:THR204 3.8 34.1 1.0
CG2 C:THR204 3.8 25.7 1.0
CA C:THR204 3.9 35.8 1.0
N C:SER54 4.1 28.2 1.0
CA C:SER54 4.1 30.8 1.0
O3G C:GSP404 4.1 41.3 1.0
OD1 C:ASP223 4.3 58.4 1.0
O C:VAL202 4.3 44.4 1.0
O C:VAL224 4.4 44.0 1.0
CG C:ASP223 4.4 60.4 1.0
O2A C:GSP404 4.5 31.4 1.0
O1B C:GSP404 4.5 27.6 1.0
O3A C:GSP404 4.6 30.8 1.0
C C:LEU203 4.7 38.2 1.0
S1G C:GSP404 4.8 42.7 1.0
PA C:GSP404 4.8 28.3 1.0
O1A C:GSP404 4.9 34.5 1.0

Reference:

J.J.Tesmer, R.K.Sunahara, A.G.Gilman, S.R.Sprang. Crystal Structure of the Catalytic Domains of Adenylyl Cyclase in A Complex with Gsalpha.Gtpgammas. Science V. 278 1907 1997.
ISSN: ISSN 0036-8075
PubMed: 9417641
DOI: 10.1126/SCIENCE.278.5345.1907
Page generated: Tue Aug 13 02:09:10 2024

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