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

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

All present enzymatic activity of Complex of Gs-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Beta-L-2',3'-Dideoxyatp, Mg, and Zn:
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, Mg, and Zn, PDB code: 1cjv 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 (°) 118.400, 134.200, 71.600, 90.00, 90.00, 90.00
R / Rfree (%) 20.3 / 26.2

Other elements in 1cjv:

The structure of Complex of Gs-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Beta-L-2',3'-Dideoxyatp, Mg, and Zn also contains other interesting chemical elements:

Chlorine (Cl) 1 atom
Zinc (Zn) 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 Beta-L-2',3'-Dideoxyatp, Mg, and Zn (pdb code 1cjv). 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, Mg, and Zn, PDB code: 1cjv:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 1cjv

Go back to Magnesium Binding Sites List in 1cjv
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, Mg, and Zn


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, Mg, and Zn within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg582

b:16.2
occ:1.00
 OD2 A:ASP396 2.0 42.4 1.0
OD2 A:ASP440 2.1 30.6 1.0
O2G A:DAD102 2.2 35.8 1.0
O1B A:DAD102 2.2 39.3 1.0
O A:ILE397 2.2 36.4 1.0
O2A A:DAD102 2.3 41.7 1.0
CG A:ASP396 2.9 42.0 1.0
CG A:ASP440 3.2 31.4 1.0
OD1 A:ASP396 3.2 43.0 1.0
PB A:DAD102 3.3 39.5 1.0
PG A:DAD102 3.4 40.0 1.0
C A:ILE397 3.4 38.0 1.0
PA A:DAD102 3.5 42.7 1.0
OD1 A:ASP440 3.6 34.3 1.0
O3B A:DAD102 3.6 40.0 1.0
O3A A:DAD102 3.6 42.4 1.0
ZN A:ZN581 3.7 70.6 1.0
O3G A:DAD102 4.0 40.9 1.0
N A:ILE397 4.0 36.9 1.0
CB A:PHE400 4.1 40.4 1.0
CA A:ILE397 4.2 37.7 1.0
CB A:ASP396 4.2 39.1 1.0
N A:PHE400 4.3 41.7 1.0
O5' A:DAD102 4.4 42.0 1.0
C A:ASP396 4.4 36.8 1.0
CB A:ASP440 4.5 29.2 1.0
N A:GLU398 4.5 39.7 1.0
N A:GLY399 4.5 39.9 1.0
CB A:ILE397 4.6 39.2 1.0
C5' A:DAD102 4.7 40.4 1.0
CA A:GLU398 4.7 41.1 1.0
O1G A:DAD102 4.7 39.9 1.0
O1A A:DAD102 4.7 43.2 1.0
O2B A:DAD102 4.7 38.5 1.0
NH2 A:ARG484 4.7 31.1 1.0
CA A:ASP396 4.8 36.5 1.0
O A:ASP396 4.9 38.2 1.0
C A:GLU398 4.9 40.2 1.0
CA A:PHE400 4.9 41.7 1.0

Magnesium binding site 2 out of 2 in 1cjv

Go back to Magnesium Binding Sites List in 1cjv
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, Mg, and Zn


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, Mg, and Zn within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg403

b:7.0
occ:1.00
 O C:HOH414 1.8 11.1 1.0
O2G C:GSP406 1.9 26.6 1.0
O2B C:GSP406 1.9 18.4 1.0
O C:HOH412 1.9 2.0 1.0
OG1 C:THR204 2.2 31.1 1.0
OG C:SER54 2.3 18.7 1.0
PG C:GSP406 2.8 29.0 1.0
O3B C:GSP406 2.9 23.6 1.0
PB C:GSP406 2.9 17.2 1.0
CB C:SER54 3.2 17.5 1.0
CB C:THR204 3.5 31.1 1.0
O3G C:GSP406 3.6 26.7 1.0
N C:SER54 3.7 15.2 1.0
O3A C:GSP406 3.9 17.0 1.0
O1B C:GSP406 4.0 14.4 1.0
CA C:SER54 4.0 16.8 1.0
O2A C:GSP406 4.1 15.9 1.0
N C:THR204 4.2 31.2 1.0
PA C:GSP406 4.3 16.8 1.0
CG2 C:THR204 4.3 29.9 1.0
OD1 C:ASP223 4.4 42.5 1.0
O1A C:GSP406 4.4 16.3 1.0
S1G C:GSP406 4.4 32.2 1.0
CA C:THR204 4.5 32.7 1.0
OD2 C:ASP223 4.6 36.9 1.0
O C:VAL224 4.6 24.8 1.0
O C:VAL202 4.7 22.1 1.0
CB C:LYS53 4.8 16.4 1.0
C C:LYS53 4.9 14.4 1.0
CG C:ASP223 4.9 38.0 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 02:29:13 2024

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