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

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: Sat Aug 9 20:24:00 2025

Last articles

Mg in 6DP4
Mg in 6DP3
Mg in 6DP2
Mg in 6DP1
Mg in 6DP0
Mg in 6DOZ
Mg in 6DOX
Mg in 6DOW
Mg in 6DOV
Mg in 6DOU
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy