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Zinc 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:

Magnesium (Mg) 2 atoms
Chlorine (Cl) 1 atom

Zinc Binding Sites:

The binding sites of Zinc 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 Zinc atom.
In total 2 binding sites of Zinc 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 Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 1cjv

Go back to Zinc Binding Sites List in 1cjv
Zinc 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 Zinc with other atoms in the Zn 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:Zn581

b:70.6
occ:1.00
 O2A A:DAD102 2.4 41.7 1.0
OD1 A:ASP396 2.7 43.0 1.0
OD1 A:ASP440 2.7 34.3 1.0
O A:HOH57 2.9 24.8 1.0
PA A:DAD102 3.4 42.7 1.0
CG A:ASP396 3.5 42.0 1.0
OD2 A:ASP396 3.6 42.4 1.0
CG A:ASP440 3.6 31.4 1.0
C5' A:DAD102 3.7 40.4 1.0
MG A:MG582 3.7 16.2 1.0
O1A A:DAD102 3.8 43.2 1.0
OD2 A:ASP440 3.8 30.6 1.0
C4' A:DAD102 4.0 39.7 1.0
O5' A:DAD102 4.0 42.0 1.0
CB A:CYS441 4.1 26.4 1.0
O4' A:DAD102 4.1 38.9 1.0
N A:CYS441 4.5 28.9 1.0
O A:LEU438 4.7 26.9 1.0
O2G A:DAD102 4.7 35.8 1.0
O3A A:DAD102 4.7 42.4 1.0
CA A:CYS441 4.7 27.9 1.0
CB A:ASP396 4.8 39.1 1.0
C A:ASP440 4.9 29.5 1.0
O1B A:DAD102 4.9 39.3 1.0
CB A:ASP440 5.0 29.2 1.0

Zinc binding site 2 out of 2 in 1cjv

Go back to Zinc Binding Sites List in 1cjv
Zinc 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 Zinc with other atoms in the Zn 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:Zn405

b:73.1
occ:1.00
 ND1 C:HIS220 2.3 52.0 1.0
NH2 C:ARG42 2.5 63.2 1.0
OE2 C:GLU209 2.6 60.0 1.0
CE1 C:HIS220 3.0 54.2 1.0
O C:HOH425 3.2 16.3 1.0
CZ C:ARG42 3.4 64.9 1.0
CG C:HIS220 3.5 51.2 1.0
CD C:GLU209 3.6 58.2 1.0
NE C:ARG42 3.6 64.7 1.0
CG C:GLU209 4.0 54.0 1.0
CB C:HIS220 4.0 47.5 1.0
NE2 C:HIS220 4.2 55.2 1.0
CE C:LYS211 4.3 38.7 1.0
CZ C:PHE222 4.4 28.2 1.0
CD2 C:HIS220 4.4 53.4 1.0
NH1 C:ARG42 4.6 66.2 1.0
NZ C:LYS211 4.6 37.9 1.0
OE1 C:GLU209 4.7 58.8 1.0
CE1 C:PHE222 5.0 29.2 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 Oct 12 23:09:58 2024

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