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Manganese in PDB 2gvd: Complex of Gs- with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Tnp-Atp and Mn

Enzymatic activity of Complex of Gs- with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Tnp-Atp and Mn

All present enzymatic activity of Complex of Gs- with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Tnp-Atp and Mn:
4.6.1.1;

Protein crystallography data

The structure of Complex of Gs- with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Tnp-Atp and Mn, PDB code: 2gvd was solved by T.-C.Mou, S.R.Sprang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 14.96 / 2.90
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 118.200, 133.400, 70.600, 90.00, 90.00, 90.00
R / Rfree (%) 24.5 / 27.9

Other elements in 2gvd:

The structure of Complex of Gs- with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Tnp-Atp and Mn also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Manganese Binding Sites:

The binding sites of Manganese atom in the Complex of Gs- with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Tnp-Atp and Mn (pdb code 2gvd). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 3 binding sites of Manganese where determined in the Complex of Gs- with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Tnp-Atp and Mn, PDB code: 2gvd:
Jump to Manganese binding site number: 1; 2; 3;

Manganese binding site 1 out of 3 in 2gvd

Go back to Manganese Binding Sites List in 2gvd
Manganese binding site 1 out of 3 in the Complex of Gs- with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Tnp-Atp and Mn


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Complex of Gs- with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Tnp-Atp and Mn within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn581

b:56.8
occ:1.00
OD1 A:ASP440 2.4 49.7 1.0
OD1 A:ASP396 3.3 44.5 1.0
OD2 A:ASP396 3.3 38.0 1.0
CG A:ASP440 3.4 47.2 1.0
CG A:ASP396 3.6 38.5 1.0
O1A A:128584 3.7 64.5 1.0
MN A:MN582 3.8 20.4 1.0
OD2 A:ASP440 3.8 46.8 1.0
C5' A:128584 3.9 70.0 1.0
CB A:CYS441 4.2 48.2 1.0
N A:CYS441 4.4 45.4 1.0
O A:LEU438 4.5 37.9 1.0
C30 A:FKP583 4.5 64.1 1.0
C A:ASP440 4.6 45.6 1.0
O4' A:128584 4.6 70.5 1.0
N A:ASP440 4.6 45.0 1.0
CB A:ASP440 4.7 46.3 1.0
O5' A:128584 4.8 72.2 1.0
CA A:CYS441 4.8 46.2 1.0
PA A:128584 4.9 71.9 1.0
C4' A:128584 4.9 69.4 1.0
CA A:ASP440 4.9 46.4 1.0
CB A:ASP396 4.9 39.7 1.0
O2B A:128584 5.0 69.3 1.0
O A:ASP440 5.0 44.5 1.0

Manganese binding site 2 out of 3 in 2gvd

Go back to Manganese Binding Sites List in 2gvd
Manganese binding site 2 out of 3 in the Complex of Gs- with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Tnp-Atp and Mn


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Complex of Gs- with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Tnp-Atp and Mn within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn582

b:20.4
occ:1.00
OD2 A:ASP440 2.2 46.8 1.0
O2B A:128584 2.3 69.3 1.0
OD2 A:ASP396 2.4 38.0 1.0
O A:ILE397 2.4 44.7 1.0
O3B A:128584 2.6 66.0 1.0
OD1 A:ASP396 2.6 44.5 1.0
CG A:ASP396 2.7 38.5 1.0
PB A:128584 2.7 66.8 1.0
CG A:ASP440 3.2 47.2 1.0
C A:ILE397 3.4 47.5 1.0
OD1 A:ASP440 3.5 49.7 1.0
N A:ILE397 3.7 47.2 1.0
O1B A:128584 3.8 60.2 1.0
MN A:MN581 3.8 56.8 1.0
O3A A:128584 3.9 68.5 1.0
PG A:128584 4.0 65.9 1.0
CA A:ILE397 4.0 47.2 1.0
CB A:ASP396 4.0 39.7 1.0
C A:ASP396 4.2 44.5 1.0
O1A A:128584 4.3 64.5 1.0
CB A:ILE397 4.3 47.2 1.0
O2G A:128584 4.4 66.4 1.0
C5' A:128584 4.4 70.0 1.0
CB A:ASP440 4.5 46.3 1.0
N A:GLU398 4.5 50.0 1.0
CA A:ASP396 4.6 40.3 1.0
PA A:128584 4.7 71.9 1.0
CB A:PHE400 4.7 56.5 1.0
NH1 A:ARG484 4.8 46.4 1.0
N A:GLY399 4.8 55.3 1.0
O1G A:128584 4.8 70.2 1.0
CA A:GLU398 4.8 54.0 1.0
O A:ASP440 4.9 44.5 1.0
N A:PHE400 4.9 57.5 1.0
O A:ASP396 4.9 45.2 1.0

Manganese binding site 3 out of 3 in 2gvd

Go back to Manganese Binding Sites List in 2gvd
Manganese binding site 3 out of 3 in the Complex of Gs- with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Tnp-Atp and Mn


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Complex of Gs- with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Tnp-Atp and Mn within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mn396

b:40.2
occ:1.00
O2B C:GSP395 2.1 38.3 1.0
O2G C:GSP395 2.3 60.9 1.0
OG1 C:THR204 2.3 30.9 1.0
OG C:SER54 2.3 26.1 1.0
CB C:THR204 3.0 29.7 1.0
PG C:GSP395 3.1 59.7 1.0
PB C:GSP395 3.2 34.4 1.0
CB C:SER54 3.3 24.8 1.0
O3G C:GSP395 3.4 61.6 1.0
O3B C:GSP395 3.5 49.1 1.0
OD1 C:ASP223 3.7 53.6 1.0
N C:SER54 3.8 22.1 1.0
CG2 C:THR204 3.9 27.8 1.0
CA C:SER54 4.1 24.2 1.0
O2A C:GSP395 4.1 28.1 1.0
O1B C:GSP395 4.1 37.4 1.0
N C:THR204 4.2 34.0 1.0
OD2 C:ASP223 4.2 53.9 1.0
CA C:THR204 4.2 32.6 1.0
O3A C:GSP395 4.3 34.6 1.0
CG C:ASP223 4.4 49.2 1.0
PA C:GSP395 4.5 30.4 1.0
O C:VAL202 4.5 33.3 1.0
CE C:LYS53 4.6 23.1 1.0
CB C:LYS53 4.6 22.3 1.0
O1A C:GSP395 4.6 34.6 1.0
O C:VAL224 4.9 29.4 1.0
S1G C:GSP395 4.9 56.7 1.0
C C:LYS53 4.9 21.4 1.0

Reference:

T.-C.Mou, A.Gille, S.Suryanarayana, M.Richter, R.Seifert, S.R.Sprang. Broad Specificity of Mammalian Adenylyl Cyclase For Interaction with 2',3'-Substituted Purine- and Pyrimidine Nucleotide Inhibitors. Mol.Pharmacol. V. 70 878 2006.
ISSN: ISSN 0026-895X
PubMed: 16766715
DOI: 10.1124/MOL.106.026427
Page generated: Tue Dec 15 04:02:23 2020

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