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Magnesium in PDB 1u0h: Structural Basis For the Inhibition of Mammalian Adenylyl Cyclase By Mant-Gtp

Enzymatic activity of Structural Basis For the Inhibition of Mammalian Adenylyl Cyclase By Mant-Gtp

All present enzymatic activity of Structural Basis For the Inhibition of Mammalian Adenylyl Cyclase By Mant-Gtp:
4.6.1.1;

Protein crystallography data

The structure of Structural Basis For the Inhibition of Mammalian Adenylyl Cyclase By Mant-Gtp, PDB code: 1u0h was solved by T.C.Mou, A.Gille, R.J.Seifert, S.R.Sprang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 15.00 / 2.90
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 118.400, 133.000, 70.400, 90.00, 90.00, 90.00
R / Rfree (%) 24.5 / 28

Other elements in 1u0h:

The structure of Structural Basis For the Inhibition of Mammalian Adenylyl Cyclase By Mant-Gtp also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structural Basis For the Inhibition of Mammalian Adenylyl Cyclase By Mant-Gtp (pdb code 1u0h). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the Structural Basis For the Inhibition of Mammalian Adenylyl Cyclase By Mant-Gtp, PDB code: 1u0h:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in 1u0h

Go back to Magnesium Binding Sites List in 1u0h
Magnesium binding site 1 out of 3 in the Structural Basis For the Inhibition of Mammalian Adenylyl Cyclase By Mant-Gtp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structural Basis For the Inhibition of Mammalian Adenylyl Cyclase By Mant-Gtp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg581

b:38.4
occ:1.00
O3B A:ONM100 2.6 74.2 1.0
OD1 A:ASP440 2.8 57.6 1.0
O2A A:ONM100 3.1 88.1 1.0
OD1 A:ASP396 3.1 80.0 1.0
CB A:CYS441 3.2 56.5 1.0
CG A:ASP440 3.6 56.3 1.0
N A:CYS441 3.7 55.9 1.0
O A:LEU438 3.8 54.7 1.0
OD2 A:ASP440 3.9 53.0 1.0
CA A:CYS441 4.0 56.6 1.0
CG A:ASP396 4.0 75.6 1.0
OD2 A:ASP396 4.2 80.3 1.0
PB A:ONM100 4.2 78.5 1.0
PA A:ONM100 4.3 81.5 1.0
C8 A:ONM100 4.3 81.8 1.0
C A:ASP440 4.4 55.6 1.0
N A:ASP440 4.4 59.0 1.0
C5' A:ONM100 4.5 77.7 1.0
SG A:CYS441 4.5 60.7 1.0
O2B A:ONM100 4.7 79.0 1.0
CA A:ASP440 4.7 57.6 1.0
O1A A:ONM100 4.7 79.7 1.0
CB A:ASP440 4.8 56.4 1.0
N7 A:ONM100 4.8 82.4 1.0
O4' A:ONM100 4.9 72.2 1.0
O5' A:ONM100 4.9 80.4 1.0
C A:LEU438 5.0 54.0 1.0

Magnesium binding site 2 out of 3 in 1u0h

Go back to Magnesium Binding Sites List in 1u0h
Magnesium binding site 2 out of 3 in the Structural Basis For the Inhibition of Mammalian Adenylyl Cyclase By Mant-Gtp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structural Basis For the Inhibition of Mammalian Adenylyl Cyclase By Mant-Gtp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg582

b:38.2
occ:1.00
O A:ILE397 2.4 76.6 1.0
OD2 A:ASP440 2.5 53.0 1.0
OD2 A:ASP396 2.6 80.3 1.0
C A:ILE397 2.7 74.2 1.0
O1G A:ONM100 2.7 76.1 1.0
O1B A:ONM100 2.9 74.8 1.0
CG A:ASP396 3.1 75.6 1.0
N A:GLU398 3.1 75.1 1.0
N A:ILE397 3.2 67.9 1.0
CA A:GLU398 3.3 75.8 1.0
CA A:ILE397 3.5 71.9 1.0
C A:ASP396 3.5 66.9 1.0
OD1 A:ASP396 3.7 80.0 1.0
CB A:ASP396 3.7 70.6 1.0
PG A:ONM100 3.7 78.4 1.0
CG A:ASP440 3.7 56.3 1.0
PB A:ONM100 3.7 78.5 1.0
O3B A:ONM100 3.8 74.2 1.0
O2B A:ONM100 3.8 79.0 1.0
C A:GLU398 3.9 73.7 1.0
N A:GLY399 3.9 72.4 1.0
O A:ASP396 4.0 66.2 1.0
O3G A:ONM100 4.1 54.4 1.0
CA A:ASP396 4.1 66.4 1.0
CB A:ILE397 4.2 73.3 1.0
N A:PHE400 4.3 72.1 1.0
CB A:PHE400 4.3 74.2 1.0
NH2 A:ARG484 4.4 80.4 1.0
CB A:ASP440 4.5 56.4 1.0
NH1 A:ARG484 4.6 82.0 1.0
OD1 A:ASP440 4.6 57.6 1.0
CB A:GLU398 4.7 80.9 1.0
O A:GLU398 4.8 71.9 1.0
CZ A:ARG484 4.8 79.2 1.0
CA A:PHE400 4.8 73.2 1.0
O2G A:ONM100 4.9 74.6 1.0
CA A:GLY399 5.0 71.8 1.0
C A:GLY399 5.0 71.3 1.0

Magnesium binding site 3 out of 3 in 1u0h

Go back to Magnesium Binding Sites List in 1u0h
Magnesium binding site 3 out of 3 in the Structural Basis For the Inhibition of Mammalian Adenylyl Cyclase By Mant-Gtp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Structural Basis For the Inhibition of Mammalian Adenylyl Cyclase By Mant-Gtp within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg396

b:21.9
occ:1.00
OG C:SER54 2.2 41.0 1.0
O2G C:GSP395 2.3 66.2 1.0
OG1 C:THR204 2.3 40.2 1.0
O2B C:GSP395 2.5 44.5 1.0
O3G C:GSP395 2.7 67.6 1.0
PG C:GSP395 2.8 66.9 1.0
CB C:THR204 2.9 41.6 1.0
OD2 C:ASP223 3.3 51.1 1.0
CB C:SER54 3.4 39.4 1.0
OD1 C:ASP223 3.4 52.1 1.0
PB C:GSP395 3.4 45.3 1.0
O3B C:GSP395 3.6 57.0 1.0
O C:VAL224 3.7 39.3 1.0
CG2 C:THR204 3.7 38.2 1.0
CG C:ASP223 3.7 51.7 1.0
N C:SER54 3.8 29.8 1.0
CA C:SER54 4.1 33.8 1.0
O1B C:GSP395 4.1 43.1 1.0
CA C:THR204 4.2 45.1 1.0
N C:THR204 4.2 45.8 1.0
CE C:LYS53 4.2 23.9 1.0
CB C:LYS53 4.4 28.6 1.0
NZ C:LYS53 4.5 22.1 1.0
S1G C:GSP395 4.6 65.7 1.0
C C:VAL224 4.7 39.0 1.0
O3A C:GSP395 4.8 45.4 1.0
C C:LYS53 4.8 29.2 1.0
O2A C:GSP395 4.9 42.7 1.0

Reference:

T.C.Mou, A.Gille, D.A.Fancy, R.Seifert, S.R.Sprang. Structural Basis For the Inhibition of Mammalian Membrane Adenylyl Cyclase By 2 '(3')-O-(N-Methylanthraniloyl)-Guanosine 5 '-Triphosphate. J.Biol.Chem. V. 280 7253 2005.
ISSN: ISSN 0021-9258
PubMed: 15591060
DOI: 10.1074/JBC.M409076200
Page generated: Tue Aug 13 14:41:19 2024

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