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Magnesium in PDB 5sg2: Crystal Structure of Human Phosphodiesterase 10 in Complex with 3- Methylimidazo[4,5-F]Quinolin-2-Amine

Enzymatic activity of Crystal Structure of Human Phosphodiesterase 10 in Complex with 3- Methylimidazo[4,5-F]Quinolin-2-Amine

All present enzymatic activity of Crystal Structure of Human Phosphodiesterase 10 in Complex with 3- Methylimidazo[4,5-F]Quinolin-2-Amine:
3.1.4.17;

Protein crystallography data

The structure of Crystal Structure of Human Phosphodiesterase 10 in Complex with 3- Methylimidazo[4,5-F]Quinolin-2-Amine, PDB code: 5sg2 was solved by C.Joseph, J.Benz, A.Flohr, M.Brunner, M.G.Rudolph, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 41.37 / 2.15
Space group H 3
Cell size a, b, c (Å), α, β, γ (°) 134.819, 134.819, 234.13, 90, 90, 120
R / Rfree (%) 18.5 / 24.3

Other elements in 5sg2:

The structure of Crystal Structure of Human Phosphodiesterase 10 in Complex with 3- Methylimidazo[4,5-F]Quinolin-2-Amine also contains other interesting chemical elements:

Zinc (Zn) 4 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Human Phosphodiesterase 10 in Complex with 3- Methylimidazo[4,5-F]Quinolin-2-Amine (pdb code 5sg2). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Crystal Structure of Human Phosphodiesterase 10 in Complex with 3- Methylimidazo[4,5-F]Quinolin-2-Amine, PDB code: 5sg2:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in 5sg2

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Magnesium binding site 1 out of 4 in the Crystal Structure of Human Phosphodiesterase 10 in Complex with 3- Methylimidazo[4,5-F]Quinolin-2-Amine


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Human Phosphodiesterase 10 in Complex with 3- Methylimidazo[4,5-F]Quinolin-2-Amine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg802

b:33.9
occ:1.00
 O A:HOH976 1.9 28.1 1.0
O A:HOH907 2.1 31.6 1.0
O A:HOH959 2.1 24.0 1.0
OD1 A:ASP564 2.1 28.7 1.0
O A:HOH948 2.1 30.2 1.0
O A:HOH929 2.2 29.3 1.0
CG A:ASP564 3.1 32.9 1.0
OD2 A:ASP564 3.4 34.4 1.0
ZN A:ZN801 3.8 36.2 1.0
O A:HOH963 4.0 32.8 1.0
O A:HOH951 4.0 47.5 1.0
O A:HOH925 4.1 43.8 1.0
NE2 A:HIS595 4.1 28.2 1.0
OE2 A:GLU592 4.1 36.8 1.0
CD2 A:HIS567 4.2 37.9 1.0
CD2 A:HIS563 4.3 29.1 1.0
CD2 A:HIS595 4.4 28.3 1.0
OG1 A:THR633 4.4 33.0 1.0
NE2 A:HIS567 4.4 37.6 1.0
CB A:ASP564 4.4 32.5 1.0
CD2 A:HIS525 4.5 36.3 1.0
O A:HIS563 4.5 32.9 1.0
O A:THR633 4.5 36.2 1.0
NE2 A:HIS525 4.6 35.1 1.0
OD2 A:ASP674 4.6 44.7 1.0
NE2 A:HIS563 4.7 30.0 1.0
CA A:ASP564 4.8 32.8 1.0
CB A:THR633 4.8 34.5 1.0
CG A:GLU592 4.9 34.6 1.0
CD A:GLU592 4.9 37.5 1.0
O A:HOH981 5.0 46.5 1.0

Magnesium binding site 2 out of 4 in 5sg2

Go back to Magnesium Binding Sites List in 5sg2
Magnesium binding site 2 out of 4 in the Crystal Structure of Human Phosphodiesterase 10 in Complex with 3- Methylimidazo[4,5-F]Quinolin-2-Amine


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of Human Phosphodiesterase 10 in Complex with 3- Methylimidazo[4,5-F]Quinolin-2-Amine within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg802

b:26.2
occ:1.00
 O B:HOH933 1.9 25.1 1.0
O B:HOH948 1.9 30.5 1.0
O B:HOH943 2.0 22.8 1.0
O B:HOH978 2.0 30.9 1.0
O B:HOH908 2.1 22.6 1.0
OD1 B:ASP564 2.2 30.4 1.0
CG B:ASP564 3.2 29.6 1.0
OD2 B:ASP564 3.5 31.1 1.0
ZN B:ZN801 3.8 36.2 1.0
OE2 B:GLU592 4.0 29.7 1.0
O B:HOH955 4.1 42.8 1.0
NE2 B:HIS595 4.1 37.4 1.0
CD2 B:HIS567 4.2 30.9 1.0
O B:HOH974 4.3 38.9 1.0
CD2 B:HIS563 4.3 32.0 1.0
NE2 B:HIS567 4.3 30.9 1.0
OG1 B:THR633 4.3 32.6 1.0
OD2 B:ASP674 4.3 35.7 1.0
O B:THR633 4.4 29.2 1.0
CD2 B:HIS595 4.4 37.0 1.0
O B:HIS563 4.5 32.2 1.0
CB B:ASP564 4.5 30.3 1.0
NE2 B:HIS563 4.5 31.6 1.0
CD2 B:HIS525 4.6 33.3 1.0
CB B:THR633 4.7 31.9 1.0
NE2 B:HIS525 4.7 33.9 1.0
CG B:GLU592 4.8 31.1 1.0
CD B:GLU592 4.8 29.5 1.0
CA B:ASP564 4.9 31.6 1.0

Magnesium binding site 3 out of 4 in 5sg2

Go back to Magnesium Binding Sites List in 5sg2
Magnesium binding site 3 out of 4 in the Crystal Structure of Human Phosphodiesterase 10 in Complex with 3- Methylimidazo[4,5-F]Quinolin-2-Amine


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Crystal Structure of Human Phosphodiesterase 10 in Complex with 3- Methylimidazo[4,5-F]Quinolin-2-Amine within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg802

b:28.2
occ:1.00
 OD1 C:ASP564 2.0 27.4 1.0
O C:HOH927 2.0 19.5 1.0
O C:HOH935 2.1 29.9 1.0
O C:HOH936 2.1 21.1 1.0
O C:HOH990 2.1 30.5 1.0
O C:HOH1003 2.2 26.3 1.0
CG C:ASP564 3.0 29.1 1.0
OD2 C:ASP564 3.3 26.2 1.0
O C:HOH1002 3.5 57.3 1.0
O C:HOH988 3.7 42.6 1.0
ZN C:ZN801 3.8 34.0 1.0
OE2 C:GLU592 3.9 33.6 1.0
O C:HOH939 4.1 32.0 1.0
CD2 C:HIS567 4.1 34.3 1.0
OG1 C:THR633 4.2 27.7 1.0
NE2 C:HIS595 4.2 29.5 1.0
OD2 C:ASP674 4.2 32.7 1.0
CD2 C:HIS563 4.2 31.0 1.0
NE2 C:HIS567 4.4 34.7 1.0
CB C:ASP564 4.4 29.5 1.0
CD2 C:HIS595 4.5 27.1 1.0
O C:THR633 4.5 31.7 1.0
O C:HIS563 4.6 30.7 1.0
NE2 C:HIS563 4.6 31.7 1.0
CB C:THR633 4.7 30.1 1.0
NE2 C:HIS525 4.7 33.3 1.0
CD2 C:HIS525 4.8 33.8 1.0
CD C:GLU592 4.8 31.6 1.0
CA C:ASP564 4.8 32.0 1.0
CG C:GLU592 4.8 31.5 1.0

Magnesium binding site 4 out of 4 in 5sg2

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Magnesium binding site 4 out of 4 in the Crystal Structure of Human Phosphodiesterase 10 in Complex with 3- Methylimidazo[4,5-F]Quinolin-2-Amine


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Crystal Structure of Human Phosphodiesterase 10 in Complex with 3- Methylimidazo[4,5-F]Quinolin-2-Amine within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg802

b:42.8
occ:1.00
 O D:HOH943 2.0 37.2 1.0
O D:HOH937 2.0 35.8 1.0
O D:HOH925 2.1 39.6 1.0
O D:HOH913 2.1 44.1 1.0
OD1 D:ASP564 2.2 42.9 1.0
O D:HOH904 2.4 37.8 1.0
CG D:ASP564 3.1 42.6 1.0
OD2 D:ASP564 3.3 45.5 1.0
O D:HOH946 3.6 52.0 1.0
ZN D:ZN801 3.8 52.2 1.0
O D:HOH940 3.9 40.8 1.0
OE2 D:GLU592 3.9 49.4 1.0
CD2 D:HIS567 4.0 44.8 1.0
NE2 D:HIS567 4.1 43.0 1.0
NE2 D:HIS595 4.1 44.0 1.0
OG1 D:THR633 4.3 44.0 1.0
O D:THR633 4.4 45.6 1.0
CD2 D:HIS595 4.5 42.5 1.0
CB D:ASP564 4.5 45.6 1.0
CD2 D:HIS525 4.5 52.5 1.0
CD2 D:HIS563 4.5 40.0 1.0
O D:HIS563 4.5 42.2 1.0
OD2 D:ASP674 4.6 48.9 1.0
NE2 D:HIS525 4.6 53.3 1.0
CB D:THR633 4.8 48.6 1.0
CA D:ASP564 4.9 42.1 1.0
NE2 D:HIS563 4.9 36.2 1.0
CD D:GLU592 4.9 51.3 1.0

Reference:

A.Flohr, D.Schlatter, B.Kuhn, M.G.Rudolph. Crystal Structure of A Human Phosphodiesterase 10 Complex To Be Published.
Page generated: Mon Sep 30 03:40:50 2024

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