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Magnesium in PDB 5sh5: Crystal Structure of Human Phosphodiesterase 10 in Complex with 2- Amino-4-Cyclohexyloxyquinoline-3-Carbonitrile

Enzymatic activity of Crystal Structure of Human Phosphodiesterase 10 in Complex with 2- Amino-4-Cyclohexyloxyquinoline-3-Carbonitrile

All present enzymatic activity of Crystal Structure of Human Phosphodiesterase 10 in Complex with 2- Amino-4-Cyclohexyloxyquinoline-3-Carbonitrile:
3.1.4.17;

Protein crystallography data

The structure of Crystal Structure of Human Phosphodiesterase 10 in Complex with 2- Amino-4-Cyclohexyloxyquinoline-3-Carbonitrile, PDB code: 5sh5 was solved by C.Joseph, J.Benz, A.Flohr, C.Riemer, M.G.Rudolph, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 43.44 / 2.30
Space group H 3
Cell size a, b, c (Å), α, β, γ (°) 135.028, 135.028, 234.735, 90, 90, 120
R / Rfree (%) 18 / 23.2

Other elements in 5sh5:

The structure of Crystal Structure of Human Phosphodiesterase 10 in Complex with 2- Amino-4-Cyclohexyloxyquinoline-3-Carbonitrile 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 2- Amino-4-Cyclohexyloxyquinoline-3-Carbonitrile (pdb code 5sh5). 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 2- Amino-4-Cyclohexyloxyquinoline-3-Carbonitrile, PDB code: 5sh5:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in 5sh5

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Magnesium binding site 1 out of 4 in the Crystal Structure of Human Phosphodiesterase 10 in Complex with 2- Amino-4-Cyclohexyloxyquinoline-3-Carbonitrile


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 2- Amino-4-Cyclohexyloxyquinoline-3-Carbonitrile within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg802

b:36.6
occ:1.00
 O A:HOH909 2.0 32.7 1.0
O A:HOH956 2.0 34.0 1.0
O A:HOH926 2.0 33.0 1.0
OD1 A:ASP564 2.1 34.0 1.0
O A:HOH940 2.1 31.2 1.0
O A:HOH921 2.1 36.5 1.0
CG A:ASP564 3.1 36.4 1.0
OD2 A:ASP564 3.4 35.3 1.0
ZN A:ZN801 3.8 41.7 1.0
OE2 A:GLU592 3.9 43.7 1.0
O A:HOH952 4.0 37.5 1.0
O A:HOH941 4.1 51.7 1.0
NE2 A:HIS595 4.1 38.1 1.0
CD2 A:HIS567 4.2 42.5 1.0
OG1 A:THR633 4.3 38.1 1.0
CD2 A:HIS595 4.3 37.0 1.0
O A:HIS563 4.3 34.4 1.0
CD2 A:HIS563 4.3 31.9 1.0
O A:THR633 4.4 40.2 1.0
NE2 A:HIS567 4.4 42.9 1.0
OD2 A:ASP674 4.4 47.2 1.0
CB A:ASP564 4.4 35.8 1.0
NE2 A:HIS525 4.7 37.2 1.0
NE2 A:HIS563 4.7 34.4 1.0
CD2 A:HIS525 4.7 38.7 1.0
CD A:GLU592 4.7 41.6 1.0
CB A:THR633 4.7 37.1 1.0
CG A:GLU592 4.8 40.1 1.0
CA A:ASP564 4.8 37.8 1.0
O A:HOH959 5.0 42.9 1.0

Magnesium binding site 2 out of 4 in 5sh5

Go back to Magnesium Binding Sites List in 5sh5
Magnesium binding site 2 out of 4 in the Crystal Structure of Human Phosphodiesterase 10 in Complex with 2- Amino-4-Cyclohexyloxyquinoline-3-Carbonitrile


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 2- Amino-4-Cyclohexyloxyquinoline-3-Carbonitrile within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg802

b:33.3
occ:1.00
 O B:HOH919 1.9 29.9 1.0
O B:HOH928 2.0 36.3 1.0
O B:HOH940 2.0 30.9 1.0
OD1 B:ASP564 2.1 29.4 1.0
O B:HOH904 2.1 29.7 1.0
O B:HOH951 2.1 29.0 1.0
CG B:ASP564 3.2 30.2 1.0
OD2 B:ASP564 3.6 34.0 1.0
ZN B:ZN801 3.9 39.9 1.0
OE2 B:GLU592 3.9 36.6 1.0
O B:HOH939 4.1 36.4 1.0
NE2 B:HIS595 4.1 36.0 1.0
OG1 B:THR633 4.2 38.8 1.0
O B:HOH942 4.2 48.8 1.0
CD2 B:HIS563 4.3 31.8 1.0
CD2 B:HIS567 4.3 32.0 1.0
NE2 B:HIS567 4.3 32.1 1.0
O B:HIS563 4.4 39.1 1.0
CD2 B:HIS595 4.4 39.6 1.0
OD2 B:ASP674 4.4 46.0 1.0
O B:THR633 4.5 35.0 1.0
CB B:ASP564 4.5 30.3 1.0
NE2 B:HIS563 4.6 29.9 1.0
CG B:GLU592 4.6 38.5 1.0
CB B:THR633 4.7 37.8 1.0
CD B:GLU592 4.7 38.2 1.0
NE2 B:HIS525 4.7 38.4 1.0
CD2 B:HIS525 4.7 40.6 1.0
CA B:ASP564 4.8 32.2 1.0

Magnesium binding site 3 out of 4 in 5sh5

Go back to Magnesium Binding Sites List in 5sh5
Magnesium binding site 3 out of 4 in the Crystal Structure of Human Phosphodiesterase 10 in Complex with 2- Amino-4-Cyclohexyloxyquinoline-3-Carbonitrile


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 2- Amino-4-Cyclohexyloxyquinoline-3-Carbonitrile within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg802

b:35.2
occ:1.00
 O C:HOH911 1.9 39.3 1.0
O C:HOH944 2.0 38.9 1.0
O C:HOH960 2.1 36.2 1.0
O C:HOH929 2.1 33.9 1.0
OD1 C:ASP564 2.1 40.6 1.0
O C:HOH932 2.2 31.3 1.0
CG C:ASP564 3.1 37.5 1.0
OD2 C:ASP564 3.5 39.0 1.0
ZN C:ZN801 3.8 44.1 1.0
O C:HOH955 3.9 37.4 1.0
NE2 C:HIS595 4.1 38.8 1.0
CD2 C:HIS567 4.1 38.9 1.0
CD2 C:HIS563 4.2 35.8 1.0
OE2 C:GLU592 4.2 39.8 1.0
O C:HOH943 4.3 45.8 1.0
NE2 C:HIS567 4.3 39.5 1.0
OG1 C:THR633 4.3 38.6 1.0
CD2 C:HIS595 4.3 38.1 1.0
O C:HIS563 4.4 38.5 1.0
OD2 C:ASP674 4.4 40.7 1.0
CB C:ASP564 4.5 37.3 1.0
O C:THR633 4.5 38.4 1.0
NE2 C:HIS563 4.6 36.4 1.0
CD2 C:HIS525 4.7 45.1 1.0
CB C:THR633 4.7 41.2 1.0
NE2 C:HIS525 4.7 44.3 1.0
CA C:ASP564 4.7 35.8 1.0
CG C:GLU592 4.8 37.4 1.0
CD C:GLU592 4.9 39.8 1.0

Magnesium binding site 4 out of 4 in 5sh5

Go back to Magnesium Binding Sites List in 5sh5
Magnesium binding site 4 out of 4 in the Crystal Structure of Human Phosphodiesterase 10 in Complex with 2- Amino-4-Cyclohexyloxyquinoline-3-Carbonitrile


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 2- Amino-4-Cyclohexyloxyquinoline-3-Carbonitrile within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg802

b:46.0
occ:1.00
 O D:HOH924 2.1 42.4 1.0
O D:HOH916 2.1 44.5 1.0
OD1 D:ASP564 2.1 46.5 1.0
O D:HOH906 2.1 35.8 1.0
O D:HOH919 2.1 43.0 1.0
O D:HOH927 2.2 37.2 1.0
CG D:ASP564 3.1 43.3 1.0
OD2 D:ASP564 3.3 51.7 1.0
O D:HOH935 3.8 43.5 1.0
ZN D:ZN801 3.8 49.8 1.0
O D:HOH923 4.0 38.4 1.0
NE2 D:HIS595 4.1 48.2 1.0
OE2 D:GLU592 4.2 51.8 1.0
CD2 D:HIS567 4.2 48.8 1.0
CD2 D:HIS563 4.3 40.6 1.0
NE2 D:HIS567 4.3 49.7 1.0
OG1 D:THR633 4.4 46.7 1.0
CD2 D:HIS595 4.4 48.9 1.0
CB D:ASP564 4.4 42.0 1.0
OD2 D:ASP674 4.5 54.0 1.0
O D:HIS563 4.5 43.8 1.0
CD2 D:HIS525 4.5 54.2 1.0
NE2 D:HIS525 4.6 53.1 1.0
O D:THR633 4.6 46.5 1.0
NE2 D:HIS563 4.8 42.5 1.0
CA D:ASP564 4.8 41.9 1.0
CB D:THR633 4.8 44.3 1.0
CG D:GLU592 4.8 48.9 1.0
CD D:GLU592 4.9 50.8 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 03:54:37 2024

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