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Magnesium in PDB 3hvj: Rat Catechol O-Methyltransferase in Complex with A Catechol-Type, N6- Propyladenine-Containing Bisubstrate Inhibitor

Enzymatic activity of Rat Catechol O-Methyltransferase in Complex with A Catechol-Type, N6- Propyladenine-Containing Bisubstrate Inhibitor

All present enzymatic activity of Rat Catechol O-Methyltransferase in Complex with A Catechol-Type, N6- Propyladenine-Containing Bisubstrate Inhibitor:
2.1.1.6;

Protein crystallography data

The structure of Rat Catechol O-Methyltransferase in Complex with A Catechol-Type, N6- Propyladenine-Containing Bisubstrate Inhibitor, PDB code: 3hvj was solved by A.Ehler, D.Schlatter, M.Stihle, J.Benz, M.G.Rudolph, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 45.04 / 1.79
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 55.346, 61.414, 132.500, 90.00, 90.00, 90.00
R / Rfree (%) 18.3 / 23.5

Other elements in 3hvj:

The structure of Rat Catechol O-Methyltransferase in Complex with A Catechol-Type, N6- Propyladenine-Containing Bisubstrate Inhibitor also contains other interesting chemical elements:

Fluorine (F) 2 atoms
Chlorine (Cl) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Rat Catechol O-Methyltransferase in Complex with A Catechol-Type, N6- Propyladenine-Containing Bisubstrate Inhibitor (pdb code 3hvj). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Rat Catechol O-Methyltransferase in Complex with A Catechol-Type, N6- Propyladenine-Containing Bisubstrate Inhibitor, PDB code: 3hvj:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 3hvj

Go back to Magnesium Binding Sites List in 3hvj
Magnesium binding site 1 out of 2 in the Rat Catechol O-Methyltransferase in Complex with A Catechol-Type, N6- Propyladenine-Containing Bisubstrate Inhibitor


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Rat Catechol O-Methyltransferase in Complex with A Catechol-Type, N6- Propyladenine-Containing Bisubstrate Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg265

b:17.4
occ:1.00
 OD1 A:ASP184 2.1 16.2 1.0
O34 A:7051 2.1 16.5 1.0
O A:HOH401 2.1 17.8 1.0
O32 A:7051 2.1 17.1 1.0
OD1 A:ASN213 2.1 13.7 1.0
OD2 A:ASP212 2.2 18.5 1.0
C33 A:7051 2.8 17.0 1.0
C31 A:7051 2.9 17.1 1.0
CG A:ASP184 3.0 17.1 1.0
CG A:ASN213 3.0 14.6 1.0
CG A:ASP212 3.2 17.8 1.0
OD2 A:ASP184 3.3 17.8 1.0
ND2 A:ASN213 3.3 14.9 1.0
NZ A:LYS187 3.8 12.9 1.0
CB A:ASP212 3.8 16.0 1.0
OE2 A:GLU242 4.2 16.8 1.0
C23 A:7051 4.2 14.6 1.0
C20 A:7051 4.2 16.4 1.0
OD1 A:ASP212 4.3 20.1 1.0
O A:MET83 4.3 20.4 1.0
CB A:ASN213 4.4 16.7 1.0
CB A:ASP184 4.4 17.4 1.0
CE A:LYS187 4.6 17.3 1.0
O A:ASP184 4.6 16.3 1.0
OE1 A:GLU242 4.7 13.6 1.0
NZ A:LYS89 4.7 20.6 1.0
N17 A:7051 4.8 16.4 1.0
CA A:ASP184 4.9 15.8 1.0
CD A:GLU242 4.9 17.7 1.0

Magnesium binding site 2 out of 2 in 3hvj

Go back to Magnesium Binding Sites List in 3hvj
Magnesium binding site 2 out of 2 in the Rat Catechol O-Methyltransferase in Complex with A Catechol-Type, N6- Propyladenine-Containing Bisubstrate Inhibitor


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Rat Catechol O-Methyltransferase in Complex with A Catechol-Type, N6- Propyladenine-Containing Bisubstrate Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg265

b:17.7
occ:1.00
 OD1 B:ASP184 2.0 13.8 1.0
OD2 B:ASP212 2.0 18.3 1.0
OD1 B:ASN213 2.1 16.3 1.0
O B:HOH433 2.1 15.9 1.0
O32 B:7052 2.2 18.3 1.0
O34 B:7052 2.2 17.1 1.0
C31 B:7052 3.0 16.8 1.0
C33 B:7052 3.0 15.4 1.0
CG B:ASP184 3.0 17.3 1.0
CG B:ASN213 3.0 15.6 1.0
CG B:ASP212 3.1 16.7 1.0
OD2 B:ASP184 3.2 19.6 1.0
ND2 B:ASN213 3.3 13.6 1.0
CB B:ASP212 3.7 16.5 1.0
NZ B:LYS187 3.7 19.0 1.0
O B:HOH408 4.1 31.9 1.0
OD1 B:ASP212 4.1 19.8 1.0
OE2 B:GLU242 4.2 17.4 1.0
C23 B:7052 4.3 16.5 1.0
O B:MET83 4.3 19.9 1.0
C20 B:7052 4.3 16.3 1.0
CB B:ASP184 4.4 16.4 1.0
CB B:ASN213 4.4 16.4 1.0
CE B:LYS187 4.6 18.5 1.0
CG2 B:VAL85 4.7 17.2 1.0
OE1 B:GLU242 4.7 18.2 1.0
NZ B:LYS89 4.8 19.4 1.0
O B:ASP184 4.8 15.4 1.0
N17 B:7052 4.8 16.4 1.0
CD B:GLU242 4.9 16.9 1.0
CA B:ASP184 4.9 16.7 1.0
N B:ASN213 5.0 15.9 1.0
CA B:ASP212 5.0 16.1 1.0

Reference:

M.Ellermann, R.Jakob-Roetne, C.Lerner, E.Borroni, D.Schlatter, D.Roth, A.Ehler, M.G.Rudolph, F.Diederich. Molecular Recognition at the Active Site of Catechol-O-Methyltransferase: Energetically Favorable Replacement of A Water Molecule Imported By A Bisubstrate Inhibitor. Angew.Chem.Int.Ed.Engl. V. 48 9092 2009.
ISSN: ISSN 1433-7851
PubMed: 19882607
DOI: 10.1002/ANIE.200904410
Page generated: Wed Aug 14 15:23:14 2024

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