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Magnesium in PDB 3nw9: Rat Comt in Complex with A Methylpurin-Containing Bisubstrate Inhibitor

Enzymatic activity of Rat Comt in Complex with A Methylpurin-Containing Bisubstrate Inhibitor

All present enzymatic activity of Rat Comt in Complex with A Methylpurin-Containing Bisubstrate Inhibitor:
2.1.1.6;

Protein crystallography data

The structure of Rat Comt in Complex with A Methylpurin-Containing Bisubstrate Inhibitor, PDB code: 3nw9 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) 36.45 / 1.65
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 49.507, 53.861, 80.257, 90.00, 90.00, 90.00
R / Rfree (%) 16.8 / 20.7

Other elements in 3nw9:

The structure of Rat Comt in Complex with A Methylpurin-Containing Bisubstrate Inhibitor also contains other interesting chemical elements:

Fluorine (F) 1 atom
Chlorine (Cl) 4 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Rat Comt in Complex with A Methylpurin-Containing Bisubstrate Inhibitor (pdb code 3nw9). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Rat Comt in Complex with A Methylpurin-Containing Bisubstrate Inhibitor, PDB code: 3nw9:

Magnesium binding site 1 out of 1 in 3nw9

Go back to Magnesium Binding Sites List in 3nw9
Magnesium binding site 1 out of 1 in the Rat Comt in Complex with A Methylpurin-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 Comt in Complex with A Methylpurin-Containing Bisubstrate Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg222

b:13.3
occ:1.00
 OD2 A:ASP169 2.0 14.6 1.0
OD1 A:ASP141 2.1 14.7 1.0
O A:HOH331 2.1 15.2 1.0
O32 A:637228 2.1 15.2 1.0
OD1 A:ASN170 2.1 14.0 1.0
O34 A:637228 2.1 13.1 1.0
C31 A:637228 2.9 12.9 1.0
C33 A:637228 2.9 12.8 1.0
CG A:ASP141 3.0 15.5 1.0
CG A:ASN170 3.1 13.8 1.0
CG A:ASP169 3.1 16.0 1.0
OD2 A:ASP141 3.3 19.7 1.0
ND2 A:ASN170 3.4 14.0 1.0
CB A:ASP169 3.7 13.8 1.0
NZ A:LYS144 3.8 14.2 1.0
O A:HOH359 4.0 28.9 1.0
OE2 A:GLU199 4.2 16.7 1.0
OD1 A:ASP169 4.2 16.5 1.0
C23 A:637228 4.2 14.3 1.0
C20 A:637228 4.2 14.4 1.0
O A:MET40 4.4 17.4 1.0
CB A:ASP141 4.4 13.5 1.0
CB A:ASN170 4.5 14.9 1.0
CE A:LYS144 4.6 15.7 1.0
O A:ASP141 4.6 16.5 1.0
N17 A:637228 4.7 16.8 1.0
NZ A:LYS46 4.7 16.2 1.0
CG1 A:VAL42 4.7 12.7 0.3
OE1 A:GLU199 4.8 15.5 1.0
CA A:ASP141 4.8 12.7 1.0
CD A:GLU199 4.9 15.3 1.0

Reference:

M.Ellermann, R.Paulini, R.Jakob-Roetne, C.Lerner, E.Borroni, D.Roth, A.Ehler, W.B.Schweizer, D.Schlatter, M.G.Rudolph, F.Diederich. Molecular Recognition at the Active Site of Catechol-O-Methyltransferase (Comt): Adenine Replacements in Bisubstrate Inhibitors Chemistry V. 17 6369 2011.
ISSN: ISSN 0947-6539
PubMed: 21538606
DOI: 10.1002/CHEM.201003648
Page generated: Thu Aug 15 08:07:36 2024

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