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Magnesium in PDB 3oe5: Rat Catechol O-Methyltransferase in Complex with A Catechol-Type, Pyridylsulfanyl-Containing Inhibitor - Humanized Form

Enzymatic activity of Rat Catechol O-Methyltransferase in Complex with A Catechol-Type, Pyridylsulfanyl-Containing Inhibitor - Humanized Form

All present enzymatic activity of Rat Catechol O-Methyltransferase in Complex with A Catechol-Type, Pyridylsulfanyl-Containing Inhibitor - Humanized Form:
2.1.1.6;

Protein crystallography data

The structure of Rat Catechol O-Methyltransferase in Complex with A Catechol-Type, Pyridylsulfanyl-Containing Inhibitor - Humanized Form, PDB code: 3oe5 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) 42.47 / 1.52
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 50.687, 50.687, 167.765, 90.00, 90.00, 120.00
R / Rfree (%) 19.3 / 22.1

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Rat Catechol O-Methyltransferase in Complex with A Catechol-Type, Pyridylsulfanyl-Containing Inhibitor - Humanized Form (pdb code 3oe5). 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 Catechol O-Methyltransferase in Complex with A Catechol-Type, Pyridylsulfanyl-Containing Inhibitor - Humanized Form, PDB code: 3oe5:

Magnesium binding site 1 out of 1 in 3oe5

Go back to Magnesium Binding Sites List in 3oe5
Magnesium binding site 1 out of 1 in the Rat Catechol O-Methyltransferase in Complex with A Catechol-Type, Pyridylsulfanyl-Containing Inhibitor - Humanized Form


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, Pyridylsulfanyl-Containing Inhibitor - Humanized Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg222

b:20.9
occ:1.00
 OD1 A:ASP141 2.0 19.6 1.0
O A:HOH236 2.1 21.3 1.0
OD2 A:ASP169 2.1 20.5 1.0
O22 A:611223 2.1 20.6 1.0
OD1 A:ASN170 2.1 18.8 1.0
O23 A:611223 2.2 22.2 1.0
C16 A:611223 2.9 21.2 1.0
C17 A:611223 3.0 20.5 1.0
CG A:ASP141 3.0 18.2 1.0
CG A:ASN170 3.1 18.2 1.0
CG A:ASP169 3.2 21.3 1.0
OD2 A:ASP141 3.3 21.7 1.0
ND2 A:ASN170 3.4 19.7 1.0
CB A:ASP169 3.8 19.0 1.0
NZ A:LYS144 3.8 19.6 1.0
O A:HOH322 3.9 35.5 1.0
OD1 A:ASP169 4.2 19.9 1.0
OE2 A:GLU199 4.2 25.2 1.0
C18 A:611223 4.3 22.6 1.0
O A:MET40 4.3 24.4 1.0
C15 A:611223 4.3 23.0 1.0
CB A:ASP141 4.4 19.4 1.0
CB A:ASN170 4.4 20.8 1.0
CE A:LYS144 4.7 19.5 1.0
CG2 A:VAL42 4.7 23.4 0.5
O A:ASP141 4.7 22.2 1.0
NZ A:LYS46 4.8 20.7 1.0
N13 A:611223 4.8 20.3 1.0
CA A:ASP141 4.8 16.6 1.0
CD A:GLU199 5.0 26.5 1.0
OE1 A:GLU199 5.0 28.5 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: Mon Aug 11 01:08:20 2025

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