Magnesium in PDB 1jr4: Catechol O-Methyltransferase Bisubstrate-Inhibitor Complex

All present enzymatic activity of Catechol O-Methyltransferase Bisubstrate-Inhibitor Complex:
2.1.1.6;

The structure of Catechol O-Methyltransferase Bisubstrate-Inhibitor Complex, PDB code: 1jr4 was solved by A.Ruf, M.Stihle, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	24.21 / 2.63
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	50.600, 50.600, 167.700, 90.00, 90.00, 120.00
R / Rfree (%)	n/a / n/a

The binding sites of Magnesium atom in the Catechol O-Methyltransferase Bisubstrate-Inhibitor Complex (pdb code 1jr4). 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 Catechol O-Methyltransferase Bisubstrate-Inhibitor Complex, PDB code: 1jr4:

Magnesium binding site 1 out of 1 in the Catechol O-Methyltransferase Bisubstrate-Inhibitor Complex


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Catechol O-Methyltransferase Bisubstrate-Inhibitor Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg300 b:32.5 occ:1.00 OD2 A:ASP169 1.8 32.7 1.0 OD2 A:ASP141 1.9 35.8 1.0 O28 A:CL4301 2.0 34.8 1.0 O A:HOH302 2.1 29.0 1.0 OD1 A:ASN170 2.2 29.3 1.0 O29 A:CL4301 2.3 38.4 1.0 CG A:ASP141 2.7 33.7 1.0 OD1 A:ASP141 2.8 30.4 1.0 C23 A:CL4301 2.9 34.9 1.0 CG A:ASP169 3.0 28.9 1.0 C22 A:CL4301 3.0 36.7 1.0 CG A:ASN170 3.1 24.4 1.0 ND2 A:ASN170 3.4 24.1 1.0 CB A:ASP169 3.7 27.8 1.0 OD1 A:ASP169 4.0 30.2 1.0 NZ A:LYS144 4.1 30.8 1.0 CB A:ASP141 4.1 31.7 1.0 C24 A:CL4301 4.2 34.1 1.0 O A:ASP141 4.3 38.1 1.0 C27 A:CL4301 4.4 36.8 1.0 CB A:ASN170 4.5 22.9 1.0 OE2 A:GLU199 4.5 54.7 1.0 CG1 A:VAL42 4.5 42.4 1.0 CA A:ASP141 4.6 33.2 1.0 O A:MET40 4.6 44.8 1.0 C A:ASP169 4.8 29.9 1.0 N3 A:CL4301 4.8 33.9 1.0 N A:ASN170 4.9 28.8 1.0 CA A:VAL42 4.9 41.6 1.0 CA A:ASP169 4.9 27.9 1.0 C A:ASP141 4.9 36.2 1.0 N A:VAL42 4.9 43.5 1.0

C.Lerner, A.Ruf, V.Gramlich, B.Masjost, G.Zurcher, R.Jakob-Roetne, E.Borroni, F.Diederich. X-Ray Crystal Structure of A Bisubstrate Inhibitor Bound to the Enzyme Catechol-O-Methyltransferase: A Dramatic Effect of Inhibitor Preorganization on Binding Affinity. Angew.Chem.Int.Ed.Engl. V. 40 4040 2001.
ISSN: ISSN 1433-7851
PubMed: 12404486
DOI: 10.1002/1521-3773(20011105)40:21<4040::AID-ANIE4040>3.0.CO;2-C