Magnesium in PDB 2cl5: Catechol-O-Methyltransferase in Complex with An Inhibitor

All present enzymatic activity of Catechol-O-Methyltransferase in Complex with An Inhibitor:
2.1.1.6;

The structure of Catechol-O-Methyltransferase in Complex with An Inhibitor, PDB code: 2cl5 was solved by P.N.Palma, M.L.Rodrigues, M.Archer, M.J.Bonifacio, A.I.Loureiro, D.A.Learmonth, M.A.Carrondo, P.Soares-Da-Silva, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	62.02 / 1.6
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	52.767, 79.627, 61.540, 90.00, 91.14, 90.00
R / Rfree (%)	14.9 / 17.8

The binding sites of Magnesium atom in the Catechol-O-Methyltransferase in Complex with An Inhibitor (pdb code 2cl5). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Catechol-O-Methyltransferase in Complex with An Inhibitor, PDB code: 2cl5:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Catechol-O-Methyltransferase in Complex with An Inhibitor


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 in Complex with An Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1216 b:9.9 occ:1.00 OD1 A:ASP141 2.0 9.1 1.0 OD2 A:ASP169 2.1 10.3 1.0 O A:HOH2205 2.1 10.3 1.0 O1 A:BIE1218 2.1 8.6 1.0 ND2 A:ASN170 2.1 6.0 1.0 O2 A:BIE1218 2.2 11.1 1.0 C1 A:BIE1218 2.8 8.1 1.0 C2 A:BIE1218 2.9 9.8 1.0 CG A:ASP141 3.0 10.3 1.0 CG A:ASP169 3.1 9.7 1.0 CG A:ASN170 3.2 11.3 1.0 OD2 A:ASP141 3.3 10.2 1.0 OD1 A:ASN170 3.5 13.8 1.0 CB A:ASP169 3.6 9.0 1.0 NZ A:LYS144 3.8 9.6 1.0 CE A:SAM1217 4.0 13.4 1.0 OD1 A:ASP169 4.1 10.7 1.0 OE2 A:GLU199 4.2 11.0 1.0 C6 A:BIE1218 4.3 8.1 1.0 C3 A:BIE1218 4.3 10.4 1.0 O A:MET40 4.4 11.2 1.0 CB A:ASP141 4.4 10.0 1.0 CB A:ASN170 4.5 9.7 1.0 CE A:LYS144 4.6 11.3 1.0 NZ A:LYS46 4.7 9.9 1.0 OE1 A:GLU199 4.7 9.3 1.0 O A:ASP141 4.8 12.3 1.0 O3 A:BIE1218 4.8 15.6 1.0 CA A:ASP141 4.8 9.9 1.0 CD A:GLU199 4.9 8.6 1.0 CA A:ASP169 4.9 9.0 1.0 C A:ASP169 5.0 9.2 1.0

Magnesium binding site 2 out of 2 in the Catechol-O-Methyltransferase in Complex with An Inhibitor


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Catechol-O-Methyltransferase in Complex with An Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg1216 b:10.7 occ:1.00 OD1 B:ASP141 2.1 10.0 1.0 O2 B:BIE1218 2.1 10.4 1.0 O1 B:BIE1218 2.1 9.3 1.0 O B:HOH2186 2.1 11.7 1.0 OD2 B:ASP169 2.1 11.8 1.0 ND2 B:ASN170 2.1 6.1 1.0 C2 B:BIE1218 2.8 9.2 1.0 C1 B:BIE1218 2.8 9.2 1.0 CG B:ASP141 3.0 10.7 1.0 CG B:ASP169 3.1 10.2 1.0 CG B:ASN170 3.1 11.5 1.0 OD2 B:ASP141 3.3 9.6 1.0 OD1 B:ASN170 3.4 13.8 1.0 CB B:ASP169 3.6 8.5 1.0 NZ B:LYS144 3.7 12.5 1.0 CE B:SAM1217 3.9 13.6 1.0 OD1 B:ASP169 4.1 9.3 1.0 C3 B:BIE1218 4.2 13.2 1.0 OE2 B:GLU199 4.2 10.8 1.0 C6 B:BIE1218 4.3 11.2 1.0 O B:MET40 4.3 10.4 1.0 CB B:ASP141 4.4 10.0 1.0 CB B:ASN170 4.5 9.8 1.0 CE B:LYS144 4.6 12.5 1.0 O3 B:BIE1218 4.7 25.1 1.0 OE1 B:GLU199 4.7 9.9 1.0 NZ B:LYS46 4.7 10.5 1.0 O B:ASP141 4.8 13.5 1.0 CA B:ASP141 4.8 10.0 1.0 CD B:GLU199 4.9 10.1 1.0 N1 B:BIE1218 4.9 19.1 1.0 CA B:ASP169 5.0 8.4 1.0 C B:ASP169 5.0 9.9 1.0

P.N.Palma, M.L.Rodrigues, M.Archer, M.J.Bonifacio, A.I.Loureiro, D.A.Learmonth, M.A.Carrondo, P.Soares-Da-Silva. Comparative Study of Ortho- and Meta-Nitrated Inhibitors of Catechol-O-Methyltransferase: Interactions with the Active Site and Regioselectivity of O-Methylation. Mol.Pharmacol. V. 70 143 2006.
ISSN: ISSN 0026-895X
PubMed: 16618795
DOI: 10.1124/MOL.106.023119