Magnesium in PDB 1vid: Catechol O-Methyltransferase

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

The structure of Catechol O-Methyltransferase, PDB code: 1vid was solved by J.Vidgren, L.A.Svensson, A.Liljas, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 2.00
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	51.300, 51.300, 168.500, 90.00, 90.00, 120.00
R / Rfree (%)	19.4 / n/a

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

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


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 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg300 b:14.6 occ:1.00 O1 A:DNC302 2.3 17.3 1.0 O2 A:DNC302 2.3 14.0 1.0 OD1 A:ASP141 2.3 10.2 1.0 OD2 A:ASP169 2.3 12.5 1.0 OD1 A:ASN170 2.3 11.1 1.0 O A:HOH400 2.4 28.4 1.0 C1 A:DNC302 3.0 17.7 1.0 C2 A:DNC302 3.0 17.2 1.0 CG A:ASP141 3.1 12.9 1.0 CG A:ASN170 3.2 8.9 1.0 OD2 A:ASP141 3.2 13.1 1.0 CG A:ASP169 3.3 11.9 1.0 ND2 A:ASN170 3.4 9.3 1.0 CB A:ASP169 3.9 10.7 1.0 NZ A:LYS144 4.0 10.9 1.0 CE A:SAM301 4.0 10.8 1.0 OD1 A:ASP169 4.2 11.4 1.0 OE2 A:GLU199 4.3 15.5 1.0 C6 A:DNC302 4.3 17.3 1.0 C3 A:DNC302 4.5 18.8 1.0 O A:MET40 4.5 15.4 1.0 CB A:ASP141 4.5 11.4 1.0 CB A:ASN170 4.6 8.0 1.0 OE1 A:GLU199 4.8 15.5 1.0 NZ A:LYS46 4.8 11.4 1.0 CE A:LYS144 4.9 8.9 1.0 N A:ASN170 4.9 11.8 1.0 CD A:GLU199 4.9 14.9 1.0 CA A:VAL42 4.9 14.5 1.0 C A:ASP169 5.0 13.0 1.0

J.Vidgren, L.A.Svensson, A.Liljas. Crystal Structure of Catechol O-Methyltransferase. Nature V. 368 354 1994.
ISSN: ISSN 0028-0836
PubMed: 8127373
DOI: 10.1038/368354A0