Magnesium in PDB 1h1d: Catechol O-Methyltransferase

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

The structure of Catechol O-Methyltransferase, PDB code: 1h1d was solved by M.Archer, M.L.Rodrigues, P.M.Matias, M.J.Bonifacio, D.A.Learmonth, P.Soares-Da-Silva, M.A.Carrondo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	25.80 / 2.00
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	51.490, 51.490, 168.290, 90.00, 90.00, 120.00
R / Rfree (%)	17.4 / 19.8

The structure of Catechol O-Methyltransferase also contains other interesting chemical elements:

Fluorine

(F)

3 atoms

The binding sites of Magnesium atom in the Catechol O-Methyltransferase (pdb code 1h1d). 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: 1h1d:

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:17.1 occ:1.00 OD2 A:ASP169 2.1 14.9 1.0 O A:HOH2053 2.1 15.5 1.0 OD1 A:ASP141 2.1 14.8 1.0 O9 A:BIA335 2.1 24.4 1.0 O5 A:BIA335 2.2 23.4 1.0 OD1 A:ASN170 2.2 15.2 1.0 C7 A:BIA335 2.9 24.1 1.0 CG A:ASP141 2.9 15.0 1.0 C32 A:BIA335 3.0 24.1 1.0 CG A:ASP169 3.1 14.3 1.0 OD2 A:ASP141 3.2 14.7 1.0 CG A:ASN170 3.2 15.3 1.0 ND2 A:ASN170 3.5 14.6 1.0 CB A:ASP169 3.7 12.2 1.0 NZ A:LYS144 3.8 12.9 1.0 CE A:SAM301 4.1 14.5 1.0 OD1 A:ASP169 4.1 12.9 1.0 OE2 A:GLU199 4.3 21.4 1.0 C3 A:BIA335 4.3 24.4 1.0 CB A:ASP141 4.4 13.8 1.0 C28 A:BIA335 4.4 24.9 1.0 CB A:ASN170 4.6 15.6 1.0 O A:MET40 4.6 19.6 1.0 O A:ASP141 4.8 15.4 1.0 CE A:LYS144 4.8 12.7 1.0 OE1 A:GLU199 4.8 23.0 1.0 NZ A:LYS46 4.8 13.7 1.0 C A:ASP169 4.9 15.9 1.0 O17 A:BIA335 4.9 24.9 1.0 CA A:ASP141 4.9 13.9 1.0 N A:ASN170 4.9 16.4 1.0 CA A:ASP169 4.9 14.4 1.0 CD A:GLU199 5.0 24.1 1.0

M.J.Bonifacio, M.Archer, M.L.Rodrigues, P.M.Matias, D.A.Learmonth, M.A.Carrondo, P.Soares-Da-Silva. Kinetics and Crystal Structure of Catechol-O-Methyltransferase Complex with Co-Substrate and A Novel Inhibitor with Potential Therapeutic Application Mol.Pharmacol. V. 62 795 2002.
ISSN: ISSN 0026-895X
PubMed: 12237326
DOI: 10.1124/MOL.62.4.795