Magnesium in PDB 4pyl: Humanized Rat Comt in Complex with Sinefungin, MG2+, and Tolcapone

All present enzymatic activity of Humanized Rat Comt in Complex with Sinefungin, MG2+, and Tolcapone:
2.1.1.6;

The structure of Humanized Rat Comt in Complex with Sinefungin, MG2+, and Tolcapone, PDB code: 4pyl was solved by A.Ehler, J.Benz, D.Schlatter, M.G.Rudolph, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	41.78 / 2.20
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	49.813, 49.813, 167.467, 90.00, 90.00, 120.00
R / Rfree (%)	18.8 / 24.2

The binding sites of Magnesium atom in the Humanized Rat Comt in Complex with Sinefungin, MG2+, and Tolcapone (pdb code 4pyl). 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 Humanized Rat Comt in Complex with Sinefungin, MG2+, and Tolcapone, PDB code: 4pyl:

Magnesium binding site 1 out of 1 in the Humanized Rat Comt in Complex with Sinefungin, MG2+, and Tolcapone


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Humanized Rat Comt in Complex with Sinefungin, MG2+, and Tolcapone within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg301 b:34.5 occ:1.00 O7 A:TCW303 2.0 35.5 1.0 OD1 A:ASP184 2.0 24.0 1.0 OD1 A:ASN213 2.1 29.9 1.0 O A:HOH440 2.1 36.4 1.0 O8 A:TCW303 2.2 28.5 1.0 OD2 A:ASP212 2.3 33.3 1.0 C2 A:TCW303 2.8 29.3 1.0 C1 A:TCW303 2.8 31.3 1.0 CG A:ASP184 3.0 35.0 1.0 CG A:ASN213 3.0 23.6 1.0 OD2 A:ASP184 3.2 31.9 1.0 CG A:ASP212 3.3 31.1 1.0 ND2 A:ASN213 3.4 33.7 1.0 NZ A:LYS187 3.8 38.7 1.0 CB A:ASP212 3.8 29.3 1.0 NE A:SFG302 4.0 26.3 1.0 C3 A:TCW303 4.1 29.0 1.0 OD1 A:ASP212 4.2 36.4 1.0 C6 A:TCW303 4.2 35.1 1.0 OE2 A:GLU242 4.3 41.2 1.0 CB A:ASP184 4.4 27.6 1.0 CB A:ASN213 4.4 29.2 1.0 O A:MET83 4.4 38.5 1.0 CE A:LYS187 4.6 30.0 1.0 O A:ASP184 4.6 44.0 1.0 OE1 A:GLU242 4.7 33.6 1.0 NZ A:LYS89 4.7 35.6 1.0 CA A:ASP184 4.8 35.4 1.0 CA A:VAL85 4.9 42.8 1.0 O10 A:TCW303 4.9 52.7 1.0 C A:ASP212 4.9 35.1 1.0 N A:ASN213 4.9 36.0 1.0 CD A:GLU242 4.9 36.8 1.0 OH A:TYR190 5.0 30.4 1.0 N9 A:TCW303 5.0 44.1 1.0 CA A:ASP212 5.0 36.6 1.0

A.Ehler, J.Benz, D.Schlatter, M.G.Rudolph. Mapping the Conformational Space Accessible to Catechol-O-Methyltransferase. Acta Crystallogr.,Sect.D V. 70 2163 2014.
ISSN: ISSN 0907-4449
PubMed: 25084335
DOI: 10.1107/S1399004714012917