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Magnesium in PDB 3bwy: Crystal Structure of Human 108M Catechol O-Methyltransferase Bound with S-Adenosylmethionine and Inhibitor Dinitrocatechol

Enzymatic activity of Crystal Structure of Human 108M Catechol O-Methyltransferase Bound with S-Adenosylmethionine and Inhibitor Dinitrocatechol

All present enzymatic activity of Crystal Structure of Human 108M Catechol O-Methyltransferase Bound with S-Adenosylmethionine and Inhibitor Dinitrocatechol:
2.1.1.6;

Protein crystallography data

The structure of Crystal Structure of Human 108M Catechol O-Methyltransferase Bound with S-Adenosylmethionine and Inhibitor Dinitrocatechol, PDB code: 3bwy was solved by K.Rutherford, I.Le Trong, R.E.Stenkamp, W.W.Parson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.62 / 1.30
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 43.249, 66.163, 68.519, 90.00, 90.00, 90.00
R / Rfree (%) 12.4 / 16.7

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Human 108M Catechol O-Methyltransferase Bound with S-Adenosylmethionine and Inhibitor Dinitrocatechol (pdb code 3bwy). 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 Crystal Structure of Human 108M Catechol O-Methyltransferase Bound with S-Adenosylmethionine and Inhibitor Dinitrocatechol, PDB code: 3bwy:

Magnesium binding site 1 out of 1 in 3bwy

Go back to Magnesium Binding Sites List in 3bwy
Magnesium binding site 1 out of 1 in the Crystal Structure of Human 108M Catechol O-Methyltransferase Bound with S-Adenosylmethionine and Inhibitor Dinitrocatechol


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Human 108M Catechol O-Methyltransferase Bound with S-Adenosylmethionine and Inhibitor Dinitrocatechol within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg300

b:14.1
occ:1.00
 O A:HOH412 2.1 13.4 1.0
O1 A:DNC302 2.1 13.8 1.0
O2 A:DNC302 2.1 15.4 1.0
OD1 A:ASP141 2.1 13.4 1.0
OD1 A:ASN170 2.1 14.1 1.0
OD2 A:ASP169 2.1 14.3 1.0
C2 A:DNC302 2.9 16.1 1.0
C1 A:DNC302 2.9 14.7 1.0
CG A:ASP141 3.1 12.1 1.0
CG A:ASN170 3.1 14.5 1.0
CG A:ASP169 3.1 12.7 1.0
OD2 A:ASP141 3.4 14.1 1.0
ND2 A:ASN170 3.4 15.0 1.0
CB A:ASP169 3.7 13.4 1.0
NZ A:LYS144 3.8 14.4 1.0
CE A:SAM301 3.8 18.1 1.0
OE2 A:GLU199 4.2 13.8 1.0
OD1 A:ASP169 4.2 13.8 1.0
C6 A:DNC302 4.3 15.4 1.0
C3 A:DNC302 4.3 16.6 1.0
O A:MET40 4.3 14.6 1.0
CB A:ASN170 4.4 15.0 1.0
CB A:ASP141 4.4 13.7 1.0
NZ A:LYS46 4.6 15.4 1.0
CE A:LYS144 4.7 15.1 1.0
OE1 A:GLU199 4.7 13.4 1.0
O3 A:DNC302 4.7 20.1 1.0
CD A:GLU199 4.9 12.5 1.0
O A:ASP141 4.9 17.7 1.0
CA A:ASP141 4.9 11.8 1.0
N1 A:DNC302 5.0 18.9 1.0
CA A:ASP169 5.0 10.6 1.0

Reference:

K.Rutherford, I.Le Trong, R.E.Stenkamp, W.W.Parson. Crystal Structures of Human 108V and 108M Catechol O-Methyltransferase. J.Mol.Biol. V. 380 120 2008.
ISSN: ISSN 0022-2836
PubMed: 18486144
DOI: 10.1016/J.JMB.2008.04.040
Page generated: Wed Aug 14 09:22:32 2024

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