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Magnesium in PDB 5fhq: Crystal Structure of (Wt) Rat Catechol-O-Methyltransferase in Complex with Adomet and 3,5-Dinitrocatechol (Dnc)

Enzymatic activity of Crystal Structure of (Wt) Rat Catechol-O-Methyltransferase in Complex with Adomet and 3,5-Dinitrocatechol (Dnc)

All present enzymatic activity of Crystal Structure of (Wt) Rat Catechol-O-Methyltransferase in Complex with Adomet and 3,5-Dinitrocatechol (Dnc):
2.1.1.6;

Protein crystallography data

The structure of Crystal Structure of (Wt) Rat Catechol-O-Methyltransferase in Complex with Adomet and 3,5-Dinitrocatechol (Dnc), PDB code: 5fhq was solved by C.Levy, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 38.90 / 1.63
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 50.720, 50.720, 167.550, 90.00, 90.00, 120.00
R / Rfree (%) 15.5 / 18.8

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of (Wt) Rat Catechol-O-Methyltransferase in Complex with Adomet and 3,5-Dinitrocatechol (Dnc) (pdb code 5fhq). 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 (Wt) Rat Catechol-O-Methyltransferase in Complex with Adomet and 3,5-Dinitrocatechol (Dnc), PDB code: 5fhq:

Magnesium binding site 1 out of 1 in 5fhq

Go back to Magnesium Binding Sites List in 5fhq
Magnesium binding site 1 out of 1 in the Crystal Structure of (Wt) Rat Catechol-O-Methyltransferase in Complex with Adomet and 3,5-Dinitrocatechol (Dnc)


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 (Wt) Rat Catechol-O-Methyltransferase in Complex with Adomet and 3,5-Dinitrocatechol (Dnc) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg303

b:18.4
occ:0.99
 HO2 A:DNC302 1.5 21.8 0.9
OD1 A:ASP141 2.0 17.7 1.0
OD2 A:ASP169 2.1 17.7 1.0
O A:HOH416 2.1 16.9 1.0
OD1 A:ASN170 2.1 16.9 1.0
O1 A:DNC302 2.2 17.8 0.9
O2 A:DNC302 2.2 18.1 0.9
HO1 A:DNC302 2.8 21.3 0.9
C2 A:DNC302 2.9 18.2 0.9
C1 A:DNC302 2.9 17.4 0.9
HD21 A:ASN170 3.0 23.1 1.0
CG A:ASP141 3.0 18.5 1.0
CG A:ASN170 3.1 16.1 1.0
CG A:ASP169 3.1 20.3 1.0
HZ1 A:LYS144 3.2 25.9 1.0
HB3 A:ASP169 3.3 18.8 1.0
OD2 A:ASP141 3.3 20.0 1.0
HE3 A:SAM301 3.4 31.8 1.0
ND2 A:ASN170 3.4 19.3 1.0
HZ2 A:LYS144 3.5 25.9 1.0
HE1 A:SAM301 3.7 31.8 1.0
CB A:ASP169 3.7 15.7 1.0
NZ A:LYS144 3.8 21.6 1.0
CE A:SAM301 4.0 26.5 1.0
HA A:VAL42 4.1 20.3 1.0
OD1 A:ASP169 4.1 21.0 1.0
HE2 A:SAM301 4.2 31.8 1.0
HB2 A:ASP169 4.2 18.8 1.0
C6 A:DNC302 4.3 18.6 0.9
HD22 A:ASN170 4.3 23.1 1.0
C3 A:DNC302 4.3 19.7 0.9
HZ2 A:LYS46 4.3 27.0 1.0
O A:MET40 4.3 21.4 1.0
O A:HOH431 4.3 23.8 1.0
HB1 A:SAM301 4.4 21.7 1.0
HE3 A:LYS144 4.4 26.2 1.0
HZ3 A:LYS144 4.4 25.9 1.0
CB A:ASP141 4.5 18.4 1.0
CB A:ASN170 4.5 18.5 1.0
HA A:ASP141 4.5 16.6 1.0
HG23 A:VAL42 4.5 23.5 1.0
HB2 A:ASN170 4.6 22.2 1.0
HB A:VAL42 4.6 22.1 1.0
HZ1 A:LYS46 4.6 27.0 1.0
O4 A:DNC302 4.7 33.6 0.9
CE A:LYS144 4.7 21.9 1.0
H6 A:DNC302 4.7 22.3 0.9
HB2 A:MET40 4.7 25.0 1.0
HB2 A:ASP141 4.8 22.0 1.0
O A:ASP141 4.8 24.6 1.0
CA A:VAL42 4.9 16.9 1.0
NZ A:LYS46 4.9 22.5 1.0
CA A:ASP141 4.9 13.8 1.0
C A:ASP169 5.0 16.9 1.0
N1 A:DNC302 5.0 29.6 0.9

Reference:

B.J.Law, M.R.Bennett, M.L.Thompson, C.Levy, S.A.Shepherd, D.Leys, J.Micklefield. Effects of Active-Site Modification and Quaternary Structure on the Regioselectivity of Catechol-O-Methyltransferase. Angew.Chem.Int.Ed.Engl. V. 55 2683 2016.
ISSN: ESSN 1521-3773
PubMed: 26797714
DOI: 10.1002/ANIE.201508287
Page generated: Sun Sep 29 04:15:08 2024

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