Magnesium in PDB 6i3c: Crystal Structure of Human Soluble Catechol O-Methyltransferase in Complex with 3,5-Dinitrocatechol and S-Adensoyl-L-Methionine

Enzymatic activity of Crystal Structure of Human Soluble Catechol O-Methyltransferase in Complex with 3,5-Dinitrocatechol and S-Adensoyl-L-Methionine

All present enzymatic activity of Crystal Structure of Human Soluble Catechol O-Methyltransferase in Complex with 3,5-Dinitrocatechol and S-Adensoyl-L-Methionine:
2.1.1.6;

Protein crystallography data

The structure of Crystal Structure of Human Soluble Catechol O-Methyltransferase in Complex with 3,5-Dinitrocatechol and S-Adensoyl-L-Methionine, PDB code: 6i3c was solved by C.W.Levy, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 39.13 / 1.34
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 43.694, 61.749, 46.071, 90.00, 116.42, 90.00
R / Rfree (%) 13.4 / 17

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Human Soluble Catechol O-Methyltransferase in Complex with 3,5-Dinitrocatechol and S-Adensoyl-L-Methionine (pdb code 6i3c). 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 Soluble Catechol O-Methyltransferase in Complex with 3,5-Dinitrocatechol and S-Adensoyl-L-Methionine, PDB code: 6i3c:

Magnesium binding site 1 out of 1 in 6i3c

Go back to Magnesium Binding Sites List in 6i3c
Magnesium binding site 1 out of 1 in the Crystal Structure of Human Soluble Catechol O-Methyltransferase in Complex with 3,5-Dinitrocatechol and S-Adensoyl-L-Methionine


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 Soluble Catechol O-Methyltransferase in Complex with 3,5-Dinitrocatechol and S-Adensoyl-L-Methionine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg301

b:8.6
occ:1.00
 O A:HOH423 2.1 8.3 1.0
OD2 A:ASP169 2.1 8.4 1.0
O1 A:DNC303 2.1 8.9 1.0
OD1 A:ASP141 2.1 7.8 1.0
O2 A:DNC303 2.1 9.2 1.0
OD1 A:ASN170 2.2 8.4 1.0
C2 A:DNC303 2.9 9.7 1.0
C1 A:DNC303 3.0 9.5 1.0
CG A:ASP141 3.1 7.1 1.0
CG A:ASN170 3.1 8.6 1.0
CG A:ASP169 3.1 7.6 1.0
OD2 A:ASP141 3.4 7.5 1.0
ND2 A:ASN170 3.4 10.1 1.0
CB A:ASP169 3.7 6.7 1.0
NZ A:LYS144 3.9 9.2 1.0
CE A:SAM302 3.9 10.0 1.0
OE2 A:GLU199 4.2 9.0 1.0
OD1 A:ASP169 4.2 8.4 1.0
C6 A:DNC303 4.3 10.8 1.0
C3 A:DNC303 4.4 9.9 1.0
O A:MET40 4.4 8.4 1.0
CB A:ASP141 4.5 6.9 1.0
CB A:ASN170 4.5 9.2 1.0
NZ A:LYS46 4.7 10.1 1.0
OE1 A:GLU199 4.7 8.9 1.0
CE A:LYS144 4.8 9.6 1.0
O3 A:DNC303 4.8 11.2 1.0
CD A:GLU199 4.9 7.8 1.0
O A:ASP141 4.9 8.9 1.0
CA A:ASP169 5.0 8.4 1.0
CA A:ASP141 5.0 7.4 1.0

Reference:

S.Czarnota, L.O.Johannissen, N.J.Baxter, F.Rummel, A.L.Wilson, M.J.Cliff, C.W.Levy, N.S.Scrutton, J.P.Waltho, S.Hay. Equatorial Active Site Compaction and Electrostatic Reorganization in Catechol-O-Methyltransferase. Acs Catalysis V. 9 4394 2019.
ISSN: ESSN 2155-5435
PubMed: 31080692
DOI: 10.1021/ACSCATAL.9B00174
Page generated: Mon Dec 14 22:56:06 2020

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