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Magnesium in PDB 5fhr: Crystal Structure of Y200L Mutant of Rat Catechol-O-Methyltransferase in Complex with Adomet and 3,5-Dinitrocatechol

Enzymatic activity of Crystal Structure of Y200L Mutant of Rat Catechol-O-Methyltransferase in Complex with Adomet and 3,5-Dinitrocatechol

All present enzymatic activity of Crystal Structure of Y200L Mutant of Rat Catechol-O-Methyltransferase in Complex with Adomet and 3,5-Dinitrocatechol:
2.1.1.6;

Protein crystallography data

The structure of Crystal Structure of Y200L Mutant of Rat Catechol-O-Methyltransferase in Complex with Adomet and 3,5-Dinitrocatechol, PDB code: 5fhr was solved by C.Levy, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.71 / 1.63
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 61.700, 79.370, 109.660, 90.00, 90.00, 90.00
R / Rfree (%) 15.9 / 17.8

Other elements in 5fhr:

The structure of Crystal Structure of Y200L Mutant of Rat Catechol-O-Methyltransferase in Complex with Adomet and 3,5-Dinitrocatechol also contains other interesting chemical elements:

Bromine (Br) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Y200L Mutant of Rat Catechol-O-Methyltransferase in Complex with Adomet and 3,5-Dinitrocatechol (pdb code 5fhr). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of Y200L Mutant of Rat Catechol-O-Methyltransferase in Complex with Adomet and 3,5-Dinitrocatechol, PDB code: 5fhr:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 5fhr

Go back to Magnesium Binding Sites List in 5fhr
Magnesium binding site 1 out of 2 in the Crystal Structure of Y200L Mutant of Rat Catechol-O-Methyltransferase in Complex with Adomet and 3,5-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 Y200L Mutant of Rat Catechol-O-Methyltransferase in Complex with Adomet and 3,5-Dinitrocatechol within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg302

b:9.3
occ:1.00
 O A:HOH434 2.0 8.4 1.0
O1 A:DNC301 2.1 10.0 1.0
OD2 A:ASP212 2.1 10.2 1.0
O2 A:DNC301 2.1 9.6 1.0
OD1 A:ASP184 2.1 7.9 1.0
OD1 A:ASN213 2.2 8.8 1.0
C1 A:DNC301 2.9 10.2 1.0
C2 A:DNC301 2.9 11.7 1.0
CG A:ASP184 3.1 8.3 1.0
CG A:ASN213 3.1 12.4 1.0
CG A:ASP212 3.1 11.7 1.0
OD2 A:ASP184 3.3 9.8 1.0
ND2 A:ASN213 3.5 9.3 1.0
CB A:ASP212 3.7 8.3 1.0
NZ A:LYS187 3.9 9.7 1.0
CE A:SAM303 4.0 15.2 1.0
O A:HOH442 4.1 11.9 1.0
OD1 A:ASP212 4.1 10.9 1.0
C6 A:DNC301 4.2 12.7 1.0
C3 A:DNC301 4.3 17.6 1.0
O A:MET83 4.3 10.6 1.0
CB A:ASP184 4.5 6.5 1.0
CB A:ASN213 4.5 9.8 1.0
O4 A:DNC301 4.6 24.0 1.0
NZ A:LYS89 4.7 11.0 1.0
CE A:LYS187 4.8 11.6 1.0
O A:ASP184 4.8 13.1 1.0
CA A:VAL85 4.8 9.5 1.0
N1 A:DNC301 4.9 19.0 1.0
CA A:ASP184 4.9 7.5 1.0

Magnesium binding site 2 out of 2 in 5fhr

Go back to Magnesium Binding Sites List in 5fhr
Magnesium binding site 2 out of 2 in the Crystal Structure of Y200L Mutant of Rat Catechol-O-Methyltransferase in Complex with Adomet and 3,5-Dinitrocatechol


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of Y200L Mutant of Rat Catechol-O-Methyltransferase in Complex with Adomet and 3,5-Dinitrocatechol within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg302

b:9.8
occ:1.00
 OD2 B:ASP212 2.1 9.7 1.0
OD1 B:ASN213 2.1 7.6 1.0
O1 B:DNC301 2.1 10.1 1.0
O B:HOH443 2.1 8.0 1.0
OD1 B:ASP184 2.1 8.7 1.0
O2 B:DNC301 2.2 9.7 1.0
C1 B:DNC301 2.9 11.2 1.0
C2 B:DNC301 3.0 13.8 1.0
CG B:ASP184 3.1 9.0 1.0
CG B:ASN213 3.1 7.7 1.0
CG B:ASP212 3.1 11.1 1.0
OD2 B:ASP184 3.3 9.8 1.0
ND2 B:ASN213 3.4 8.8 1.0
CB B:ASP212 3.7 7.0 1.0
NZ B:LYS187 3.8 8.9 1.0
CE B:SAM303 4.1 17.0 1.0
O B:HOH446 4.1 11.1 1.0
OD1 B:ASP212 4.1 9.6 1.0
C6 B:DNC301 4.3 11.5 1.0
C3 B:DNC301 4.3 15.5 1.0
O B:MET83 4.3 9.8 1.0
CB B:ASP184 4.4 8.5 1.0
CB B:ASN213 4.4 8.7 1.0
O4 B:DNC301 4.6 20.8 1.0
NZ B:LYS89 4.7 9.8 1.0
CE B:LYS187 4.7 11.9 1.0
CA B:VAL85 4.8 7.9 1.0
O B:ASP184 4.9 11.9 1.0
CA B:ASP184 4.9 7.8 1.0
C B:ASP212 5.0 6.9 1.0
CA B:ASP212 5.0 7.9 1.0
N1 B:DNC301 5.0 19.8 1.0
N B:ASN213 5.0 8.6 1.0

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 04:15:13 2024

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