Atomistry » Magnesium » PDB 5lmn-5ltt » 5lsa
Atomistry »
  Magnesium »
    PDB 5lmn-5ltt »
      5lsa »

Magnesium in PDB 5lsa: Human Catechol O-Methyltransferase in Complex with Sam and Dnc at 1.50A

Enzymatic activity of Human Catechol O-Methyltransferase in Complex with Sam and Dnc at 1.50A

All present enzymatic activity of Human Catechol O-Methyltransferase in Complex with Sam and Dnc at 1.50A:
2.1.1.6;

Protein crystallography data

The structure of Human Catechol O-Methyltransferase in Complex with Sam and Dnc at 1.50A, PDB code: 5lsa was solved by A.Ehler, C.Lerner, M.G.Rudolph, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 37.88 / 1.50
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 43.021, 61.311, 44.773, 90.00, 118.30, 90.00
R / Rfree (%) 16.7 / 21

Other elements in 5lsa:

The structure of Human Catechol O-Methyltransferase in Complex with Sam and Dnc at 1.50A also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Human Catechol O-Methyltransferase in Complex with Sam and Dnc at 1.50A (pdb code 5lsa). 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 Human Catechol O-Methyltransferase in Complex with Sam and Dnc at 1.50A, PDB code: 5lsa:

Magnesium binding site 1 out of 1 in 5lsa

Go back to Magnesium Binding Sites List in 5lsa
Magnesium binding site 1 out of 1 in the Human Catechol O-Methyltransferase in Complex with Sam and Dnc at 1.50A


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Human Catechol O-Methyltransferase in Complex with Sam and Dnc at 1.50A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg301

b:10.2
occ:1.00
 OD1 A:ASP191 2.0 7.4 1.0
O A:HOH433 2.1 9.9 1.0
OD2 A:ASP219 2.1 8.6 1.0
OD1 A:ASN220 2.1 7.3 1.0
O2 A:DNC304 2.2 9.1 1.0
O1 A:DNC304 2.2 10.7 1.0
CG A:ASP191 2.9 9.0 1.0
C2 A:DNC304 3.0 10.4 1.0
C1 A:DNC304 3.0 8.2 1.0
CG A:ASN220 3.1 8.8 1.0
CG A:ASP219 3.1 10.3 1.0
OD2 A:ASP191 3.3 10.8 1.0
ND2 A:ASN220 3.4 8.7 1.0
CB A:ASP219 3.7 8.1 1.0
NZ A:LYS194 3.8 10.0 1.0
CE A:SAM303 3.9 8.8 1.0
OD1 A:ASP219 4.1 9.6 1.0
OE2 A:GLU249 4.1 8.1 1.0
O A:MET90 4.3 10.2 1.0
C6 A:DNC304 4.3 8.9 1.0
CB A:ASP191 4.4 8.8 1.0
C3 A:DNC304 4.4 11.1 1.0
CB A:ASN220 4.4 8.4 1.0
NZ A:LYS96 4.6 8.4 1.0
CE A:LYS194 4.7 11.7 1.0
OE1 A:GLU249 4.8 10.6 1.0
O3 A:DNC304 4.8 11.6 1.0
O A:ASP191 4.9 11.0 1.0
CA A:ASP191 4.9 8.3 1.0
CD A:GLU249 4.9 10.8 1.0
C A:ASP219 4.9 7.8 1.0
N A:ASN220 4.9 7.9 1.0
CA A:ASP219 4.9 9.2 1.0

Reference:

C.Lerner, M.G.Rudolph. Human Catechol O-Methyltransferase in Complex with Sam and Dnc at 1.50A To Be Published.
Page generated: Sun Sep 29 20:37:02 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy