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Magnesium in PDB 1h1d: Catechol O-Methyltransferase

Enzymatic activity of Catechol O-Methyltransferase

All present enzymatic activity of Catechol O-Methyltransferase:
2.1.1.6;

Protein crystallography data

The structure of Catechol O-Methyltransferase, PDB code: 1h1d was solved by M.Archer, M.L.Rodrigues, P.M.Matias, M.J.Bonifacio, D.A.Learmonth, P.Soares-Da-Silva, M.A.Carrondo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.80 / 2.00
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 51.490, 51.490, 168.290, 90.00, 90.00, 120.00
R / Rfree (%) 17.4 / 19.8

Other elements in 1h1d:

The structure of Catechol O-Methyltransferase also contains other interesting chemical elements:

Fluorine (F) 3 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Catechol O-Methyltransferase (pdb code 1h1d). 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 Catechol O-Methyltransferase, PDB code: 1h1d:

Magnesium binding site 1 out of 1 in 1h1d

Go back to Magnesium Binding Sites List in 1h1d
Magnesium binding site 1 out of 1 in the Catechol O-Methyltransferase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Catechol O-Methyltransferase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg300

b:17.1
occ:1.00
OD2 A:ASP169 2.1 14.9 1.0
O A:HOH2053 2.1 15.5 1.0
OD1 A:ASP141 2.1 14.8 1.0
O9 A:BIA335 2.1 24.4 1.0
O5 A:BIA335 2.2 23.4 1.0
OD1 A:ASN170 2.2 15.2 1.0
C7 A:BIA335 2.9 24.1 1.0
CG A:ASP141 2.9 15.0 1.0
C32 A:BIA335 3.0 24.1 1.0
CG A:ASP169 3.1 14.3 1.0
OD2 A:ASP141 3.2 14.7 1.0
CG A:ASN170 3.2 15.3 1.0
ND2 A:ASN170 3.5 14.6 1.0
CB A:ASP169 3.7 12.2 1.0
NZ A:LYS144 3.8 12.9 1.0
CE A:SAM301 4.1 14.5 1.0
OD1 A:ASP169 4.1 12.9 1.0
OE2 A:GLU199 4.3 21.4 1.0
C3 A:BIA335 4.3 24.4 1.0
CB A:ASP141 4.4 13.8 1.0
C28 A:BIA335 4.4 24.9 1.0
CB A:ASN170 4.6 15.6 1.0
O A:MET40 4.6 19.6 1.0
O A:ASP141 4.8 15.4 1.0
CE A:LYS144 4.8 12.7 1.0
OE1 A:GLU199 4.8 23.0 1.0
NZ A:LYS46 4.8 13.7 1.0
C A:ASP169 4.9 15.9 1.0
O17 A:BIA335 4.9 24.9 1.0
CA A:ASP141 4.9 13.9 1.0
N A:ASN170 4.9 16.4 1.0
CA A:ASP169 4.9 14.4 1.0
CD A:GLU199 5.0 24.1 1.0

Reference:

M.J.Bonifacio, M.Archer, M.L.Rodrigues, P.M.Matias, D.A.Learmonth, M.A.Carrondo, P.Soares-Da-Silva. Kinetics and Crystal Structure of Catechol-O-Methyltransferase Complex with Co-Substrate and A Novel Inhibitor with Potential Therapeutic Application Mol.Pharmacol. V. 62 795 2002.
ISSN: ISSN 0026-895X
PubMed: 12237326
DOI: 10.1124/MOL.62.4.795
Page generated: Mon Dec 14 05:58:31 2020

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