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Magnesium in PDB 2zvj: Crystal Structures of Rat Catechol-O-Methyltransferase Complexed with Coumarine-Based Inhibitor

Enzymatic activity of Crystal Structures of Rat Catechol-O-Methyltransferase Complexed with Coumarine-Based Inhibitor

All present enzymatic activity of Crystal Structures of Rat Catechol-O-Methyltransferase Complexed with Coumarine-Based Inhibitor:
2.1.1.6;

Protein crystallography data

The structure of Crystal Structures of Rat Catechol-O-Methyltransferase Complexed with Coumarine-Based Inhibitor, PDB code: 2zvj was solved by E.Tsuji, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 42.30 / 2.30
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 50.448, 50.448, 167.626, 90.00, 90.00, 120.00
R / Rfree (%) 21.1 / 28.6

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structures of Rat Catechol-O-Methyltransferase Complexed with Coumarine-Based Inhibitor (pdb code 2zvj). 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 Structures of Rat Catechol-O-Methyltransferase Complexed with Coumarine-Based Inhibitor, PDB code: 2zvj:

Magnesium binding site 1 out of 1 in 2zvj

Go back to Magnesium Binding Sites List in 2zvj
Magnesium binding site 1 out of 1 in the Crystal Structures of Rat Catechol-O-Methyltransferase Complexed with Coumarine-Based Inhibitor


Mono view


Stereo pair view

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

b:33.9
occ:1.00
 OD2 A:ASP169 1.9 30.5 1.0
O10 A:KOM302 1.9 49.4 1.0
OD1 A:ASN170 2.0 31.5 1.0
OD2 A:ASP141 2.0 17.1 1.0
O A:HOH371 2.0 27.1 1.0
O9 A:KOM302 2.4 49.8 1.0
C6 A:KOM302 2.8 50.3 1.0
CG A:ASP169 2.9 29.7 1.0
CG A:ASN170 2.9 29.8 1.0
C5 A:KOM302 2.9 50.2 1.0
CG A:ASP141 3.0 24.0 1.0
OD1 A:ASP141 3.2 24.8 1.0
ND2 A:ASN170 3.3 25.6 1.0
CB A:ASP169 3.5 28.7 1.0
OD1 A:ASP169 3.8 32.5 1.0
NZ A:LYS144 4.0 28.4 1.0
C1 A:KOM302 4.1 50.3 1.0
CB A:ASN170 4.3 32.3 1.0
O A:MET40 4.3 46.1 1.0
CB A:ASP141 4.4 25.4 1.0
C4 A:KOM302 4.4 50.6 1.0
CE A:SAM301 4.4 39.4 1.0
OE2 A:GLU199 4.5 69.3 1.0
OE1 A:GLU199 4.6 67.5 1.0
CA A:VAL42 4.7 39.5 1.0
NZ A:LYS46 4.7 41.5 1.0
N A:ASN170 4.7 31.4 1.0
CA A:ASP169 4.8 30.1 1.0
C A:ASP169 4.8 31.2 1.0
N A:VAL42 4.9 40.8 1.0
O A:ASP141 4.9 28.7 1.0
CG2 A:VAL42 4.9 40.2 1.0
CB A:VAL42 5.0 39.2 1.0
CA A:ASP141 5.0 27.2 1.0
CD A:GLU199 5.0 68.8 1.0

Reference:

E.Tsuji, K.Okazaki, K.Takeda. Crystal Structures of Rat Catechol-O-Methyltransferase Complexed with Coumarine-Based Inhibitor Biochem.Biophys.Res.Commun. V. 378 494 2009.
ISSN: ISSN 0006-291X
PubMed: 19056347
DOI: 10.1016/J.BBRC.2008.11.085
Page generated: Sun Aug 10 17:06:03 2025

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