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Magnesium in PDB 3a7d: Crystal Structures of Rat Catechol-O-Methyltransferase Complexed with New Bi-Substrate Type Inhibitor

Enzymatic activity of Crystal Structures of Rat Catechol-O-Methyltransferase Complexed with New Bi-Substrate Type Inhibitor

All present enzymatic activity of Crystal Structures of Rat Catechol-O-Methyltransferase Complexed with New Bi-Substrate Type Inhibitor:
2.1.1.6;

Protein crystallography data

The structure of Crystal Structures of Rat Catechol-O-Methyltransferase Complexed with New Bi-Substrate Type Inhibitor, PDB code: 3a7d was solved by E.Tsuji, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 2.40
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 50.075, 58.082, 79.198, 90.00, 90.00, 90.00
R / Rfree (%) 15.9 / 22.5

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structures of Rat Catechol-O-Methyltransferase Complexed with New Bi-Substrate Type Inhibitor (pdb code 3a7d). 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 New Bi-Substrate Type Inhibitor, PDB code: 3a7d:

Magnesium binding site 1 out of 1 in 3a7d

Go back to Magnesium Binding Sites List in 3a7d
Magnesium binding site 1 out of 1 in the Crystal Structures of Rat Catechol-O-Methyltransferase Complexed with New Bi-Substrate Type 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 New Bi-Substrate Type Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg300

b:31.4
occ:1.00
 O A:HOH312 2.0 24.7 1.0
OD1 A:ASP141 2.0 21.5 1.0
OD2 A:ASP169 2.1 25.6 1.0
OD1 A:ASN170 2.2 17.9 1.0
O53 A:FBN304 2.2 31.9 1.0
O52 A:FBN304 2.4 30.0 1.0
CG A:ASP141 2.9 21.2 1.0
C46 A:FBN304 3.0 28.7 1.0
C45 A:FBN304 3.1 30.3 1.0
CG A:ASP169 3.1 26.3 1.0
OD2 A:ASP141 3.2 22.4 1.0
CG A:ASN170 3.2 20.3 1.0
ND2 A:ASN170 3.6 21.3 1.0
CB A:ASP169 3.7 23.6 1.0
NZ A:LYS144 3.9 21.9 1.0
O A:HOH224 4.0 42.3 1.0
OD1 A:ASP169 4.2 24.4 1.0
OE2 A:GLU199 4.3 29.9 1.0
CB A:ASP141 4.3 21.4 1.0
C47 A:FBN304 4.3 32.4 1.0
O A:MET40 4.3 30.9 1.0
C42 A:FBN304 4.5 33.4 1.0
CB A:ASN170 4.5 21.1 1.0
O A:ASP141 4.6 24.0 1.0
CA A:ASP141 4.7 23.4 1.0
CG2 A:VAL42 4.9 27.3 1.0
OE1 A:GLU199 4.9 28.1 1.0
CE A:LYS144 4.9 23.2 1.0
C A:ASP169 4.9 23.9 1.0
CA A:ASP169 4.9 23.9 1.0
CD A:GLU199 5.0 30.9 1.0
N A:ASN170 5.0 24.3 1.0
NZ A:LYS46 5.0 26.1 1.0

Reference:

H.Muranaka, M.Nakatsu, E.Tsuji, K.Okazaki. Hit to Lead: Comprehensive Strategy of De Novo Scaffold Generation By Fbdd. Part 2: Ligand Fishing Using Mass Spectrometry By Detection of Ligand-Protein Non-Covalent Complex After Matrix Click Chemistry To Be Published.
Page generated: Wed Aug 14 08:30:18 2024

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