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Chlorine in PDB 4yq0: Crystal Structure of Trmd, A M1G37 Trna Methyltransferase with Sam- Competitive Compounds

Enzymatic activity of Crystal Structure of Trmd, A M1G37 Trna Methyltransferase with Sam- Competitive Compounds

All present enzymatic activity of Crystal Structure of Trmd, A M1G37 Trna Methyltransferase with Sam- Competitive Compounds:
2.1.1.228;

Protein crystallography data

The structure of Crystal Structure of Trmd, A M1G37 Trna Methyltransferase with Sam- Competitive Compounds, PDB code: 4yq0 was solved by P.A.Elkins, W.G.Bonnette, J.A.Stuckey, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.56 / 1.76
Space group H 3 2
Cell size a, b, c (Å), α, β, γ (°) 94.746, 94.746, 178.511, 90.00, 90.00, 120.00
R / Rfree (%) 16.6 / 18.9

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Trmd, A M1G37 Trna Methyltransferase with Sam- Competitive Compounds (pdb code 4yq0). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of Trmd, A M1G37 Trna Methyltransferase with Sam- Competitive Compounds, PDB code: 4yq0:

Chlorine binding site 1 out of 1 in 4yq0

Go back to Chlorine Binding Sites List in 4yq0
Chlorine binding site 1 out of 1 in the Crystal Structure of Trmd, A M1G37 Trna Methyltransferase with Sam- Competitive Compounds


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Trmd, A M1G37 Trna Methyltransferase with Sam- Competitive Compounds within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl301

b:25.5
occ:1.00
 CL A:4FM301 0.0 25.5 1.0
C7 A:4FM301 1.7 25.4 1.0
C6 A:4FM301 2.7 22.8 1.0
C8 A:4FM301 2.7 24.0 1.0
H6 A:4FM301 2.8 27.4 1.0
H7 A:4FM301 2.9 28.8 1.0
O A:ARG114 3.1 17.9 1.0
CA A:GLY117 3.2 25.1 1.0
N A:GLY117 3.4 20.1 1.0
C A:GLY117 3.4 22.5 1.0
OH A:TYR86 3.4 19.2 1.0
CA A:GLY113 3.5 17.6 1.0
N A:ARG114 3.5 17.0 1.0
C A:GLY113 3.6 19.6 1.0
O A:GLY117 3.7 15.6 1.0
C A:ARG114 3.8 17.7 1.0
C5 A:4FM301 4.0 23.4 1.0
N A:ILE118 4.0 18.6 1.0
C9 A:4FM301 4.0 24.5 1.0
CG2 A:ILE118 4.1 20.3 1.0
CA A:ARG114 4.2 15.0 0.2
CA A:ARG114 4.2 15.7 0.8
O A:TYR115 4.2 18.9 1.0
C A:GLU116 4.4 25.5 1.0
O A:GLY113 4.4 17.3 1.0
C4 A:4FM301 4.5 26.8 1.0
C A:TYR115 4.5 21.7 1.0
O A:HOH425 4.6 30.4 1.0
O A:HOH570 4.6 50.0 1.0
CZ A:TYR86 4.6 16.4 1.0
N A:GLY113 4.7 16.8 1.0
CG A:MET62 4.8 13.2 0.4
H5 A:4FM301 4.8 28.0 1.0
N A:TYR115 4.8 17.1 1.0
SD A:MET62 4.8 13.9 0.6
N A:GLU116 4.8 21.3 1.0
H8 A:4FM301 4.9 29.4 1.0
CG A:MET62 4.9 11.5 0.6
CE1 A:TYR86 5.0 16.1 1.0

Reference:

P.A.Elkins, W.G.Bonnette, J.A.Stuckey. Crystal Structure of Trmd, A M1G37 Trna Methyltransferase with Sam-Competitive Compounds To Be Published.
Page generated: Fri Jul 26 04:13:13 2024

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