Magnesium in PDB 3crq: Structure of Trna Dimethylallyltransferase: Rna Modification Through A Channel

All present enzymatic activity of Structure of Trna Dimethylallyltransferase: Rna Modification Through A Channel:
2.5.1.8;

The structure of Structure of Trna Dimethylallyltransferase: Rna Modification Through A Channel, PDB code: 3crq was solved by R.H.Huang, W.Xie, C.Zhou, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.20
Space group	P 41
Cell size a, b, c (Å), α, β, γ (°)	76.312, 76.312, 57.532, 90.00, 90.00, 90.00
R / Rfree (%)	22 / 25

The binding sites of Magnesium atom in the Structure of Trna Dimethylallyltransferase: Rna Modification Through A Channel (pdb code 3crq). 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 Structure of Trna Dimethylallyltransferase: Rna Modification Through A Channel, PDB code: 3crq:

Magnesium binding site 1 out of 1 in the Structure of Trna Dimethylallyltransferase: Rna Modification Through A Channel


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Trna Dimethylallyltransferase: Rna Modification Through A Channel within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg324 b:32.1 occ:1.00 O7 A:DPO325 1.9 35.4 1.0 O3 A:DPO325 2.0 34.7 1.0 OG1 A:THR19 2.0 37.9 1.0 O A:HOH346 2.1 36.9 1.0 O A:HOH342 2.1 34.1 1.0 O A:HOH376 2.2 39.8 1.0 P2 A:DPO325 3.2 35.8 1.0 CB A:THR19 3.2 40.4 1.0 P1 A:DPO325 3.3 37.1 1.0 O4 A:DPO325 3.6 37.7 1.0 O2 A:DPO325 3.8 37.4 1.0 O5 A:DPO325 3.9 37.9 1.0 N A:THR19 4.0 37.9 1.0 O A:HOH378 4.1 33.7 1.0 CA A:THR19 4.2 40.7 1.0 CG2 A:THR19 4.3 41.2 1.0 O A:HOH341 4.3 26.4 1.0 O6 A:DPO325 4.4 33.2 1.0 O1 A:DPO325 4.5 37.7 1.0 O A:ALA50 4.7 31.7 1.0 O A:HOH331 4.7 27.3 1.0 O A:HOH362 4.9 33.5 1.0

W.Xie, C.Zhou, R.H.Huang. Structure of Trna Dimethylallyltransferase: Rna Modification Through A Channel J.Mol.Biol. V. 367 872 2007.
ISSN: ISSN 0022-2836
PubMed: 17292915
DOI: 10.1016/J.JMB.2007.01.048