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Magnesium in PDB 5tyq: Crystal Structure of A Holoenzyme Methyltransferase Involved in the Biosynthesis of Gentamicin

Protein crystallography data

The structure of Crystal Structure of A Holoenzyme Methyltransferase Involved in the Biosynthesis of Gentamicin, PDB code: 5tyq was solved by P.Bury, F.Huang, P.Leadlay, M.V.B.Dias, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.90 / 2.16
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 66.692, 66.922, 68.849, 90.00, 90.00, 90.00
R / Rfree (%) 19.4 / 21.6

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of A Holoenzyme Methyltransferase Involved in the Biosynthesis of Gentamicin (pdb code 5tyq). 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 Structure of A Holoenzyme Methyltransferase Involved in the Biosynthesis of Gentamicin, PDB code: 5tyq:

Magnesium binding site 1 out of 1 in 5tyq

Go back to Magnesium Binding Sites List in 5tyq
Magnesium binding site 1 out of 1 in the Crystal Structure of A Holoenzyme Methyltransferase Involved in the Biosynthesis of Gentamicin


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of A Holoenzyme Methyltransferase Involved in the Biosynthesis of Gentamicin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg402

b:22.5
occ:1.00
O A:HOH567 1.9 27.9 1.0
OD2 A:ASP206 2.2 27.3 1.0
OE2 A:GLU98 2.2 42.4 1.0
O A:HOH509 2.3 22.8 1.0
OE1 A:GLU98 2.6 51.0 1.0
CD A:GLU98 2.7 47.4 1.0
CG A:ASP206 2.9 16.5 1.0
OD1 A:ASP206 3.0 17.5 1.0
OE1 A:GLN101 4.1 17.1 1.0
O A:HOH595 4.2 17.9 1.0
CG A:GLU98 4.2 43.4 1.0
CB A:ASP206 4.4 16.0 1.0
O A:HOH575 4.4 28.9 1.0
OE1 A:GLU209 4.6 35.0 1.0
CB A:LEU208 4.7 10.1 1.0
O A:HOH550 4.8 20.7 1.0
CG1 A:VAL205 4.9 9.8 1.0

Reference:

P.D.S.Bury, F.Huang, S.Li, Y.Sun, P.F.Leadlay, M.V.B.Dias. Structural Basis of the Selectivity of Genn, An Aminoglycoside N-Methyltransferase Involved in Gentamicin Biosynthesis. Acs Chem. Biol. V. 12 2779 2017.
ISSN: ESSN 1554-8937
PubMed: 28876898
DOI: 10.1021/ACSCHEMBIO.7B00466
Page generated: Mon Sep 30 05:06:22 2024

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