Atomistry » Magnesium » PDB 1h7q-1hx9 » 1ha3
Atomistry »
  Magnesium »
    PDB 1h7q-1hx9 »
      1ha3 »

Magnesium in PDB 1ha3: Elongation Factor Tu in Complex with Aurodox

Enzymatic activity of Elongation Factor Tu in Complex with Aurodox

All present enzymatic activity of Elongation Factor Tu in Complex with Aurodox:
3.1.5.1;

Protein crystallography data

The structure of Elongation Factor Tu in Complex with Aurodox, PDB code: 1ha3 was solved by L.Vogeley, G.J.Palm, J.R.Mesters, R.Hilgenfeld, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.00
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 69.000, 101.400, 79.100, 90.00, 113.60, 90.00
R / Rfree (%) 19.1 / 22.1

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Elongation Factor Tu in Complex with Aurodox (pdb code 1ha3). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Elongation Factor Tu in Complex with Aurodox, PDB code: 1ha3:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 1ha3

Go back to Magnesium Binding Sites List in 1ha3
Magnesium binding site 1 out of 2 in the Elongation Factor Tu in Complex with Aurodox


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Elongation Factor Tu in Complex with Aurodox within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg407

b:22.8
occ:1.00
O A:HOH2018 2.0 21.1 1.0
OG1 A:THR25 2.1 23.6 1.0
O2B A:GDP406 2.1 22.4 1.0
O A:HOH2043 2.1 21.2 1.0
O A:HOH2258 2.1 18.7 1.0
O A:HOH2260 2.2 18.2 1.0
CB A:THR25 3.2 23.4 1.0
PB A:GDP406 3.3 22.0 1.0
O1B A:GDP406 3.5 21.5 1.0
N A:THR25 3.8 22.6 1.0
OD2 A:ASP81 4.1 22.0 1.0
O A:HOH2027 4.1 43.4 1.0
O1A A:GDP406 4.1 19.3 1.0
OD1 A:ASP51 4.1 67.8 1.0
CA A:THR25 4.1 23.9 1.0
O3B A:GDP406 4.2 20.6 1.0
O A:HOH2042 4.3 33.6 1.0
CG2 A:THR25 4.3 24.9 1.0
O3A A:GDP406 4.3 21.0 1.0
OD1 A:ASP81 4.4 19.7 1.0
O A:CYS82 4.4 21.8 1.0
CA A:PRO83 4.5 20.8 1.0
O A:PRO83 4.5 20.6 1.0
CB A:LYS24 4.5 21.5 1.0
CE A:LYS24 4.5 20.9 1.0
PA A:GDP406 4.6 24.0 1.0
CG A:ASP81 4.6 21.4 1.0
O2A A:GDP406 4.8 21.7 1.0
O A:HOH2261 4.8 30.8 1.0
C A:LYS24 4.8 23.1 1.0
NZ A:LYS24 4.9 18.2 1.0
C A:PRO83 4.9 20.9 1.0

Magnesium binding site 2 out of 2 in 1ha3

Go back to Magnesium Binding Sites List in 1ha3
Magnesium binding site 2 out of 2 in the Elongation Factor Tu in Complex with Aurodox


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Elongation Factor Tu in Complex with Aurodox within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg407

b:22.6
occ:1.00
O B:HOH2311 2.0 16.9 1.0
O3B B:GDP406 2.0 18.7 1.0
O B:HOH2019 2.1 20.9 1.0
OG1 B:THR25 2.1 20.7 1.0
O B:HOH2319 2.1 20.2 1.0
O B:HOH2051 2.2 16.9 1.0
PB B:GDP406 3.2 20.1 1.0
CB B:THR25 3.2 20.8 1.0
O2B B:GDP406 3.3 20.1 1.0
N B:THR25 3.8 19.4 1.0
OD2 B:ASP81 4.0 23.1 1.0
CA B:THR25 4.1 21.3 1.0
O1A B:GDP406 4.1 19.0 1.0
O B:HOH2056 4.2 50.1 1.0
O1B B:GDP406 4.2 22.2 1.0
O3A B:GDP406 4.3 20.4 1.0
CG2 B:THR25 4.4 22.2 1.0
O B:HOH2119 4.4 42.6 1.0
CE B:LYS24 4.4 20.6 1.0
O B:HOH2049 4.4 39.6 1.0
OD1 B:ASP81 4.4 22.4 1.0
CB B:LYS24 4.5 19.5 1.0
O B:PRO83 4.5 20.3 1.0
O B:CYS82 4.5 21.5 1.0
O B:HOH2013 4.5 45.7 1.0
O B:HOH2312 4.6 32.3 1.0
PA B:GDP406 4.6 21.6 1.0
CA B:PRO83 4.6 19.9 1.0
CG B:ASP81 4.6 24.2 1.0
C B:LYS24 4.8 20.8 1.0
O2A B:GDP406 4.8 21.2 1.0
NZ B:LYS24 4.9 17.7 1.0
C B:PRO83 5.0 19.5 1.0

Reference:

L.Vogeley, G.J.Palm, J.R.Mesters, R.Hilgenfeld. Conformational Change of Elongation Factor Tu Induced By Antibiotic Binding: Crystal Structure of the Complex Between Ef-Tu:Gdp and Aurodox J.Biol.Chem. V. 276 17149 2001.
ISSN: ISSN 0021-9258
PubMed: 11278992
DOI: 10.1074/JBC.M100017200
Page generated: Mon Dec 14 05:58:58 2020

Last articles

Zn in 7L0B
Zn in 7KZZ
Zn in 7KZL
Zn in 7L3O
Zn in 7L52
Zn in 7L6T
Zn in 7KZ7
Zn in 7L6R
Zn in 7KKM
Zn in 7KKQ
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy