Atomistry » Magnesium » PDB 2qrn-2r1y » 2qui
Atomistry »
  Magnesium »
    PDB 2qrn-2r1y »
      2qui »

Magnesium in PDB 2qui: Crystal Structures of Human Tryptophanyl-Trna Synthetase in Complex with Tryptophanamide and Atp

Enzymatic activity of Crystal Structures of Human Tryptophanyl-Trna Synthetase in Complex with Tryptophanamide and Atp

All present enzymatic activity of Crystal Structures of Human Tryptophanyl-Trna Synthetase in Complex with Tryptophanamide and Atp:
6.1.1.2;

Protein crystallography data

The structure of Crystal Structures of Human Tryptophanyl-Trna Synthetase in Complex with Tryptophanamide and Atp, PDB code: 2qui was solved by N.Shen, J.P.Ding, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 2.40
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 79.700, 79.700, 383.200, 90.00, 90.00, 90.00
R / Rfree (%) 21.1 / 23.8

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structures of Human Tryptophanyl-Trna Synthetase in Complex with Tryptophanamide and Atp (pdb code 2qui). 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 Human Tryptophanyl-Trna Synthetase in Complex with Tryptophanamide and Atp, PDB code: 2qui:

Magnesium binding site 1 out of 1 in 2qui

Go back to Magnesium Binding Sites List in 2qui
Magnesium binding site 1 out of 1 in the Crystal Structures of Human Tryptophanyl-Trna Synthetase in Complex with Tryptophanamide and Atp


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 Human Tryptophanyl-Trna Synthetase in Complex with Tryptophanamide and Atp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg500

b:75.0
occ:1.00
 O2A A:ATP502 2.7 0.4 1.0
OG A:SER165 2.8 48.6 1.0
O1B A:ATP502 2.8 0.7 1.0
NZ A:LYS200 2.9 46.7 1.0
O A:HOH622 3.5 58.0 1.0
CZ3 A:TRP88 3.7 0.9 1.0
CE A:LYS200 3.8 45.6 1.0
CB A:SER165 3.9 44.2 1.0
PA A:ATP502 3.9 0.7 1.0
O3A A:ATP502 4.0 1.0 1.0
PB A:ATP502 4.0 0.2 1.0
CE3 A:TRP88 4.0 0.5 1.0
CD A:LYS200 4.2 41.5 1.0
C5' A:ATP502 4.5 0.1 1.0
CD A:LYS204 4.7 62.0 1.0
O5' A:ATP502 4.7 0.9 1.0
O1G A:ATP502 4.8 0.6 1.0
O3G A:ATP502 4.8 0.1 1.0
CH2 A:TRP88 4.9 0.7 1.0
O2B A:ATP502 4.9 0.8 1.0

Reference:

N.Shen, M.Zhou, B.Yang, Y.Yu, X.Dong, J.Ding. Catalytic Mechanism of the Tryptophan Activation Reaction Revealed By Crystal Structures of Human Tryptophanyl-Trna Synthetase in Different Enzymatic States Nucleic Acids Res. V. 36 1288 2008.
ISSN: ISSN 0305-1048
PubMed: 18180246
DOI: 10.1093/NAR/GKM1153
Page generated: Wed Aug 14 03:10:25 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy