Atomistry » Magnesium » PDB 2xni-2xzs » 2xz7
Atomistry »
  Magnesium »
    PDB 2xni-2xzs »
      2xz7 »

Magnesium in PDB 2xz7: Crystal Structure of the Phosphoenolpyruvate-Binding Domain of Enzyme I in Complex with Phosphoenolpyruvate From the Thermoanaerobacter Tengcongensis Pep-Sugar Phosphotransferase System (Pts)

Enzymatic activity of Crystal Structure of the Phosphoenolpyruvate-Binding Domain of Enzyme I in Complex with Phosphoenolpyruvate From the Thermoanaerobacter Tengcongensis Pep-Sugar Phosphotransferase System (Pts)

All present enzymatic activity of Crystal Structure of the Phosphoenolpyruvate-Binding Domain of Enzyme I in Complex with Phosphoenolpyruvate From the Thermoanaerobacter Tengcongensis Pep-Sugar Phosphotransferase System (Pts):
2.7.3.9;

Protein crystallography data

The structure of Crystal Structure of the Phosphoenolpyruvate-Binding Domain of Enzyme I in Complex with Phosphoenolpyruvate From the Thermoanaerobacter Tengcongensis Pep-Sugar Phosphotransferase System (Pts), PDB code: 2xz7 was solved by S.M.Waltersperger, A.E.Oberholzer, P.Schneider, U.Baumann, B.Erni, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 61.868 / 1.83
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 83.499, 92.125, 47.069, 90.00, 90.00, 90.00
R / Rfree (%) 16.48 / 19.46

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of the Phosphoenolpyruvate-Binding Domain of Enzyme I in Complex with Phosphoenolpyruvate From the Thermoanaerobacter Tengcongensis Pep-Sugar Phosphotransferase System (Pts) (pdb code 2xz7). 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 the Phosphoenolpyruvate-Binding Domain of Enzyme I in Complex with Phosphoenolpyruvate From the Thermoanaerobacter Tengcongensis Pep-Sugar Phosphotransferase System (Pts), PDB code: 2xz7:

Magnesium binding site 1 out of 1 in 2xz7

Go back to Magnesium Binding Sites List in 2xz7
Magnesium binding site 1 out of 1 in the Crystal Structure of the Phosphoenolpyruvate-Binding Domain of Enzyme I in Complex with Phosphoenolpyruvate From the Thermoanaerobacter Tengcongensis Pep-Sugar Phosphotransferase System (Pts)


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 the Phosphoenolpyruvate-Binding Domain of Enzyme I in Complex with Phosphoenolpyruvate From the Thermoanaerobacter Tengcongensis Pep-Sugar Phosphotransferase System (Pts) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg6081

b:12.4
occ:1.00
OD2 A:ASP455 2.4 24.5 1.0
OE1 A:GLU431 2.4 24.1 1.0
O1 A:PEP6080 2.5 17.3 1.0
O1P A:PEP6080 2.5 26.7 1.0
O2 A:PEP6080 2.6 24.6 1.0
O A:HOH2272 2.7 32.8 1.0
O A:HOH2080 2.8 19.7 1.0
P A:PEP6080 3.1 26.8 1.0
C1 A:PEP6080 3.3 19.2 1.0
C2 A:PEP6080 3.3 22.4 1.0
CG A:ASP455 3.3 26.2 1.0
CD A:GLU431 3.5 23.3 1.0
CB A:ASP455 3.7 16.3 1.0
OE2 A:GLU431 3.9 20.7 1.0
O2P A:PEP6080 4.0 23.2 1.0
OD2 A:ASP335 4.1 28.7 1.0
NH2 A:ARG465 4.2 41.9 1.0
O3P A:PEP6080 4.3 29.3 1.0
CE A:MET429 4.3 20.4 0.5
O A:HOH2371 4.3 47.7 1.0
NH1 A:ARG332 4.3 18.3 1.0
OD1 A:ASP455 4.4 33.3 1.0
O2' A:PEP6080 4.4 17.8 1.0
O A:HOH2275 4.6 29.4 1.0
O A:HOH2370 4.6 40.3 1.0
C3 A:PEP6080 4.6 25.8 1.0
N A:ASP455 4.7 16.0 1.0
CG A:GLU431 4.8 13.5 1.0
CB A:GLU431 4.8 17.5 1.0
CA A:ASP455 4.9 16.7 1.0

Reference:

V.Navdaeva, A.Zurbriggen, S.M.Waltersperger, P.Schneider, A.E.Oberholzer, P.Bahler, C.Bachler, A.Grieder, U.Baumann, B.Erni. Phosphoenolpyruvate: Sugar Phosphotransferase System From the Hyperthermophilic Thermoanaerobacter Tengcongensis. Biochemistry V. 50 1184 2011.
ISSN: ISSN 0006-2960
PubMed: 21250658
DOI: 10.1021/BI101721F
Page generated: Wed Aug 14 07:20:57 2024

Last articles

Mg in 2WTZ
Mg in 2WTY
Mg in 2WTP
Mg in 2WTO
Mg in 2WSS
Mg in 2WSB
Mg in 2WPD
Mg in 2WOQ
Mg in 2WOJ
Mg in 2WQS
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy