Atomistry » Magnesium » PDB 5v6s-5vp0 » 5v8t
Atomistry »
  Magnesium »
    PDB 5v6s-5vp0 »
      5v8t »

Magnesium in PDB 5v8t: Crystal Structure of Smt Fusion Peptidyl-Prolyl Cis-Trans Isomerase From Burkholderia Pseudomallei Complexed with SF354

Enzymatic activity of Crystal Structure of Smt Fusion Peptidyl-Prolyl Cis-Trans Isomerase From Burkholderia Pseudomallei Complexed with SF354

All present enzymatic activity of Crystal Structure of Smt Fusion Peptidyl-Prolyl Cis-Trans Isomerase From Burkholderia Pseudomallei Complexed with SF354:
5.2.1.8;

Protein crystallography data

The structure of Crystal Structure of Smt Fusion Peptidyl-Prolyl Cis-Trans Isomerase From Burkholderia Pseudomallei Complexed with SF354, PDB code: 5v8t was solved by D.D.Lorimer, D.M.Dranow, F.Seufert, J.Abendroth, U.Holzgrabe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.92 / 2.10
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 60.640, 32.500, 99.350, 90.00, 96.73, 90.00
R / Rfree (%) 18.4 / 22.1

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Smt Fusion Peptidyl-Prolyl Cis-Trans Isomerase From Burkholderia Pseudomallei Complexed with SF354 (pdb code 5v8t). 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 Smt Fusion Peptidyl-Prolyl Cis-Trans Isomerase From Burkholderia Pseudomallei Complexed with SF354, PDB code: 5v8t:

Magnesium binding site 1 out of 1 in 5v8t

Go back to Magnesium Binding Sites List in 5v8t
Magnesium binding site 1 out of 1 in the Crystal Structure of Smt Fusion Peptidyl-Prolyl Cis-Trans Isomerase From Burkholderia Pseudomallei Complexed with SF354


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 Smt Fusion Peptidyl-Prolyl Cis-Trans Isomerase From Burkholderia Pseudomallei Complexed with SF354 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg202

b:7.8
occ:1.00
 OD1 B:ASP51 2.1 21.6 1.0
O A:HOH334 2.2 15.3 1.0
O B:HOH336 2.2 20.4 1.0
OD1 A:ASP51 2.2 20.2 1.0
O B:PRO52 2.3 20.5 1.0
O A:PRO52 2.3 16.3 1.0
CG A:ASP51 2.9 18.9 1.0
OD2 A:ASP51 3.0 18.6 1.0
CG B:ASP51 3.0 22.5 1.0
OD2 B:ASP51 3.4 23.2 1.0
C B:PRO52 3.5 18.5 1.0
C A:PRO52 3.5 14.3 1.0
N B:PRO52 4.1 17.4 1.0
C B:ASP51 4.1 17.5 1.0
C A:ASP51 4.1 13.7 1.0
N A:PRO52 4.2 13.0 1.0
CB A:ASP51 4.2 18.2 1.0
CB B:ASP51 4.3 21.2 1.0
CA B:PRO52 4.3 17.8 1.0
O A:ASP51 4.4 13.8 1.0
CA A:PRO52 4.4 13.1 1.0
N B:PHE53 4.4 16.9 1.0
O B:ASP51 4.4 17.3 1.0
O A:HOH326 4.4 17.5 1.0
N A:PHE53 4.5 13.4 1.0
CA B:ASP51 4.5 18.9 1.0
O B:HOH307 4.5 25.9 1.0
CA A:ASP51 4.5 16.6 1.0
CA B:PHE53 4.6 16.9 1.0
CA A:PHE53 4.6 12.8 1.0
CD B:PRO52 4.6 17.9 1.0
CD A:PRO52 4.7 13.8 1.0
O B:HOH340 4.8 28.6 1.0
CB B:PRO52 4.8 17.9 1.0
O A:HOH427 4.9 25.1 1.0
CB A:PRO52 4.9 13.3 1.0

Reference:

D.D.Lorimer, D.M.Dranow, F.Seufert, J.Abendroth, U.Holzgrabe. Crystal Structure of Smt Fusion Peptidyl-Prolyl Cis-Trans Isomerase From Burkholderia Pseudomallei Complexed with SF354 To Be Published.
Page generated: Mon Sep 30 06:06:35 2024

Last articles

Zn in 9MJ5
Zn in 9HNW
Zn in 9G0L
Zn in 9FNE
Zn in 9DZN
Zn in 9E0I
Zn in 9D32
Zn in 9DAK
Zn in 8ZXC
Zn in 8ZUF
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy