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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

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