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Magnesium in PDB 5klx: Crystal Structure of Smt Fusion Peptidyl-Prolyl Cis-Trans Isomerase From Burkholderia Pseudomallei Complexed with SF110

Enzymatic activity of Crystal Structure of Smt Fusion Peptidyl-Prolyl Cis-Trans Isomerase From Burkholderia Pseudomallei Complexed with SF110

All present enzymatic activity of Crystal Structure of Smt Fusion Peptidyl-Prolyl Cis-Trans Isomerase From Burkholderia Pseudomallei Complexed with SF110:
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 SF110, PDB code: 5klx was solved by D.Fox Iii, T.E.Edwards, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 37.79 / 2.45
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 107.890, 34.110, 119.920, 90.00, 115.45, 90.00
R / Rfree (%) 19.8 / 25.6

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 SF110 (pdb code 5klx). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of Smt Fusion Peptidyl-Prolyl Cis-Trans Isomerase From Burkholderia Pseudomallei Complexed with SF110, PDB code: 5klx:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 5klx

Go back to Magnesium Binding Sites List in 5klx
Magnesium binding site 1 out of 2 in the Crystal Structure of Smt Fusion Peptidyl-Prolyl Cis-Trans Isomerase From Burkholderia Pseudomallei Complexed with SF110


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 SF110 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg202

b:14.7
occ:1.00
OD1 A:ASP51 2.0 38.1 1.0
O A:PRO52 2.2 22.8 1.0
O A:HOH349 2.5 39.9 1.0
CG A:ASP51 2.8 36.4 1.0
OD2 A:ASP51 3.0 41.4 1.0
C A:PRO52 3.4 20.7 1.0
O A:HOH303 3.8 28.8 1.0
C A:ASP51 4.0 37.9 1.0
N A:PRO52 4.1 38.6 1.0
O D:HOH326 4.2 39.9 1.0
O A:ASP51 4.2 30.4 1.0
CB A:ASP51 4.2 36.0 1.0
O A:HOH304 4.3 57.0 1.0
CA A:PRO52 4.3 29.1 1.0
N A:PHE53 4.4 19.3 1.0
CA A:ASP51 4.5 38.6 1.0
CA A:PHE53 4.6 19.6 1.0
CB A:PRO52 4.8 31.1 1.0
CD A:PRO52 4.9 27.0 1.0

Magnesium binding site 2 out of 2 in 5klx

Go back to Magnesium Binding Sites List in 5klx
Magnesium binding site 2 out of 2 in the Crystal Structure of Smt Fusion Peptidyl-Prolyl Cis-Trans Isomerase From Burkholderia Pseudomallei Complexed with SF110


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of Smt Fusion Peptidyl-Prolyl Cis-Trans Isomerase From Burkholderia Pseudomallei Complexed with SF110 within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg202

b:19.5
occ:1.00
OD1 B:ASP51 2.1 51.5 1.0
OD1 D:ASP51 2.1 49.2 1.0
O D:PRO52 2.1 29.5 1.0
O B:PRO52 2.3 33.9 1.0
O D:HOH311 2.6 29.6 1.0
CG B:ASP51 2.7 50.0 1.0
OD2 B:ASP51 2.7 46.8 1.0
O B:HOH318 2.8 35.0 1.0
CG D:ASP51 3.1 44.2 1.0
C D:PRO52 3.3 37.2 1.0
OD2 D:ASP51 3.5 44.3 1.0
C B:PRO52 3.6 38.3 1.0
O B:HOH307 4.0 37.5 1.0
N D:PRO52 4.1 50.5 1.0
C D:ASP51 4.1 47.0 1.0
O B:HOH310 4.1 44.5 1.0
CB B:ASP51 4.2 50.5 1.0
N D:PHE53 4.2 27.9 1.0
CA D:PRO52 4.3 44.5 1.0
C B:ASP51 4.3 49.9 1.0
CA D:PHE53 4.4 27.8 1.0
N B:PRO52 4.4 46.5 1.0
CB D:ASP51 4.4 36.4 1.0
O D:HOH327 4.4 35.1 1.0
O D:ASP51 4.5 49.1 1.0
N B:PHE53 4.5 33.3 1.0
CA B:PRO52 4.5 37.8 1.0
O B:ASP51 4.5 47.7 1.0
CA D:ASP51 4.6 41.6 1.0
CA B:PHE53 4.6 31.9 1.0
CD D:PRO52 4.6 36.0 1.0
CA B:ASP51 4.7 51.4 1.0
CB D:PRO52 4.9 41.3 1.0
N D:ALA54 4.9 43.3 1.0

Reference:

D.D.Lorimer, D.Fox Iii, F.Seufert, T.E.Edwards, U.Holzgrabe. Crystal Structure of Smt Fusion Peptidyl-Prolyl Cis-Trans Isomerase From Burkholderia Pseudomallei Complexed with SF110 To Be Published.
Page generated: Sun Sep 29 19:08:34 2024

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