Calcium in PDB 6o4a: Crystal Structure of Smt Fusion Peptidyl-Prolyl Cis-Trans Isomerase From Burkholderia Pseudomallei Complexed with SF355

All present enzymatic activity of Crystal Structure of Smt Fusion Peptidyl-Prolyl Cis-Trans Isomerase From Burkholderia Pseudomallei Complexed with SF355:
5.2.1.8;

The structure of Crystal Structure of Smt Fusion Peptidyl-Prolyl Cis-Trans Isomerase From Burkholderia Pseudomallei Complexed with SF355, PDB code: 6o4a was solved by Seattle Structural Genomics Center For Infectious Disease (Ssgcid), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	44.55 / 2.10
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	62.820, 32.650, 178.190, 90.00, 90.01, 90.00
R / Rfree (%)	15.7 / 20.8

The binding sites of Calcium atom in the Crystal Structure of Smt Fusion Peptidyl-Prolyl Cis-Trans Isomerase From Burkholderia Pseudomallei Complexed with SF355 (pdb code 6o4a). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Crystal Structure of Smt Fusion Peptidyl-Prolyl Cis-Trans Isomerase From Burkholderia Pseudomallei Complexed with SF355, PDB code: 6o4a:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Crystal Structure of Smt Fusion Peptidyl-Prolyl Cis-Trans Isomerase From Burkholderia Pseudomallei Complexed with SF355


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of Smt Fusion Peptidyl-Prolyl Cis-Trans Isomerase From Burkholderia Pseudomallei Complexed with SF355 within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca201 b:14.0 occ:1.00 O B:PRO52 2.3 13.8 1.0 O A:HOH390 2.3 11.5 1.0 OD1 B:ASP51 2.4 14.1 1.0 O A:PRO52 2.4 13.2 1.0 OD1 A:ASP51 2.5 14.4 1.0 O B:HOH354 2.6 16.9 1.0 OD2 A:ASP51 2.6 14.0 1.0 CG A:ASP51 2.9 22.7 1.0 CG B:ASP51 3.3 19.9 1.0 C B:PRO52 3.5 12.7 1.0 C A:PRO52 3.6 17.5 1.0 OD2 B:ASP51 3.7 16.9 1.0 O A:HOH344 3.9 21.0 1.0 C B:ASP51 4.3 15.1 1.0 CB A:ASP51 4.3 15.6 1.0 N B:PRO52 4.3 17.9 1.0 CA B:PHE53 4.3 10.9 1.0 N A:PRO52 4.3 12.9 1.0 C A:ASP51 4.3 14.8 1.0 N B:PHE53 4.4 11.4 1.0 O A:HOH357 4.4 27.8 1.0 O B:ASP51 4.5 14.2 1.0 CA A:PRO52 4.5 16.0 1.0 CB B:ASP51 4.5 20.5 1.0 CA B:PRO52 4.5 17.2 1.0 O A:ASP51 4.5 12.4 1.0 N A:PHE53 4.6 12.7 1.0 O B:HOH362 4.6 10.0 1.0 CA B:ASP51 4.6 19.4 1.0 CA A:PHE53 4.7 12.4 1.0 CD A:PRO52 4.8 16.0 1.0 CA A:ASP51 4.8 18.2 1.0 O A:HOH369 4.9 21.5 1.0 O A:HOH425 4.9 35.7 1.0 CD B:PRO52 4.9 17.8 1.0 N B:ALA54 5.0 12.3 1.0

Calcium binding site 2 out of 2 in the Crystal Structure of Smt Fusion Peptidyl-Prolyl Cis-Trans Isomerase From Burkholderia Pseudomallei Complexed with SF355


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Crystal Structure of Smt Fusion Peptidyl-Prolyl Cis-Trans Isomerase From Burkholderia Pseudomallei Complexed with SF355 within 5.0Å range: probe atom residue distance (Å) B Occ C:Ca201 b:15.5 occ:1.00 O D:PRO52 2.3 13.4 1.0 O C:PRO52 2.4 14.9 1.0 O C:HOH397 2.4 15.8 1.0 OD1 D:ASP51 2.4 15.0 1.0 O D:HOH323 2.6 23.4 1.0 OD1 C:ASP51 2.6 15.3 1.0 OD2 C:ASP51 2.6 16.1 1.0 CG C:ASP51 2.9 21.2 1.0 CG D:ASP51 3.3 23.0 1.0 C D:PRO52 3.5 13.7 1.0 C C:PRO52 3.6 13.3 1.0 OD2 D:ASP51 3.7 14.8 1.0 O C:HOH324 4.1 21.5 1.0 C D:ASP51 4.3 15.8 1.0 CB C:ASP51 4.3 17.8 1.0 CA D:PHE53 4.3 13.5 1.0 N C:PRO52 4.3 13.6 1.0 C C:ASP51 4.3 13.7 1.0 N D:PRO52 4.3 17.4 1.0 N D:PHE53 4.4 12.1 1.0 O C:HOH358 4.4 30.5 1.0 O D:ASP51 4.4 16.1 1.0 CA C:PRO52 4.5 12.8 1.0 O D:HOH359 4.5 9.9 1.0 N C:PHE53 4.5 13.7 1.0 O C:ASP51 4.5 13.1 1.0 CB D:ASP51 4.5 21.7 1.0 CA D:PRO52 4.6 17.9 1.0 CA D:ASP51 4.6 19.9 1.0 CA C:PHE53 4.7 17.0 1.0 CD C:PRO52 4.8 17.6 1.0 CA C:ASP51 4.8 17.2 1.0 O C:HOH418 4.8 32.9 1.0 O C:HOH368 4.9 21.8 1.0 N D:ALA54 4.9 12.5 1.0 CD D:PRO52 5.0 15.6 1.0

J.Iwasaki, D.D.Lorimer, M.Vivoli, N.J.Harmer, E.A.Kibble, C.S.Peacock, J.Abendroth, S.J.Mayclin, D.M.Dranow, P.G.Pierce, D.Fox Iii, M.Lewis, N.Bzdyl, S.Kristensen, J.W.Schmidberger, C.B.Bond, F.Seufert, J.Schmitz, I.H.Norville, P.J.Myler, U.Holzgrabe, M.Sarkar-Tyson. Crystal Structure of Smt Fusion Peptidyl-Prolyl Cis-Trans Isomerase From Burkholderia Pseudomallei Complexed with SF355 To Be Published.