Calcium in PDB 6o49: Crystal Structure of Smt Fusion Peptidyl-Prolyl Cis-Trans Isomerase From Burkholderia Pseudomallei Complexed with SF339

All present enzymatic activity of Crystal Structure of Smt Fusion Peptidyl-Prolyl Cis-Trans Isomerase From Burkholderia Pseudomallei Complexed with SF339:
5.2.1.8;

The structure of Crystal Structure of Smt Fusion Peptidyl-Prolyl Cis-Trans Isomerase From Burkholderia Pseudomallei Complexed with SF339, PDB code: 6o49 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)	48.13 / 1.85
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	58.860, 33.600, 98.140, 90.00, 101.21, 90.00
R / Rfree (%)	16.8 / 21.1

The binding sites of Calcium atom in the Crystal Structure of Smt Fusion Peptidyl-Prolyl Cis-Trans Isomerase From Burkholderia Pseudomallei Complexed with SF339 (pdb code 6o49). 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 SF339, PDB code: 6o49:
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 SF339


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 SF339 within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca202 b:13.3 occ:1.00 O A:PRO52 2.3 12.5 1.0 O B:PRO52 2.3 14.5 1.0 OD1 B:ASP51 2.3 16.9 1.0 O A:HOH395 2.3 15.7 1.0 OD1 A:ASP51 2.4 25.7 1.0 O B:HOH372 2.5 12.9 1.0 OD2 A:ASP51 2.7 20.3 1.0 CG A:ASP51 2.8 22.0 1.0 CG B:ASP51 3.3 21.6 1.0 C A:PRO52 3.5 12.9 1.0 C B:PRO52 3.5 9.9 1.0 OD2 B:ASP51 3.7 17.6 1.0 N A:PRO52 4.0 13.1 1.0 O A:HOH347 4.1 20.3 1.0 C A:ASP51 4.2 14.0 1.0 CB A:ASP51 4.2 25.8 1.0 C B:ASP51 4.2 12.5 1.0 O A:HOH321 4.2 27.8 1.0 O B:ASP51 4.3 13.6 1.0 CA A:PRO52 4.3 11.9 1.0 N B:PRO52 4.3 12.3 1.0 CA B:PHE53 4.4 9.8 1.0 N B:PHE53 4.4 9.3 1.0 CD A:PRO52 4.4 13.9 1.0 N A:PHE53 4.5 11.7 1.0 CA B:PRO52 4.5 10.9 1.0 O B:HOH343 4.5 14.4 1.0 O A:ASP51 4.5 14.7 1.0 CB B:ASP51 4.6 23.3 1.0 CA A:ASP51 4.6 20.7 1.0 O A:HOH472 4.6 20.5 1.0 CA B:ASP51 4.7 12.3 1.0 CB A:PRO52 4.7 19.3 1.0 CA A:PHE53 4.8 13.4 1.0 O A:HOH307 4.8 22.1 1.0 N B:ALA54 4.9 9.4 1.0 CD B:PRO52 5.0 12.8 1.0 O A:HOH309 5.0 16.4 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 SF339


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 SF339 within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca202 b:14.6 occ:1.00 O B:VAL113 2.4 17.2 1.0 O B:HOH318 2.4 10.7 1.0 OD1 B:ASP112 2.4 17.6 1.0 O B:HOH304 2.5 18.6 1.0 CG B:ASP112 3.4 13.4 1.0 C B:VAL113 3.5 19.7 1.0 OD2 B:ASP112 3.7 14.1 1.0 OXT B:VAL113 4.1 15.6 1.0 N B:VAL113 4.4 13.4 1.0 O B:THR28 4.4 14.0 1.0 CA B:VAL113 4.5 11.6 1.0 O B:HOH354 4.5 14.2 1.0 CB B:ASP112 4.7 10.5 1.0 C B:ASP112 4.9 15.9 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 SF339 To Be Published.