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Calcium in PDB 4dz3: Crystal Structure of A Peptidyl-Prolyl Cis-Trans Isomerase with Surface Mutation M61H From Burkholderia Pseudomallei Complexed with FK506

Enzymatic activity of Crystal Structure of A Peptidyl-Prolyl Cis-Trans Isomerase with Surface Mutation M61H From Burkholderia Pseudomallei Complexed with FK506

All present enzymatic activity of Crystal Structure of A Peptidyl-Prolyl Cis-Trans Isomerase with Surface Mutation M61H From Burkholderia Pseudomallei Complexed with FK506:
5.2.1.8;

Protein crystallography data

The structure of Crystal Structure of A Peptidyl-Prolyl Cis-Trans Isomerase with Surface Mutation M61H From Burkholderia Pseudomallei Complexed with FK506, PDB code: 4dz3 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) 47.72 / 2.00
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 48.980, 106.580, 107.160, 90.00, 90.00, 90.00
R / Rfree (%) 19.2 / 21.9

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of A Peptidyl-Prolyl Cis-Trans Isomerase with Surface Mutation M61H From Burkholderia Pseudomallei Complexed with FK506 (pdb code 4dz3). 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 A Peptidyl-Prolyl Cis-Trans Isomerase with Surface Mutation M61H From Burkholderia Pseudomallei Complexed with FK506, PDB code: 4dz3:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in 4dz3

Go back to Calcium Binding Sites List in 4dz3
Calcium binding site 1 out of 2 in the Crystal Structure of A Peptidyl-Prolyl Cis-Trans Isomerase with Surface Mutation M61H From Burkholderia Pseudomallei Complexed with FK506


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 A Peptidyl-Prolyl Cis-Trans Isomerase with Surface Mutation M61H From Burkholderia Pseudomallei Complexed with FK506 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca202

b:20.4
occ:1.00
 OD1 B:ASP51 2.3 23.0 1.0
O B:PRO52 2.4 19.6 1.0
O B:HOH333 2.4 16.1 1.0
OXT A:VAL113 2.4 22.5 1.0
OD2 A:ASP112 2.4 24.4 1.0
O B:HOH321 2.4 16.6 1.0
OD1 A:ASP112 2.6 24.4 1.0
CG A:ASP112 2.9 23.7 1.0
CG B:ASP51 3.3 23.7 1.0
C B:PRO52 3.5 18.8 1.0
C A:VAL113 3.6 21.3 1.0
OD2 B:ASP51 3.8 24.4 1.0
N B:PRO52 4.1 20.5 1.0
N A:VAL113 4.2 20.6 1.0
O A:VAL113 4.2 21.7 1.0
C B:ASP51 4.3 21.2 1.0
CA B:PRO52 4.3 19.4 1.0
CB A:ASP112 4.4 22.6 1.0
O A:HOH343 4.4 37.6 1.0
O A:HOH332 4.4 27.2 1.0
CD B:PRO52 4.5 21.4 1.0
CA A:VAL113 4.5 20.1 1.0
CB B:ASP51 4.6 23.7 1.0
N B:PHE53 4.6 17.8 1.0
CB B:PRO52 4.6 19.5 1.0
O B:ASP51 4.6 20.3 1.0
O B:HOH338 4.7 28.6 1.0
CA B:ASP51 4.7 23.1 1.0
CA B:PHE53 4.8 17.4 1.0
O A:HOH342 4.9 27.9 1.0
C A:ASP112 4.9 20.2 1.0

Calcium binding site 2 out of 2 in 4dz3

Go back to Calcium Binding Sites List in 4dz3
Calcium binding site 2 out of 2 in the Crystal Structure of A Peptidyl-Prolyl Cis-Trans Isomerase with Surface Mutation M61H From Burkholderia Pseudomallei Complexed with FK506


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 A Peptidyl-Prolyl Cis-Trans Isomerase with Surface Mutation M61H From Burkholderia Pseudomallei Complexed with FK506 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ca202

b:18.1
occ:1.00
 O A:HOH321 2.3 21.6 1.0
O A:PRO52 2.3 23.5 1.0
OD1 A:ASP51 2.4 28.6 1.0
O B:VAL113 2.4 19.5 1.0
O A:HOH326 2.4 22.2 1.0
OD2 B:ASP112 2.4 20.2 1.0
OD1 B:ASP112 2.6 20.1 1.0
CG B:ASP112 2.9 19.6 1.0
CG A:ASP51 3.4 29.3 1.0
C A:PRO52 3.5 22.9 1.0
C B:VAL113 3.6 19.1 1.0
OD2 A:ASP51 3.9 29.8 1.0
O A:HOH355 4.1 37.5 1.0
N A:PRO52 4.1 25.6 1.0
N B:VAL113 4.2 18.1 1.0
OXT B:VAL113 4.3 19.6 1.0
C A:ASP51 4.3 26.4 1.0
CA A:PRO52 4.3 23.8 1.0
CB B:ASP112 4.4 18.8 1.0
O A:HOH345 4.4 32.3 1.0
O A:HOH346 4.5 38.5 1.0
O B:HOH356 4.5 32.5 1.0
N A:PHE53 4.5 21.5 1.0
CA B:VAL113 4.5 18.2 1.0
O A:ASP51 4.6 25.1 1.0
O A:HOH322 4.6 35.4 1.0
CB A:ASP51 4.7 29.5 1.0
CD A:PRO52 4.7 27.0 1.0
CA A:PHE53 4.7 20.9 1.0
CA A:ASP51 4.7 29.0 1.0
CB A:PRO52 4.7 24.1 1.0
O A:HOH308 4.9 24.5 1.0
N A:ALA54 5.0 20.9 1.0
C B:ASP112 5.0 17.6 1.0

Reference:

D.W.Begley, D.Fox, D.Jenner, C.Juli, P.G.Pierce, J.Abendroth, M.Muruthi, K.Safford, V.Anderson, K.Atkins, S.R.Barnes, S.O.Moen, A.C.Raymond, R.Stacy, P.J.Myler, B.L.Staker, N.J.Harmer, I.H.Norville, U.Holzgrabe, M.Sarkar-Tyson, T.E.Edwards, D.D.Lorimer. A Structural Biology Approach Enables the Development of Antimicrobials Targeting Bacterial Immunophilins. Antimicrob.Agents Chemother. V. 58 1458 2014.
ISSN: ISSN 0066-4804
PubMed: 24366729
DOI: 10.1128/AAC.01875-13
Page generated: Sat Jul 13 23:44:48 2024

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