Atomistry » Calcium » PDB 4dtm-4ec5 » 4dz3
Atomistry »
  Calcium »
    PDB 4dtm-4ec5 »
      4dz3 »

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

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy