spacer
spacer

SAS results for UniProt accession no. Q3JK38

Sequence annotated by structure

Key:
Sec. struc: By homology
  Helix Strand  
Residue contacts:   to ligand   to metal
Catalytic residues:   (from CSA)
Active sites:   (from PDB SITE records)

Secondary structure shown in red comes from a homologous protein structure which is at least 30% sequence identical to the target protein and has an alignment overlap of at least 80 residues or at least three-quarters of the length of the target sequence (whichever overlap is the larger).

Click on annotated residues to get source(s) of each annotation.

 

FASTA alignment for UniProt accession no. Q3JK38 - coloured by no. of contacts to ligand

Below are the FASTA results from a search of the sequence of UniProt accession no. Q3JK38 against all protein sequences in the PDB. Identical sequences are grouped together and represented by a single 'consensus' sequence (asterisked) onto which all relevant annotations are mapped. The number of sequences represented by each consensus sequence is shown by the '×n' on the right of the alignment. Use the box below to modify the annotations shown on the alignment. At the bottom of the page are given the FASTA stats for all the sequences. There you can exclude any sequences from the alignment.

Struct

FASTA

The search returned 132 unique sequences (including 22 consensus sequences) giving 201 sequence matches in all. The 146 sequences excluded from the alignment are listed at the end.

Modify alignment: Annotate by:
  Number:  
  Show secondary structure: Yes No  


                1         2         3         4         5         6     
       12345678901234567890123456789012345678901234567890123456789012345    Protein name
       ---------+---------+---------+---------+---------+---------+-----    ------------
Q3JK38 -----------------------------------------------------------------    Peptidyl-prolyl cis-trans isomerase OS=Burkholderia  ...
2ke0:A*-----------------------------------------------------------------×3  Solution structure of peptidyl-prolyl cis-trans isomerase  ...
2y78:A -----------------------------------------------------------------    Crystal structure of bpss1823, a mip-like chaperone from  ...
4ggq:D ---------------THINLKVSDGEIFFKIKKTTPLRRLMEAFAKRQSLRFLYDGIRIQADQTP    Crystal structure of a smt fusion peptidyl-prolyl cis-trans  ...
  " :C -ETHINLKVSDGSSEIFFKIKKTTPLRRLMEAFAKRQGKEMDSLRFLYDGIRIQADQTPEDLDME    Crystal structure of a smt fusion peptidyl-prolyl cis-trans  ...
3vaw:A -------ETHINLKVSDGSSEIFFKIKKTTPLRRLMEAFAKRQLRFLYDGIRIQADQTPEDLDME    Crystal structure of a smt fusion peptidyl-prolyl cis-trans  ...
4dz3:A -----------------------------------------------------------------    Crystal structure of a peptidyl-prolyl cis-trans isomerase  ...
3uqa:A --THINLKVSDGSSEIFFKIKKTTPLRRLMEAFAKRQGKEMDSLRFLYDGIRIQADQTPEDLDME    Crystal structure of a smt fusion peptidyl-prolyl cis-trans  ...
4dz2:A -----------------------------------------------------------------    Crystal structure of a peptidyl-prolyl cis-trans isomerase  ...
3uf8:A PETHINLKVSDGSSEIFFKIKKTTPLRRLMEAFAKRQGKEMDSLRFLYDGIRIQADQTPEDLDME    Crystal structure of a smt fusion peptidyl-prolyl cis-trans  ...
4fn2:A --THINLKVSDGSSEIFFKIKKTTPLRRLMEAFAKRQGKEMDSLRFLYDGIRIQADQTPEDLDME    Crystal structure of a smt fusion peptidyl-prolyl cis-trans  ...
4g50:A -ETHINLKVSDGSSEIFFKIKKTTPLRRLMEAFAKRQGKEMDSLRFLYDGIRIQADQTPEDLDME    Crystal structure of a smt fusion peptidyl-prolyl cis-trans  ...
4giv:A PETHINLKVSDGSSEIFFKIKKTTPLRRLMEAFAKRQGKEMDSLRFLYDGIRIQADQTPEDLDME    Crystal structure of a smt fusion peptidyl-prolyl cis-trans  ...
3uqb:A PETHINLKVSDGSSEIFFKIKKTTPLRRLMEAFAKRQGKEMDSLRFLYDGIRIQADQTPEDLDME    Crystal structure of a smt fusion peptidyl-prolyl cis-trans  ...
1fkk:A*-----------------------------------------------------------------×2  Atomic structure of fkbp12, an immunophilin binding protein
4ipx:A -----------------------------------------------------------------    Analyzing the visible conformational substates of the fk506  ...
1tco:C -----------------------------------------------------------------    Ternary complex of a calcineurin a fragment, calcineurin b,  ...
1a7x:A*-----------------------------------------------------------------×33 Fkbp12-fk1012 complex
3mdy:B -----------------------------------------------------------------    Crystal structure of the cytoplasmic domain of the bone  ...
1bkf:A -----------------------------------------------------------------    Fk506 binding protein fkbp mutant r42k/h87v complex with  ...
2ppp:A -----------------------------------------------------------------    Crystal structure of e60q mutant of fkbp12

                                         1         1         1         1
           7         8         9         0         1         2         3
       67890123456789012345678901234567890123456789012345678901234567890    Protein name
       ----+---------+---------+---------+---------+---------+---------+    ------------
Q3JK38 --------------mtvvttesglkyedltegsgae-aragqtvsvhytgwltdgqkfdsskdrn    Peptidyl-prolyl cis-trans isomerase OS=Burkholderia  ...
2ke0:A*----------GPGSMTVVTTESGLKYEDLTEGSGAE-ARAGQTVSVHYTGWLTDGQKFDSSKDRN×3  Solution structure of peptidyl-prolyl cis-trans isomerase  ...
2y78:A -----SGLVPRGSHMTVVTTESGLKYEDLTEGSGAE-ARAGQTVSVHYTGWLTDGQKFDSSKDRN    Crystal structure of bpss1823, a mip-like chaperone from  ...
4ggq:D EDLDMEDNDIIEAHSTVVTTESGLKYEDLTEGSGAE-ARAGQTVSVHYTGWLTDGQKFDSSKDRN    Crystal structure of a smt fusion peptidyl-prolyl cis-trans  ...
  " :C DNDIIEAHREQIGGSTVVTTESGLKYEDLTEGSGAE-ARAGQTVSVHYTGWLTDGQKFDSSKDRN    Crystal structure of a smt fusion peptidyl-prolyl cis-trans  ...
3vaw:A DNDIIEAHREQIGGSTIVTTESGLKYEDLTEGSGAE-ARAGQTVSVHYTGWLTDGQKFDSSKDRN    Crystal structure of a smt fusion peptidyl-prolyl cis-trans  ...
4dz3:A --------------STVVTTESGLKYEDLTEGSGAE-ARAGQTVSVHYTGWLTDGQKFDSSKDRN    Crystal structure of a peptidyl-prolyl cis-trans isomerase  ...
3uqa:A DNDIIEAHREQIGGSTVVTTESGLKYEDLTEGSGAE-ARAGQTVSVHYTGWLTDGQKFDSSKDRN    Crystal structure of a smt fusion peptidyl-prolyl cis-trans  ...
4dz2:A --------------STVVTTESGLKYEDLTEGSGAE-ARAGQTVSVHYTGWLTDGQKFDSSKDRN    Crystal structure of a peptidyl-prolyl cis-trans isomerase  ...
3uf8:A DNDIIEAHREQIGGSTVVTTESGLKYEDLTEGSGAE-ARAGQTVSVHYTGWLTDGQKFDSSKDRN    Crystal structure of a smt fusion peptidyl-prolyl cis-trans  ...
4fn2:A DNDIIEAHREQIGGSTVVTTESGLKYEDLTEGSGAE-ARAGQTVSVHYTGWLTDGQKFGSSKDRN    Crystal structure of a smt fusion peptidyl-prolyl cis-trans  ...
4g50:A DNDIIEAHREQIGGSTVVTTESGLKYEDLTEGSGAE-ARAGQTVSVHYTGWLTDGQKFGSSKDRN    Crystal structure of a smt fusion peptidyl-prolyl cis-trans  ...
4giv:A DNDIIEAHREQIGGSTVVTTESGLKYEDLTEGSGAE-ARAGQTVSVHYTGWLTDGQKFGSSKDRN    Crystal structure of a smt fusion peptidyl-prolyl cis-trans  ...
3uqb:A DNDIIEAHREQIGGSTVVTTESGLKYEDLTEGSGAE-ARAGQTVSVHYTGWLTDGQKFGSSKDRN    Crystal structure of a smt fusion peptidyl-prolyl cis-trans  ...
1fkk:A*----------------------GVQVETISPGDGRTFPKRGQTCVVHYTGMLEDGKKFDSSRDRN×2  Atomic structure of fkbp12, an immunophilin binding protein
4ipx:A ----------------------GVQVETISPGDGRTFPKRGQTVVVHYTGMLEDGKKFDSSRDRN    Analyzing the visible conformational substates of the fk506  ...
1tco:C ----------------------GVQVETISPGDGRTFPKAGQTCVVHYTGMLEDGKKFDSSRDRN    Ternary complex of a calcineurin a fragment, calcineurin b,  ...
1a7x:A*----------------------GVQVETISPGDGRTFPKRGQTCVVHYTGMLEDGKKFDSSRDRN×33 Fkbp12-fk1012 complex
3mdy:B --------------------smgvqvetispgdgrtfpkrgqtcvvhytgmledgkkfdssrdrn    Crystal structure of the cytoplasmic domain of the bone  ...
1bkf:A ----------------------GVQVETISPGDGRTFPKRGQTCVVHYTGMLEDGKKFDSSRDKN    Fk506 binding protein fkbp mutant r42k/h87v complex with  ...
2ppp:A ----------------------gvqvetispgdgrtfpkrgqtcvvhytgmledgkkfdssrdrn    Crystal structure of e60q mutant of fkbp12

                1         1         1         1         1         1    
                4         5         6         7         8         9    
       1234567890123456789012345678901234567890123456789012345678901234     Protein name
       ---------+---------+---------+---------+---------+---------+----     ------------
Q3JK38 dpfafvlgggmvikgwdegvqgmkvggvrrltippqlgygargaggvippnatlvfevelldv-     Peptidyl-prolyl cis-trans isomerase OS=Burkholderia  ...
2ke0:A*DPFAFVLGGGMVIKGWDEGVQGMKVGGVRRLTIPPQLGYGARGAGGVIPPNATLVFEVELLDV- ×3  Solution structure of peptidyl-prolyl cis-trans isomerase  ...
2y78:A DPFAFVLGGGMVIKGWDEGVQGMKVGGVRRLTIPPQLGYGARGAGGVIPPNATLVFEVELLDV-     Crystal structure of bpss1823, a mip-like chaperone from  ...
4ggq:D DPFAFVLGGGMVIKGWDEGVQGMKVGGVRRLTIPPQLGYGARGAGGVIPPNATLVFEVELLDV-     Crystal structure of a smt fusion peptidyl-prolyl cis-trans  ...
  " :C DPFAFVLGGGMVIKGWDEGVQGMKVGGVRRLTIPPQLGYGARGAGGVIPPNATLVFEVELLDV-     Crystal structure of a smt fusion peptidyl-prolyl cis-trans  ...
3vaw:A DPFAFVLGGGMVIKGWDEGVQGMKVGGVRRLTIPPQLGYGARGAGGVIPPNATLVFEVELLDV-     Crystal structure of a smt fusion peptidyl-prolyl cis-trans  ...
4dz3:A DPFAFVLGGGHVIKGWDEGVQGMKVGGVRRLTIPPQLGYGARGAGGVIPPNATLVFEVELLDV-     Crystal structure of a peptidyl-prolyl cis-trans isomerase  ...
3uqa:A DPFEFVLGGGMVIKGWDEGVQGMKVGGVRRLTIPPQLGYGARGAGGVIPPNATLVFEVELLDV-     Crystal structure of a smt fusion peptidyl-prolyl cis-trans  ...
4dz2:A DPFAFVLGGGMVIKGWDEGVQGMKVGGVRRLTIPPQLGYGAGGAGGVIPPNATLVFEVELLDV-     Crystal structure of a peptidyl-prolyl cis-trans isomerase  ...
3uf8:A DPFAFVLGGGMVIKGWDEGVQGMKVGGVRRLTIPPQLGYGARGAAGVIPPNATLVFEVELLDV-     Crystal structure of a smt fusion peptidyl-prolyl cis-trans  ...
4fn2:A DPFAFVLGGGMVIKGWDEGVQGMKVGGVRRLTIPPQLGYGARGAGGVIPPNATLVFEVELLDV-     Crystal structure of a smt fusion peptidyl-prolyl cis-trans  ...
4g50:A DPFAFVLGGGMVIKGWDEGVQGMKVGGVRRLTIPPQLGYGARGAGGVIPPNATLVFEVELLDV-     Crystal structure of a smt fusion peptidyl-prolyl cis-trans  ...
4giv:A DPFAFVLGGGMVIKGWDEGVQGMKVGGVRRLTIPPQLGYGARGAGGVIPPNATLVFEVELLDV-     Crystal structure of a smt fusion peptidyl-prolyl cis-trans  ...
3uqb:A -PFAFVLGGGMVIKGWDEGVQGMKVGGVRRLTIPPQLGYGARGAGGVIPPNATLVFEVELLDV-     Crystal structure of a smt fusion peptidyl-prolyl cis-trans  ...
1fkk:A*KPFKFVLGKQEVIRGWEEGVAQMSVGQRAKLTISPDYAYGATGHPGIIPPNATLIFDVELLKLE ×2  Atomic structure of fkbp12, an immunophilin binding protein
4ipx:A KPFKFMLGKQEVIRGWEEGVAQMSVGQRAKLTISPDYAYGATGVPGIIPPHATLVFDVELLKLE     Analyzing the visible conformational substates of the fk506  ...
1tco:C KPFKFMLGKQEVIRGWEEGVAQMSVGQRAKLTISPDYAYGATGHPGIIPPHATLVFDVELLKLE     Ternary complex of a calcineurin a fragment, calcineurin b,  ...
1a7x:A*KPFKFMLGKQEVIRGWEEGVAQMSVGQRAKLTISPDYAYGATGHPGIIPPHATLVFDVELLKLE ×33 Fkbp12-fk1012 complex
3mdy:B kpfkfmlgkqevirgweegvaqmsvgqrakltispdyaygatghpgiipphatlvfdvellkle     Crystal structure of the cytoplasmic domain of the bone  ...
1bkf:A KPFKFMLGKQEVIRGWEEGVAQMSVGQRAKLTISPDYAYGATGVPGIIPPHATLVFDVELLKLE     Fk506 binding protein fkbp mutant r42k/h87v complex with  ...
2ppp:A kpfkfmlgkqevirgwqegvaqmsvgqrakltispdyaygatghpgiipphatlvfdvellkle     Crystal structure of e60q mutant of fkbp12

Residue colours: black = 0, purple = 1, blue = 2, green = 3, orange = 4, red = 5 or more contacts.

Sequence listing

The listing below shows the FASTA statistics for the PDB entries that matched UniProt accession no. Q3JK38. Ditto marks indicate identical sequences represented by a single representative sequence in the alignment above. The representative is asterisked and the names of all its duplicate sequences are indented to the right.

Structures whose names are given in purple are those that are annotated above. The parameters defining which sequences can transfer their annotations are shown at the bottom of the page where they can be altered and the alignment regenerated.

Use the checkboxes to the left of the PDB codes to exclude any sequences from the alignment (or to add back any sequences in the Excluded list). Then click the SELECT button at the bottom of the page to redisplay the alignment.

Aligned sequences

  Smith-
Waterman
score
%-tage
identity
a.a.
overlap
Seq
len
z-score E-
value
  PDB
code
Protein name
1. - - - 113 - - Q3JK38 Peptidyl-prolyl cis-trans isomerase OS=Burkholderia pseudomallei (strain 1710b) GN=BURPS1710b_A0907 PE=1 SV=1
2. 754 100.0% 113 117 995.2 1.9e-48 2ke0:A * Solution structure of peptidyl-prolyl cis-trans isomerase fr burkholderia pseudomallei
3. " " " " " "  = 2ko7:A *
Solution structure of peptidyl-prolyl cis-trans isomerase fr burkholderia pseudomallei complexed with cycloheximide-n- ethylethanoate
4. " " " " " "  = 2l2s:A *
Solution structure of peptidyl-prolyl cis-trans isomerase fr burkholderia pseudomallei complexed with 1-{[(4-methylpheny thio]acetyl}piperidine
5. 754 100.0% 113 122 994.9 1.9e-48 2y78:A Crystal structure of bpss1823, a mip-like chaperone from burkholderia pseudomallei
6. 747 100.0% 112 177 982.9 9e-48 4ggq:D Crystal structure of a smt fusion peptidyl-prolyl cis-trans from burkholderia pseudomallei complexed with cj40
7. 747 100.0% 112 191 982.4 9.7e-48 4ggq:C Crystal structure of a smt fusion peptidyl-prolyl cis-trans from burkholderia pseudomallei complexed with cj40
8. 746 99.1% 112 185 981.3 1.1e-47 3vaw:A Crystal structure of a smt fusion peptidyl-prolyl cis-trans with surface mutation v3i from burkholderia pseudomallei co with fk506
9. 739 99.1% 112 113 975.9 2.2e-47 4dz3:A Crystal structure of a peptidyl-prolyl cis-trans isomerase w surface mutation m61h from burkholderia pseudomallei comple fk506
10. 741 99.1% 112 190 974.6 2.6e-47 3uqa:A Crystal structure of a smt fusion peptidyl-prolyl cis-trans with surface mutation a54e from burkholderia pseudomallei c with fk506
11. 737 99.1% 112 113 973.3 3.1e-47 4dz2:A Crystal structure of a peptidyl-prolyl cis-trans isomerase w surface mutation r92g from burkholderia pseudomallei comple fk506
12. 739 99.1% 112 192 971.9 3.7e-47 3uf8:A Crystal structure of a smt fusion peptidyl-prolyl cis-trans with a g95a surface mutation from burkholderia pseudomallei with fk506
13. 738 99.1% 112 190 970.6 4.3e-47 4fn2:A Crystal structure of a smt fusion peptidyl-prolyl cis-trans with surface mutation d44g from burkholderia pseudomallei c with cj37
14. 738 99.1% 112 191 970.6 4.4e-47 4g50:A Crystal structure of a smt fusion peptidyl-prolyl cis-trans with surface mutation d44g from burkholderia pseudomallei c with cj168
15. 738 99.1% 112 192 970.6 4.4e-47 4giv:A Crystal structure of a smt fusion peptidyl-prolyl cis-trans with surface mutation d44g from burkholderia pseudomallei c with cj183
16. 718 98.2% 112 191 944.5 1.2e-45 3uqb:A Crystal structure of a smt fusion peptidyl-prolyl cis-trans with surface mutation d44g from burkholderia pseudomallei c with fk506
17. 397 57.7% 104 107 529.9 1.5e-22 1fkk:A * Atomic structure of fkbp12, an immunophilin binding protein
18. " " " " " "  = 1fkl:A *
Atomic structure of fkbp12-rapaymycin, an immunophilin- immunosuppressant complex
19. 396 57.7% 104 107 528.6 1.8e-22 4ipx:A Analyzing the visible conformational substates of the fk506 protein fkbp12
20. 395 57.7% 104 107 527.3 2.2e-22 1tco:C Ternary complex of a calcineurin a fragment, calcineurin b, fkbp12 and the immunosuppressant drug fk506 (tacrolimus)
21. 388 56.7% 104 107 518.1 6.9e-22 1a7x:A * Fkbp12-fk1012 complex
22. " " " " " "  = 1b6c:A *
Crystal structure of the cytoplasmic domain of the type i tgf-beta receptor in complex with fkbp12
23. " " " " " "  = 1d6o:A *
Native fkbp
24. " " " " " "  = 1d7h:A *
Fkbp complexed with dmso
25. " " " " " "  = 1d7i:A *
Fkbp complexed with methyl methylsulfinylmethyl sulfide (dss
26. " " " " " "  = 1d7j:A *
Fkbp complexed with 4-hydroxy-2-butanone
27. " " " " " "  = 1f40:A *
Solution structure of fkbp12 complexed with gpi-1046, a neurotrophic ligand
28. " " " " " "  = 1fap:A *
The structure of the immunophilin-immunosuppressant fkbp12- rapamycin complex interacting with human frap
29. " " " " " "  = 1fkb:A *
Atomic structure of the rapamycin human immunophilin fkbp- 12 complex
30. " " " " " "  = 1fkd:A *
Fk-506 binding protein: three-dimensional structure of thE C with the antagonist l-685,818
31. " " " " " "  = 1fkf:A *
Atomic structure of fkbp-fk506, an immunophilin-immunosuppre complex
32. " " " " " "  = 1fkg:A *
Design, synthesis, and kinetic evaluation of high-affinity fkbp ligands, and the x-ray crystal structures of their complexes with fkbp12
33. " " " " " "  = 1fkh:A *
Design, synthesis, and kinetic evaluation of high-affinity fkbp ligands, and the x-ray crystal structures of their complexes with fkbp12
34. " " " " " "  = 1fki:A *
Design, synthesis, and kinetic evaluation of high-affinity fkbp ligands, and the x-ray crystal structures of their complexes with fkbp12
35. " " " " " "  = 1fkj:A *
Atomic structure of fkbp12-fk506, an immunophilin immunosupp complex
36. " " " " " "  = 1fkr:A *
Solution structure of fkbp, a rotamase enzyme and receptor for fk506 and rapamycin
37. " " " " " "  = 1fks:A *
Solution structure of fkbp, a rotamase enzyme and receptor for fk506 and rapamycin
38. " " " " " "  = 1fkt:A *
Solution structure of fkbp, a rotamase enzyme and receptor for fk506 and rapamycin
39. " " " " " "  = 1j4h:A *
Crystal structure analysis of the fkbp12 complexed with 000107 small molecule
40. " " " " " "  = 1j4i:A *
Crystal structure analysis of the fkbp12 complexed with 000308 small molecule
41. " " " " " "  = 1j4r:A *
Fk506 binding protein complexed with fkb-001
42. " " " " " "  = 1nsg:A *
The structure of the immunophilin-immunosuppressant fkbp12-r complex interacting with human frap
43. " " " " " "  = 1qpf:A *
Fk506 binding protein (12 kda, human) complex with l-709,858
44. " " " " " "  = 1qpl:A *
Fk506 binding protein (12 kda, human) complex with l-707,587
45. " " " " " "  = 2dg3:A *
Wildtype fk506-binding protein complexed with rapamycin
46. " " " " " "  = 2fap:A *
The structure of the immunophilin-immunosuppressant fkbp12-( ethoxy rapamycin complex interacting with huma
47. " " " " " "  = 2fke:A *
Fk-506-binding protein: three-dimensional structure of thE C with the antagonist l-685,818
48. " " " " " "  = 2ppn:A *
Crystal structure of fkbp12
49. " " " " " "  = 2rse:A *
Nmr structure of fkbp12-mtor frb domain-rapamycin complex st determined based on pcs
50. " " " " " "  = 3fap:A *
Atomic structures of the rapamycin analogs in complex with both human fkbp12 and frb domain of frap
51. " " " " " "  = 3h9r:B *
Crystal structure of the kinase domain of type i activin rec (acvr1) in complex with fkbp12 and dorsomorphin
52. " " " " " "  = 4dh0:A *
X-ray crystal structure of 28-o-methylrapamycin complexed wi is the cyclohexyl moiety part of the effector domain of rap
53. " " " " " "  = 4fap:A *
Atomic structures of the rapamycin analogs in complex with both human fkbp12 and frb domain of frap
54. 388 56.7% 104 109 518.0 7.1e-22 3mdy:B Crystal structure of the cytoplasmic domain of the bone morp protein receptor type-1b (bmpr1b) in complex with fkbp12 an 193189
55. 386 55.8% 104 107 515.5 9.7e-22 1bkf:A Fk506 binding protein fkbp mutant r42k/h87v complex with immunosuppressant fk506
56. 386 56.7% 104 107 515.5 9.7e-22 2ppp:A Crystal structure of e60q mutant of fkbp12

Number of sequences: 56

Excluded sequences

  Smith-
Waterman
score
%-tage
identity
a.a.
overlap
Seq
len
z-score E-
value
  PDB
code
Protein name
1. 384 56.7% 104 107 512.9 1.4e-21 2ppo:A Crystal structure of e60a mutant of fkbp12
2. 384 56.7% 104 107 512.9 1.4e-21 4n19:A Structural basis of conformational transitions in the active 80 s loop in the fk506 binding protein fkbp12
3. 380 55.8% 104 107 507.7 2.7e-21 1eym:A Fk506 binding protein mutant, homodimeric complex
4. 379 55.8% 104 107 506.4 3.1e-21 1bl4:A Fkbp mutant f36v complexed with remodeled synthetic ligand
5. 374 55.8% 104 107 499.9 7.2e-21 2dg4:A Fk506-binding protein mutant wf59 complexed with rapamycin
6. 372 53.8% 106 107 497.3 1e-20 4iq2:A * P21 crystal form of fkbp12.6
7. " " " " " "  = 4iqc:A *
P3121 crystal form of fkbp12.6
8. 371 55.8% 104 107 495.9 1.2e-20 2dg9:A Fk506-binding protein mutant wl59 complexed with rapamycin
9. 368 52.8% 108 113 491.6 2.1e-20 1yat:A Improved calcineurin inhibition by yeast fkbp12-drug complexes. Crystallographic and functional analysis
10. 367 56.2% 105 130 489.2 2.8e-20 2lgo:A Solution nmr structure of a fkbp-type peptidyl-prolyl cis-tr isomerase from giardia lamblia, seattle structural genomics for infectious disease target gilaa.00840.A
11. 359 51.9% 106 107 480.3 8.9e-20 1c9h:A Crystal structure of fkbp12.6 in complex with rapamycin
12. 359 53.8% 106 108 480.2 9e-20 2lpv:A * Solution structure of fkbp12 from aedes aegypti
13. " " " " " "  = 3uqi:A *
Crystallographic structure of fkbp12 from aedes aegypti
14. 359 51.9% 106 108 480.2 9e-20 4c02:B Crystal structure of human acvr1 (alk2) in complex with fkbp12.6 and dorsomorphin
15. 358 57.3% 96 100 479.5 9.9e-20 2pbc:A Fk506-binding protein 2
16. 356 58.8% 97 118 475.6 1.6e-19 1rot:A * Structure of fkbp59-i, the n-terminal domain of a 59 kda fk506-binding protein, nmr, minimized average structure
17. " " " " " "  = 1rou:A *
Structure of fkbp59-i, the n-terminal domain of a 59 kda fk506-binding protein, nmr, 22 structures
18. 351 57.7% 97 121 468.9 3.8e-19 4drj:A O-crystal structure of the ppiase domain of fkbp52, rapamyci frb fragment of mtor
19. 348 57.6% 92 102 466.3 5.4e-19 4nnr:A Fkbp13-fk506 complex
20. 351 57.7% 97 235 463.9 7.3e-19 4law:A Crystal structure analysis of fkbp52, crystal form iii
21. 351 57.7% 97 234 463.9 7.3e-19 4lay:A Crystal structure analysis of fkbp52, complex with i63
22. 351 57.7% 97 237 463.8 7.4e-19 1q1c:A Crystal structure of n(1-260) of human fkbp52
23. 351 57.7% 97 237 463.8 7.4e-19 4lax:A Crystal structure analysis of fkbp52, complex with fk506
24. 351 57.7% 97 240 463.7 7.5e-19 4lav:A Crystal structure analysis of fkbp52, crystal form ii
25. 340 49.5% 111 210 450.4 4.1e-18 1q6h:A * Crystal structure of a truncated form of fkpa from escherich
26. " " " " " "  = 1q6i:A *
Crystal structure of a truncated form of fkpa from escherich in complex with immunosuppressant fk506
27. 340 49.5% 111 213 450.2 4.2e-18 1q6u:A Crystal structure of fkpa from escherichia coli
28. 326 54.2% 96 121 436.3 2.5e-17 4dri:A Co-crystal structure of the ppiase domain of fkbp51, rapamyc frb fragment of mtor
29. 326 54.2% 96 124 436.1 2.6e-17 3o5j:A Fk1 domain of fkbp51, crystal form iii
30. 326 54.2% 96 125 436.0 2.6e-17 3o5f:A Fk1 domain of fkbp51, crystal form vii
31. 326 54.2% 96 127 435.9 2.6e-17 3o5k:A Fk1 domain of fkbp51, crystal form viii
32. 326 54.2% 96 127 435.9 2.6e-17 3o5m:A * Fk1 domain mutant a19t of fkbp51, crystal form ii
33. " " " " " "  = 4jfi:A *
Increasing the efficiency efficiency of ligands for the fk50 protein 51 by conformational control: complex of fkbp51 wit 1-[(9s,13r,13ar)-1,3-dimethoxy-8-oxo-5,8,9,10,11,12,13,13a- 6h-9,13-epiminoazocino[2,1-a]isoquinolin-14-yl]-2-(3,4,5- trimethoxyphenyl)ethane-1,2-dione
34. 326 54.2% 96 128 435.8 2.7e-17 3o5e:A Fk1 domain of fkbp51, crystal form vi
35. 326 54.2% 96 128 435.8 2.7e-17 3o5g:A * Fk1 domain of fkbp51, crystal form i
36. " " " " " "  = 3o5i:A *
Fk1 domain of fkbp51, crystal form ii
37. 326 54.2% 96 128 435.8 2.7e-17 3o5l:A * Fk1 domain mutant a19t of fkbp51, crystal form i
38. " " " " " "  = 3o5o:A *
Fk1 domain mutant a19t of fkbp51, crystal form iii
39. " " " " " "  = 3o5p:A *
Fk1 domain mutant a19t of fkbp51, crystal form iv
40. " " " " " "  = 3o5q:A *
Fk1 domain mutant a19t of fkbp51, crystal form iv, in presen
41. " " " " " "  = 3o5r:A *
Complex of fk506 with the fk1 domain mutant a19t of fkbp51
42. " " " " " "  = 4drk:A *
Evaluation of synthetic fk506 analogs as ligands for fkbp51 fkbp52: complex of fkbp51 with {3-[(1r)-3-(3,4-dimethoxyphe ({[(2s)-1-(3,3-dimethyl-2-oxopentanoyl)piperidin-2-yl]carbo propyl]phenoxy}acetic acid
43. " " " " " "  = 4drm:A *
Evaluation of synthetic fk506 analogs as ligands for fkbp51 fkbp52: complex of fkbp51 with {3-[(1r)-3-(3,4-dimethoxyphe ({[(2s)-1-{[(1s,2r)-2-ethyl-1-hydroxycyclohexyl](oxo) acetyl}piperidin-2-yl]carbonyl}oxy)propyl]phenoxy}acetic ac
44. " " " " " "  = 4drn:A *
Evaluation of synthetic fk506 analogs as ligands for fkbp51 fkbp52: complex of fkbp51 with {3-[(1r)-3-(3,4-dimethoxyphe ({[(2s)-1-{[(1s,2r)-2-ethyl-1-hydroxycyclohexyl](oxo) acetyl}piperidin-2-yl]carbonyl}oxy)propyl]phenoxy}acetic ac
45. " " " " " "  = 4dro:A *
Evaluation of synthetic fk506 analogs as ligands for fkbp51 fkbp52: complex of fkbp51 with (1r)-3-(3,4-dimethoxyphenyl) phenylpropyl (2s)-1-{[(1r,2s)-2-ethyl-1-hydroxycyclohexyl]( acetyl}piperidine-2-carboxylate
46. " " " " " "  = 4drp:A *
Evaluation of synthetic fk506 analogs as ligands for the fk5 proteins 51 and 52: complex of fkbp51 with 2-(3-((r)-3-(3,4 dimethoxyphenyl)-1-((s)-1-(2-((1r,2s)-2-ethyl-1-hydroxy-cyc 2-oxoacetyl)piperidine-2-carbonyloxy)propyl)phenoxy)acetic cocrystallization
47. " " " " " "  = 4drq:A *
Exploration of pipecolate sulfonamides as binders of the fk5 proteins 51 and 52: complex of fkbp51 with 2-(3-((r)-1-((s) dichlorophenylsulfonyl)piperidine-2-carbonyloxy)-3-(3,4-dim phenyl)propyl)phenoxy)acetic acid
48. " " " " " "  = 4jfj:A *
Increasing the efficiency efficiency of ligands for the fk50 protein 51 by conformational control: complex of fkbp51 wit (1s,6r)-10-(1,3-benzothiazol-6-ylsulfonyl)-3-[2-(3,4- dimethoxyphenoxy)ethyl]-3,10-diazabicyclo[4.3.1]decan-2-one
49. " " " " " "  = 4jfk:A *
Increasing the efficiency efficiency of ligands for the fk50 protein 51 by conformational control: complex of fkbp51 wit 3-[2-(3,4-dimethoxyphenoxy)ethyl]-10-[(2-oxo-2,3-dihydro-1, benzothiazol-6-yl)sulfonyl]-3,10-diazabicyclo[4.3.1]decan-2
50. " " " " " "  = 4jfl:A *
Increasing the efficiency efficiency of ligands for the fk50 protein 51 by conformational control: complex of fkbp51 wit 5r)-3-[2-(3,4-dimethoxyphenoxy)ethyl]-2-oxo-3,9- diazabicyclo[3.3.1]non-9-yl}sulfonyl)-1,3-benzothiazol-2(3h
51. " " " " " "  = 4jfm:A *
Increasing the efficiency efficiency of ligands for the fk50 protein 51 by conformational control: complex of fkbp51 wit dimethoxyphenoxy)ethyl (2s)-1-[(2-oxo-2,3-dihydro-1,3-benzo yl)sulfonyl]piperidine-2-carboxylate
52. 326 54.2% 96 132 435.6 2.7e-17 4drh:A Co-crystal structure of the ppiase domain of fkbp51, rapamyc frb fragment of mtor at low ph
53. 326 54.2% 96 242 431.0 5e-17 3o5d:A Crystal structure of a fragment of fkbp51 comprising the fk1 domains
54. 312 53.6% 97 118 418.2 2.6e-16 1r9h:A Structural genomics of c.Elegans: fkbp-type peptidylprolyl isomerase
55. 310 54.6% 97 121 415.4 3.7e-16 1n1a:A Crystal structure of the n-terminal domain of human fkbp52
56. 332 46.2% 117 125 403.4 1.7e-15 1u79:A * Crystal structure of atfkbp13
57. " " " " " "  = 1y0o:A *
Crystal structure of reduced atfkbp13
58. 300 44.9% 107 117 402.6 1.9e-15 4bf8:A Fpr4 ppi domain
59. 295 45.9% 111 160 393.7 5.9e-15 1jvw:A Trypanosoma cruzi macrophage infectivity potentiator (tcmip)
60. 280 45.3% 95 121 376.2 5.6e-14 4dip:A Crystal structure of human peptidyl-prolyl cis-trans isomera
61. 279 40.5% 111 137 374.0 7.4e-14 2uz5:A * Solution structure of the fkbp-domain of legionella pneumophila mip
62. " " " " " "  = 2vcd:A *
Solution structure of the fkbp-domain of legionella pneumophila mip in complex with rapamycin
63. 280 45.3% 95 189 372.8 8.6e-14 4msp:A Crystal structure of human peptidyl-prolyl cis-trans isomera (aka fkbp14) containing two ef-hand motifs
64. 279 40.5% 111 204 371.0 1.1e-13 1fd9:A Crystal structure of the macrophage infectivity potentiator (mip) a major virulence factor from legionella pneumophila
65. 273 42.9% 112 121 367.1 1.8e-13 4itz:A Crystal structure of the fk506 binding domain of plasmodium fkbp35 in complex with a tetrapeptide substrate
66. 273 42.9% 112 123 367.0 1.8e-13 3ihz:A Crystal structure of the fk506 binding domain of plasmodium fkbp35 in complex with fk506
67. 273 42.9% 112 122 367.0 1.8e-13 4j4o:A * Crystal structure of fk506 binding domain of plasmodium viva in complex with d44
68. " " " " " "  = 4mgv:A *
Crystal structure of fk506 binding domain of plasmodium viva in complex with inhibitor d5
69. 273 42.9% 112 124 366.9 1.8e-13 3ni6:A * Crystal structure of the fk506 binding domain of plasmodium fkbp35
70. " " " " " "  = 3pa7:A *
Crystal structure of fkbp from plasmodium vivax in complex w tetrapeptide alpf
71. 273 42.9% 112 126 366.8 1.9e-13 2ki3:A Structural and biochemical characterization of fk506 binding domain from plasmodium vivax
72. 252 42.9% 112 123 339.6 6.2e-12 2vn1:A * Crystal structure of the fk506-binding domain of plasmodium falciparum fkbp35 in complex with fk506
73. " " " " " "  = 4j4n:A *
Crystal structure of fk506 binding domain of plasmodium falc fkbp35 in complex with d44
74. 252 42.9% 112 135 338.8 6.7e-12 2ofn:A Solution structure of fk506-binding domain (fkbd)of fkbp35 f plasmodium falciparum
75. 244 42.2% 116 119 329.4 2.3e-11 3kz7:A C-terminal domain of murine fkbp25 rapamycin complex
76. 244 42.9% 105 133 328.5 2.5e-11 3oe2:A 1.6 a crystal structure of peptidyl-prolyl cis-trans isomera from pseudomonas syringae pv. Tomato str. Dc3000 (pspto dc3
77. 242 42.2% 116 116 326.9 3.1e-11 1pbk:A Homologous domain of human fkbp25
78. 213 39.6% 101 236 283.7 8e-09 3jxv:A Crystal structure of the 3 fkbp domains of wheat fkbp73
79. 228 49.4% 87 357 280.5 1.2e-08 1kt0:A Structure of the large fkbp-like protein, fkbp51, involved i receptor complexes
80. 193 46.0% 87 374 242.3 1.6e-06 1kt1:A Structure of the large fkbp-like protein, fkbp51, involved in steroid receptor complexes
81. 170 29.5% 112 117 232.9 5.4e-06 3b7x:A Crystal structure of human fk506-binding protein 6
82. 152 30.7% 101 131 208.5 0.00012 2f4e:A N-terminal domain of fkbp42 from arabidopsis thaliana
83. 152 30.7% 101 258 203.4 0.00024 2if4:A Crystal structure of a multi-domain immunophilin from arabidopsis thaliana
84. 144 32.7% 104 118 198.9 0.00042 2awg:A Structure of the ppiase domain of the human fk506-binding protein 8
85. 144 32.7% 104 118 198.9 0.00042 3ey6:A Crystal structure of the fk506-binding domain of human fkbp3
86. 144 32.7% 104 121 198.7 0.00043 2f2d:A Solution structure of the fk506-binding domain of human fkbp38
87. 140 31.0% 113 114 193.9 0.00079 4jys:B Crystal structure of fkbp25 from plasmodium vivax
88. 140 31.0% 113 132 192.8 0.00092 4jys:A Crystal structure of fkbp25 from plasmodium vivax
89. 135 32.4% 105 135 186.1 0.0022 2d9f:A Solution structure of ruh-047, an fkbp domain from human cdna
90. 135 32.4% 105 157 185.0 0.0025 2jwx:A * Solution structure of the n-terminal domain of human fkbp38 (fkbp38ntd)
91. " " " " " "  = 2mf9:A *
Solution structure of the n-terminal domain of human fkbp38 (fkbp38ntd)
92. 145 33.7% 92 151 170.9 0.015 1ix5:A Solution structure of the methanococcus thermolithotrophicus fkbp
93. 122 28.4% 67 160 167.9 0.023 4dt4:A Crystal structure of the ppiase-chaperone slpa with the chap binding site occupied by the linker of the purification tag
94. 213 39.6% 101 300 165.7 0.03 3jym:A Crystal structure of the 3 fkbp domains of wheat fkbp73
95. 115 33.3% 60 106 161.9 0.049 1l1p:A Solution structure of the ppiase domain from e. Coli trigger factor
96. 117 34.0% 97 449 153.5 0.14 4kc7:A * Crystal structure of endo-1,5-alpha-l-arabinanase from therm petrophila rku-1
97. " " " " " "  = 4kc8:A *
Crystal structure of endo-1,5-alpha-l-arabinanase from therm petrophila rku-1 in complex with tris
98. 131 29.2% 89 150 152.7 0.16 3pr9:A * Structural analysis of protein folding by the methanococcus chaperone fkbp26
99. " " " " " "  = 3pra:A *
Structural analysis of protein folding by the methanococcus chaperone fkbp26
100. 131 29.2% 89 223 149.7 0.23 3prb:A * Structural analysis of protein folding by the methanococcus chaperone fkbp26
101. " " " " " "  = 3prd:A *
Structural analysis of protein folding by the methanococcus chaperone fkbp26
102. 105 28.4% 109 283 141.3 0.68 1p5q:A Crystal structure of fkbp52 c-terminal domain
103. 105 28.4% 109 285 141.3 0.68 1qz2:A Crystal structure of fkbp52 c-terminal domain complex with thE C-terminal peptide meevd of hsp90
104. 106 28.7% 87 376 140.5 0.75 1t11:A Trigger factor
105. 97 25.0% 76 165 135.0 1.5 2lkn:A Solution structure of the ppiase domain of human aryl-hydroc receptor-interacting protein (aip)
106. 87 27.6% 58 85 127.0 4.3 1hxv:A Ppiase domain of the mycoplasma genitalium trigger factor
107. 90 27.1% 48 151 126.5 4.5 2kr7:A Solution structure of helicobacter pylori slyd
108. 93 29.2% 89 443 122.3 7.8 2x8f:A Native structure of endo-1,5-alpha-l-arabinanases from bacil subtilis
109. 93 29.2% 89 443 122.3 7.8 2x8t:A Crystal structure of the abn2 h318a mutant
110. 93 29.2% 89 443 122.3 7.8 4cot:A The importance of the abn2 calcium cluster in the endo-1,5- arabinanase activity from bacillus subtilis
111. 91 28.0% 93 441 119.7 11 3lv4:A Crystal structure of the glycoside hydrolase, family 43 yxia protein from bacillus licheniformis. Northeast structural genomics consortium target bir14.
112. 82 31.7% 60 154 115.9 18 2d36:A The crystal structure of flavin reductase hpac
113. 82 31.7% 60 155 115.9 18 2d37:A The crystal structure of flavin reductase hpac complexed wit
114. 82 31.7% 60 156 115.8 18 2d38:A The crystal structure of flavin reductase hpac complexed wit
115. 82 35.0% 60 195 114.1 22 1ka9:H Imidazole glycerol phosphate synthase
116. 85 33.8% 65 346 113.7 23 1xhc:A Nadh oxidase /nitrite reductase from pyrococcus furiosus pfu 001
117. 82 26.1% 92 267 111.8 30 1r88:A The crystal structure of mycobacterium tuberculosis mpt51 (fbpc1)
118. 78 24.1% 83 145 111.2 32 3luo:A Crystal structure and functional characterization of the the prolyl isomerase and chaperone slyd
119. 78 24.1% 83 151 110.9 34 3cgn:A Crystal structure of thermophilic slyd
120. 81 28.7% 101 216 110.8 34 2g19:A Cellular oxygen sensing: crystal structure of hypoxia- inducible factor prolyl hydroxylase (phd2)
121. 83 28.7% 101 215 110.8 34 2y33:A S-nitrosylated phd2 (gsno soaked) in complex with zn(ii) and
122. 83 28.7% 101 215 110.8 34 2y34:A S-nitrosylated phd2 (no exposed) in complex with fe(ii) and
123. 81 28.7% 101 215 110.8 34 3hqu:A Phd2:fe:un9:partial hif1-alpha substrate complex
124. 81 28.7% 101 216 110.8 34 4bqw:A Hif prolyl hydroxylase 2 (phd2/ egln1) in complex with mn(ii 2-(4-hydroxy-2-oxo-1,2-dihydroquinoline-3-carboxamido)aceti
125. 81 28.7% 101 219 110.7 35 2hbu:A Crystal structure of hif prolyl hydroxylase egln-1 in complex with a biologically active inhibitor
126. 81 28.7% 101 217 110.7 34 4bqx:A Hif prolyl hydroxylase 2 (phd2/ egln1) in complex with mn(ii and n-[(1-chloro-4-hydroxyisoquinolin-3-yl)carbonyl]glycine (iox3/un9)
127. 78 24.1% 83 157 110.6 35 3cgm:A Crystal structure of thermophilic slyd
128. 81 28.7% 101 221 110.6 35 4bqy:A Hif prolyl hydroxylase 2 (phd2/ egln1) in complex with fe(ii and n-[(1-chloro-4-hydroxyisoquinolin-3-yl)carbonyl]alanine
129. 81 28.7% 101 224 110.5 35 2hbt:A Crystal structure of hif prolyl hydroxylase egln-1 in complex with a biologically active inhibitor
130. 81 28.7% 101 225 110.4 36 3hqr:A Phd2:mn:nog:hif1-alpha substrate complex
131. 81 28.7% 101 231 110.2 36 4kbz:A Crystal structure of hypoxia-inducible factor prolyl hydroxy (phd2) with (s)-{2-[2-(5-cyano-3-hydroxy-pyridin-2-yl)-thia acetylamino}-phenyl-acetic acid
132. 85 31.6% 95 586 109.7 39 1vk3:A Crystal structure of phosphoribosylformylglycinamidine synthase ii (tm1246) from thermotoga maritima at 2.15 a resolution
133. 85 31.6% 95 583 109.7 39 3d54:A Stucture of purlqs from thermotoga maritima
134. 73 38.5% 39 78 109.4 41 2ed0:A Solution structure of the sh3 domain of abl interactor 2 (abelson interactor 2)
135. 83 28.1% 89 443 109.2 42 2x8s:A Crystal structure of the abn2 d171a mutant in complex with arabinotriose
136. 83 28.3% 60 450 109.1 42 3njt:A Crystal structure of the r450a mutant of the membrane protei
137. 68 32.1% 28 35 108.9 43 1um3:S * Crystal structure of cytochrome b6f complex from m.Laminosus
138. " " " " " "  = 1vf5:S *
Crystal structure of cytochrome b6f complex from m.Laminosus
139. " " " " " "  = 2d2c:F *
Crystal structure of cytochrome b6f complex with dbmib from laminosus
140. 77 36.0% 50 173 108.5 45 1v3w:A * Structure of ferripyochelin binding protein from pyrococcus ot3
141. " " " " " "  = 1v67:A *
Structure of ferripyochelin binding protein from pyrococcus ot3
142. " " " " " "  = 2fko:A *
Structure of ph1591 from pyrococcus horikoshii ot3
143. 76 27.6% 98 147 108.5 46 3uxq:P * The structure of thermorubin in complex with the 70s ribosom thermus thermophilus. This file contains the 50s subunit of ribosome. The entire crystal structure contains two 70s rib
144. " " " " " "  = 3uxr:P *
The structure of thermorubin in complex with the 70s ribosom thermus thermophilus. This file contains the 50s subunit of ribosome. The entire crystal structure contains two 70s rib
145. 79 26.8% 97 212 108.3 47 3ouh:A Phd2-r127 with jnj41536014
146. 83 28.3% 60 516 108.1 48 2qdz:A Structure of the membrane protein fhac: a member of the omp85/tpsb transporter family

Number of sequences: 146

Select or deselect any sequence by clicking its checkbox.
Selection shortcuts : select all/none invert selection

Then click to effect selection changes.

Annotation parameters

The parameters below were used in determining which structural annotations could be transferred on to the target sequence. You can change the parameters and regenerate the SAS alignments and annotation by pressing the Rerun button.

Min. seq. identity:   Min. seq. overlap   Max. E-value

  spacer

spacer