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SAS results for UniProt accession no. Q57YG1

Sequence annotated by structure

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

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. Q57YG1 - coloured by no. of contacts to ligand

Below are the FASTA results from a search of the sequence of UniProt accession no. Q57YG1 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 58 unique sequences (including 13 consensus sequences) giving 88 sequence matches in all. The 49 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
       ---------+---------+---------+---------+---------+---------+-----   ------------
Q57YG1 ---------------------------------------------------------------ms   Peptidyl-prolyl cis-trans isomerase/rotamase, putative  ...
2lj4:A ---------------------------------------------------------------ms   Solution structure of the tbpin1
1j6y:A ------------------------------------------------------------hmasr   Solution structure of pin1at from arabidopsis thaliana
1yw5:A maststglppnwtirvsrshnkeyflnqstnesswdppygtdkevlnayiakfknngykplvned   Peptidyl-prolyl isomerase ess1 from candida albicans
3i6c:A*---------------------------------------------------------------EP×6 Structure-based design of novel pin1 inhibitors (ii)
1nmw:A --------------------------------------------------------------GEP   Solution structure of the ppiase domain of human pin1
1zcn:A ---------------------------------LPPGWEKRMSNGRVYYFNHITNASQWERPSEP   Human pin1 ng mutant
2xp4:A*--------------------------------LPPGWEKAMSRSSGRVYYFNHITNASQWERPEP×3 Discovery of cell-active phenyl-imidazole pin1 inhibitors  ...
2iti:A*-------------------------------LPPGWEKAMSRSSGRVYYFNHITNASQWERPSEP×7 Human pin1 bound to l-peptide
2xpa:A*------------------------------LPPGWEKAMSRSSGRVYYFNHITNASQWERPSGEP×2 Discovery of cell-active phenyl-imidazole pin1 inhibitors  ...
3kab:A*-------------------------------LPPGWEKAMSRSSGRVYYFNHITNASQWERPSEP×4 Structure-guided design of alpha-amino acid-derived pin1  ...
3kce:A ------------------------------KLPPGWEKAMSRSSGRVYYFNHITNASQWERPSEP   Structure-guided design of alpha-amino acid-derived pin1  ...
3odk:A -------------------------------LPPGWEKAMSRSSGRVYYFNHITNASQWERPSEP   Discovery of cell-active phenyl-imidazole pin1 inhibitors  ...
3oob:A*------------------------------KLPPGWEKAMSRSSGRVYYFNHITNASQWERPSEP×3 Structural and functional insights of directly targeting  ...
3ntp:A -----------------------------KLPPGWEKAMSRSSGRVYYFNHITNASQWERPSGEP   Human pin1 complexed with reduced amide inhibitor
1pin:A -----------------------KLPPGWEKRMSRSSGRVYYFNHITNASQWERPSGGKNGQGEP   Pin1 peptidyl-prolyl cis-trans isomerase from homo sapiens
2f21:A -----------------------MADEEKLPPGWEKRMSADGRVYYFNHITNASQWERPSGQGEP   Human pin1 fip mutant
2zqu:A -----------------------KLPPGWEKRMSRSSGRVYYFNHITNASQAERPSGGKNGQGEP   Crystal structure of a mutant pin1 peptidyl-prolyl  ...
2zqv:A -----------------------KLPPGWEKRMSRSSGRVYYANHITNASQWERPSGGKNGQGEP   Crystal structure of a mutant pin1 peptidyl-prolyl  ...
2zr4:A -----------------------KLPPGWEKRMSRSSGRVYYFNHITNAAQWERPSGGKNGQGEP   Crystal structure of a mutant pin1 peptidyl-prolyl  ...
2zr6:A -----------------------KLPPGWEKAMSRSSGRVYYFNHITNASQWERPSGGKNGQGEP   Crystal structure of a mutant pin1 peptidyl-prolyl  ...

                                         1         1         1         1
           7         8         9         0         1         2         3
       67890123456789012345678901234567890123456789012345678901234567890   Protein name
       ----+---------+---------+---------+---------+---------+---------+   ------------
Q57YG1 eklraahllvkfsgsrnpvsrrt--gdstadvtyedaikelqkwsqriasgevsfeeaasqrsdc   Peptidyl-prolyl cis-trans isomerase/rotamase, putative  ...
2lj4:A eklraahllvkfsgsrnpvsrrt--gdstadvtyedaikelqkwsqriasgevsfeeaasqrsdc   Solution structure of the tbpin1
1j6y:A dqvkashilikhqgsrrkaswkdpegkiiltttreaaveqlksiredivsgkanfeevatrvsdc   Solution structure of pin1at from arabidopsis thaliana
1yw5:A gqvrvshlliknnqsrkpkswks--pdgisr-trdesiqilkkhlerilsgevklselantesdc   Peptidyl-prolyl isomerase ess1 from candida albicans
3i6c:A*ARVRCSHLLVKHSQSRRPSSWRQ--EQITR--TQEEALELINGYIQKIKSGEEDFESLASQFSDC×6 Structure-based design of novel pin1 inhibitors (ii)
1nmw:A ARVRCSHLLVKHSQSRRPSSWRQ--EKITR--TKEEALELINGYIQKIKSGEEDFESLASQFSDC   Solution structure of the ppiase domain of human pin1
1zcn:A ARVRCSHLLVKHSQSRRPSSWRQ--EKITR--TKEEALELINGYIQKIKSGEEDFESLASQFSDC   Human pin1 ng mutant
2xp4:A*ARVRCSHLLVKHSQSRRPSSWRQ--EKITR--TKEEALELINGYIQKIKSGEEDFESLASQFSDC×3 Discovery of cell-active phenyl-imidazole pin1 inhibitors  ...
2iti:A*ARVRCSHLLVKHSQSRRPSSWRQ--EKITR--TKEEALELINGYIQKIKSGEEDFESLASQFSDC×7 Human pin1 bound to l-peptide
2xpa:A*ARVRCSHLLVKHSQSRRPSSWRQ--EKITR--TKEEALELINGYIQKIKSGEEDFESLASQFSDC×2 Discovery of cell-active phenyl-imidazole pin1 inhibitors  ...
3kab:A*ARVRCSHLLVKHSQSRRPSSWRQ--EKITR--TKEEALELINGYIQKIKSGEEDFESLASQFSDC×4 Structure-guided design of alpha-amino acid-derived pin1  ...
3kce:A ARVRCSHLLVKHSQSRRPSSWRQ--EKITR--TKEEALELINGYIQKIKSGEEDFESLASQFSDC   Structure-guided design of alpha-amino acid-derived pin1  ...
3odk:A ARVRCSHLLVKHSQSRRPSSWRQ--EKITR--TKEEALELINGYIQKIKSGEEDFESLASQFSDC   Discovery of cell-active phenyl-imidazole pin1 inhibitors  ...
3oob:A*ARVRCSHLLVKHSQSRRPSSWRQ--EKITR--TKEEALELINGYIQKIKSGEEDFESLASQFSDC×3 Structural and functional insights of directly targeting  ...
3ntp:A ARVRCSHLLVKHSQSRRPSSWRQ--EKITR--TKEEALELINGYIQKIKSGEEDFESLASQFSDC   Human pin1 complexed with reduced amide inhibitor
1pin:A ARVRCSHLLVKHSQSRRPSSWRQ--EKITR--TKEEALELINGYIQKIKSGEEDFESLASQFSDC   Pin1 peptidyl-prolyl cis-trans isomerase from homo sapiens
2f21:A ARVRCSHLLVKHSQSRRPSSWRQ--EKITR--TKEEALELINGYIQKIKSGEEDFESLASQFSDC   Human pin1 fip mutant
2zqu:A ARVRCSHLLVKHSQSRRPSSWRQ--EKITR--TKEEALELINGYIQKIKSGEEDFESLASQFSDC   Crystal structure of a mutant pin1 peptidyl-prolyl  ...
2zqv:A ARVRCSHLLVKHSQSRRPSSWRQ--EKITR--TKEEALELINGYIQKIKSGEEDFESLASQFSDC   Crystal structure of a mutant pin1 peptidyl-prolyl  ...
2zr4:A ARVRCSHLLVKHSQSRRPSSWRQ--EKITR--TKEEALELINGYIQKIKSGEEDFESLASQFSDC   Crystal structure of a mutant pin1 peptidyl-prolyl  ...
2zr6:A ARVRCSHLLVKHSQSRRPSSWRQ--EKITR--TKEEALELINGYIQKIKSGEEDFESLASQFSDC   Crystal structure of a mutant pin1 peptidyl-prolyl  ...

                1         1         1         1         1
                4         5         6         7         8
       12345678901234567890123456789012345678901234567890                  Protein name
       ---------+---------+---------+---------+---------+                  ------------
Q57YG1 gsyasggdlgffssgemmkpfedavralkigdispivqtdsglhiikrla                  Peptidyl-prolyl cis-trans isomerase/rotamase, putative  ...
2lj4:A gsyasggdlgffssgemmkpfedavralkigdispivqtdsglhiikrla                  Solution structure of the tbpin1
1j6y:A ssakrggdlgsfgrgqmqkpfeeatyalkvgdisdivdtdsgvhiikrta                  Solution structure of pin1at from arabidopsis thaliana
1yw5:A sshdrggdlgffskgqmqppfeeaafnlhvgevsniietnsgvhilqrtg                  Peptidyl-prolyl isomerase ess1 from candida albicans
3i6c:A*SSAKARGDLGAFSRGQMQKPFEDASFALRTGEMSGPVFTDSGIHIILRTE               ×6 Structure-based design of novel pin1 inhibitors (ii)
1nmw:A SSAKARGDLGAFSRGQMQKPFEDASFALRTGEMSGPVFTDSGIHIILRTE                  Solution structure of the ppiase domain of human pin1
1zcn:A SSAKARGDLGAFSRGQMQKPFEDASFALRTGEMSGPVFTDSGIHIILRTE                  Human pin1 ng mutant
2xp4:A*SSAKARGDLGAFSRGQMQKPFEDASFALRTGEMSGPVFTDSGIHIILRTE               ×3 Discovery of cell-active phenyl-imidazole pin1 inhibitors  ...
2iti:A*SSAKARGDLGAFSRGQMQKPFEDASFALRTGEMSGPVFTDSGIHIILRTE               ×7 Human pin1 bound to l-peptide
2xpa:A*SSAKARGDLGAFSRGQMQKPFEDASFALRTGEMSGPVFTDSGIHIILRTE               ×2 Discovery of cell-active phenyl-imidazole pin1 inhibitors  ...
3kab:A*SSAKARGDLGAFSRGQMQKPFEDASFALRTGEMSGPVFTDSGIHIILRTE               ×4 Structure-guided design of alpha-amino acid-derived pin1  ...
3kce:A SSAKARGDLGAFSRGQMQKPFEDASFALRTGEMSGPVFTDSGIHIILRTE                  Structure-guided design of alpha-amino acid-derived pin1  ...
3odk:A SSAKARGDLGAFSRGQMQKPFEDASFALRTGEMSGPVFTDSGIHIILRTE                  Discovery of cell-active phenyl-imidazole pin1 inhibitors  ...
3oob:A*SSAKARGDLGAFSRGQMQKPFEDASFALRTGEMSGPVFTDSGIHIILRTE               ×3 Structural and functional insights of directly targeting  ...
3ntp:A SSAKARGDLGAFSRGQMQKPFEDASFALRTGEMSGPVFTDSGIHIILRTE                  Human pin1 complexed with reduced amide inhibitor
1pin:A SSAKARGDLGAFSRGQMQKPFEDASFALRTGEMSGPVFTDSGIHIILRTE                  Pin1 peptidyl-prolyl cis-trans isomerase from homo sapiens
2f21:A SSAKARGDLGAFSRGQMQKPFEDASFALRTGEMSGPVFTDSGIHIILRTE                  Human pin1 fip mutant
2zqu:A SSAKARGDLGAFSRGQMQKPFEDASFALRTGEMSGPVFTDSGIHIILRTE                  Crystal structure of a mutant pin1 peptidyl-prolyl  ...
2zqv:A SSAKARGDLGAFSRGQMQKPFEDASFALRTGEMSGPVFTDSGIHIILRTE                  Crystal structure of a mutant pin1 peptidyl-prolyl  ...
2zr4:A SSAKARGDLGAFSRGQMQKPFEDASFALRTGEMSGPVFTDSGIHIILRTE                  Crystal structure of a mutant pin1 peptidyl-prolyl  ...
2zr6:A SSAKARGDLGAFSRGQMQKPFEDASFALRTGEMSGPVFTDSGIHIILRTE                  Crystal structure of a mutant pin1 peptidyl-prolyl  ...

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. Q57YG1. 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. - - - 115 - - Q57YG1 Peptidyl-prolyl cis-trans isomerase/rotamase, putative OS=Trypanosoma brucei brucei (strain 927/4 GUTat10.1) GN=Tb927.8.690 PE=1 SV=1
2. 740 100.0% 115 115 962.9 1.2e-46 2lj4:A Solution structure of the tbpin1
3. 356 48.7% 115 120 468.7 3.9e-19 1j6y:A Solution structure of pin1at from arabidopsis thaliana
4. 333 45.5% 110 177 436.7 2.4e-17 1yw5:A Peptidyl-prolyl isomerase ess1 from candida albicans
5. 321 51.8% 110 113 424.1 1.2e-16 3i6c:A * Structure-based design of novel pin1 inhibitors (ii)
6. " " " " " "  = 3ik8:A *
Structure-based design of novel pin1 inhibitors (i)
7. " " " " " "  = 3ikd:A *
Structure-based design of novel pin1 inhibitors (i)
8. " " " " " "  = 3ikg:A *
Structure-based design of novel pin1 inhibitors (i)
9. " " " " " "  = 3jyj:A *
Structure-based design of novel pin1 inhibitors (ii)
10. " " " " " "  = 3kac:A *
Structure-guided design of alpha-amino acid-derived pin1 inhibitors
11. 319 51.8% 110 114 421.4 1.7e-16 1nmw:A Solution structure of the ppiase domain of human pin1
12. 319 51.8% 110 143 420.0 2e-16 1zcn:A Human pin1 ng mutant
13. 319 51.8% 110 144 420.0 2e-16 2xp4:A * Discovery of cell-active phenyl-imidazole pin1 inhibitors by structure-guided fragment evolution
14. " " " " " "  = 2xp9:A *
Discovery of cell-active phenyl-imidazole pin1 inhibitors by structure-guided fragment evolution
15. " " " " " "  = 3tc5:A *
Selective targeting of disease-relevant protein binding doma phosphorylated natural product derivatives
16. 319 51.8% 110 145 419.9 2.1e-16 2iti:A * Human pin1 bound to l-peptide
17. " " " " " "  = 2itk:A *
Human pin1 bound to d-peptide
18. " " " " " "  = 2q5a:A *
Human pin1 bound to l-peptide
19. " " " " " "  = 2xp3:A *
Discovery of cell-active phenyl-imidazole pin1 inhibitors by structure-guided fragment evolution
20. " " " " " "  = 2xp5:A *
Discovery of cell-active phenyl-imidazole pin1 inhibitors by structure-guided fragment evolution
21. " " " " " "  = 2xp7:A *
Discovery of cell-active phenyl-imidazole pin1 inhibitors by structure-guided fragment evolution
22. " " " " " "  = 2xp8:A *
Discovery of cell-active phenyl-imidazole pin1 inhibitors by structure-guided fragment evolution
23. 319 51.8% 110 146 419.9 2.1e-16 2xpa:A * Discovery of cell-active phenyl-imidazole pin1 inhibitors by structure-guided fragment evolution
24. " " " " " "  = 2xpb:A *
Discovery of cell-active phenyl-imidazole pin1 inhibitors by structure-guided fragment evolution
25. 319 51.8% 110 145 419.9 2.1e-16 3kab:A * Structure-guided design of alpha-amino acid-derived pin1 inhibitors
26. " " " " " "  = 3kag:A *
Structure-guided design of alpha-amino acid-derived pin1 inhibitors
27. " " " " " "  = 3kah:A *
Structure-guided design of alpha-amino acid-derived pin1 inhibitors
28. " " " " " "  = 3kai:A *
Structure-guided design of alpha-amino acid-derived pin1 inhibitors
29. 319 51.8% 110 146 419.9 2.1e-16 3kce:A Structure-guided design of alpha-amino acid-derived pin1 inhibitors
30. 319 51.8% 110 145 419.9 2.1e-16 3odk:A Discovery of cell-active phenyl-imidazole pin1 inhibitors by structure-guided fragment evolution
31. 319 51.8% 110 146 419.9 2.1e-16 3oob:A * Structural and functional insights of directly targeting pin epigallocatechin-3-gallate
32. " " " " " "  = 3tcz:A *
Human pin1 bound to cis peptidomimetic inhibitor
33. " " " " " "  = 3tdb:A *
Human pin1 bound to trans peptidomimetic inhibitor
34. 319 51.8% 110 147 419.8 2.1e-16 3ntp:A Human pin1 complexed with reduced amide inhibitor
35. 319 51.8% 110 153 419.6 2.1e-16 1pin:A Pin1 peptidyl-prolyl cis-trans isomerase from homo sapiens
36. 319 51.8% 110 153 419.6 2.1e-16 2f21:A Human pin1 fip mutant
37. 319 51.8% 110 153 419.6 2.1e-16 2zqu:A Crystal structure of a mutant pin1 peptidyl-prolyl cis-trans isomerase
38. 319 51.8% 110 153 419.6 2.1e-16 2zqv:A Crystal structure of a mutant pin1 peptidyl-prolyl cis-trans isomerase
39. 319 51.8% 110 153 419.6 2.1e-16 2zr4:A Crystal structure of a mutant pin1 peptidyl-prolyl cis-trans isomerase
40. 319 51.8% 110 153 419.6 2.1e-16 2zr6:A Crystal structure of a mutant pin1 peptidyl-prolyl cis-trans isomerase

Number of sequences: 40

Excluded sequences

  Smith-
Waterman
score
%-tage
identity
a.a.
overlap
Seq
len
z-score E-
value
  PDB
code
Protein name
1. 319 51.8% 110 155 419.5 2.2e-16 1f8a:B Structural basis for the phosphoserine-proline recognition b ww domains
2. 319 51.8% 110 163 419.2 2.3e-16 1nmv:A Solution structure of human pin1
3. 318 51.8% 110 145 418.6 2.4e-16 2xp6:A * Discovery of cell-active phenyl-imidazole pin1 inhibitors by structure-guided fragment evolution
4. " " " " " "  = 3kad:A *
Structure-guided design of alpha-amino acid-derived pin1 inhibitors
5. " " " " " "  = 3kaf:A *
Structure-guided design of alpha-amino acid-derived pin1 inhibitors
6. 312 50.9% 110 153 410.6 6.8e-16 2zr5:A Crystal structure of a mutant pin1 peptidyl-prolyl cis-trans isomerase
7. 311 50.9% 110 153 409.3 8e-16 2zqt:A Crystal structure of a mutant pin1 peptidyl-prolyl cis-trans isomerase
8. 305 50.9% 110 153 401.6 2.2e-15 2zqs:A Crystal structure of a mutant pin1 peptidyl-prolyl cis-trans isomerase
9. 192 44.3% 70 97 259.1 1.9e-07 2m1i:A * High resolution structure and dynamics of cspina parvulin at physiological temperature
10. " " " " " "  = 2rqs:A *
3d structure of pin from the psychrophilic archeon cenarchea symbiosum (cspin)
11. 172 32.1% 112 111 232.5 5.6e-06 2jzv:A Solution structure of s. Aureus prsa-ppiase
12. 160 38.2% 76 91 218.4 3.5e-05 1zk6:A Nmr solution structure of b. Subtilis prsa ppiase
13. 164 40.5% 79 252 217.0 4.1e-05 3rfw:A The virulence factor peb4 and the periplasmic protein cj1289 structurally-related sura-like chaperones in the human path campylobacter jejuni
14. 143 37.7% 77 108 195.4 0.00066 4g2p:A Crystal structure of peptidyl-prolyl cis-trans isomerase dom molecular chaperone sura from salmonella enterica subsp. En serovar typhimurium str. 14028s
15. 145 36.5% 85 388 189.9 0.0013 1m5y:A Crystallographic structure of sura, a molecular chaperone that facilitates outer membrane porin folding
16. 133 36.1% 72 96 183.3 0.0031 1eq3:A Nmr structure of human parvulin hpar14
17. 133 36.1% 72 101 183.0 0.0032 3ui4:A * 0.8 a resolution crystal structure of human parvulin 14
18. " " " " " "  = 3ui5:A *
Crystal structure of human parvulin 14
19. " " " " " "  = 3ui6:A *
0.89 a resolution crystal structure of human parvulin 14 in with oxidized dtt
20. 133 36.1% 72 104 182.8 0.0033 1fjd:A Human parvulin-like peptidyl prolyl cis/trans isomerase, hpar14
21. 128 34.8% 69 92 177.1 0.0069 1jns:A * Nmr structure of the e. Coli peptidyl-prolyl cis/trans- isomerase parvulin 10
22. " " " " " "  = 1jnt:A *
Nmr structure of the e. Coli peptidyl-prolyl cis/trans- isomerase parvulin 10
23. 91 22.9% 109 103 123.7 6.5 2pv1:A * Crystallographic structure of sura first peptidyl-prolyl isomerase domain complexed with peptide weyipnv
24. " " " " " "  = 2pv2:A *
Crystallographic structure of sura first peptidyl-prolyl isomerase domain complexed with peptide nftlkfwdifrk
25. 87 29.4% 85 105 123.6 6.6 1x5u:A Solution structure of rrm domain in splicing factor 3b
26. 96 24.3% 111 284 117.2 15 2pv3:A Crystallographic structure of sura fragment lacking the seco peptidyl-prolyl isomerase domain complexed with peptide nft
27. 81 31.7% 60 108 115.7 18 3gpk:A Crystal structure of ppic-type peptidyl-prolyl cis-trans iso domain at 1.55a resolution.
28. 83 25.7% 101 170 115.4 19 2ckf:B Crystal structure of the terminal component of the pah- hydroxylating dioxygenase from sphingomonas sp chy-1
29. 87 24.7% 77 398 115.1 20 2hp1:B Inter-subunit signaling in gsam
30. 87 24.7% 77 402 115.0 20 2hoy:A Inter-subunit signaling in gsam
31. 87 24.7% 77 402 115.0 20 3usf:B Crystal structure of dava-4
32. 87 24.7% 77 427 114.7 21 2gsa:A Crystal structure of glutamate-1-semialdehyde aminomutase (aminotransferase, wild-type form)
33. 87 24.7% 77 427 114.7 21 2hoz:A * Inter-subunit signaling in gsam
34. " " " " " "  = 2hp1:A *
Inter-subunit signaling in gsam
35. " " " " " "  = 2hp2:A *
Inter-subunit signaling in gsam
36. " " " " " "  = 3fq7:A *
Gabaculine complex of gsam
37. 87 24.7% 77 427 114.7 21 3fq8:A M248i mutant of gsam
38. 87 24.7% 77 426 114.7 21 3fqa:A Gabaculien complex of gabaculine resistant gsam version
39. 87 24.7% 77 427 114.7 21 3gsa:A * Crystal structure of glutamate-1-semialdehyde aminomutase in complex with gabaculine
40. " " " " " "  = 3gsb:A *
Crystal structure of glutamate-1-semialdehyde aminomutase in complex with gabaculine
41. 87 24.7% 77 427 114.7 21 3usf:A Crystal structure of dava-4
42. 87 24.7% 77 427 114.7 21 4gsa:A Crystal structure of glutamate-1-semialdehyde aminomutase (aminotransferase) reduced with cyanoborohydrate
43. 85 45.7% 46 292 114.5 21 1up0:A Structure of the endoglucanase cel6 from mycobacterium tuberculosis in complex with cellobiose at 1.75 angstrom
44. 85 45.7% 46 291 114.5 21 1up2:A Structure of the endoglucanase cel6 from mycobacterium tuberculosis in complex with glucose-isofagomine at 1.9 angstrom
45. 85 45.7% 46 293 114.5 21 1up3:A Structure of the endoglucanase cel6 from mycobacterium tuberculosis in complex with methyl-cellobiosyl-4-deoxy-4-thio-beta-d-cellobioside at 1.6 angstrom
46. 85 45.7% 46 300 114.3 22 1uoz:A Structure of the endoglucanase cel6 from mycobacterium tuberculosis in complex with thiocellopentaose at 1.1 angstrom
47. 87 23.5% 85 556 113.0 26 1t10:A Phosphoglucose isomerase from leishmania mexicana in complex substrate d-fructose-6-phosphate
48. 87 23.5% 85 561 112.9 26 1q50:A Phosphoglucose isomerase from leishmania mexicana.
49. 77 24.2% 91 102 110.9 34 2kgj:A Solution structure of parvulin domain of ppid from e.Coli

Number of sequences: 49

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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

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