Receptor
PDB id Resolution Class Description Source Keywords
2PV1 1.3 Å EC: 5.2.1.8 CRYSTALLOGRAPHIC STRUCTURE OF SURA FIRST PEPTIDYL-PROLYL ISOMERASE DOMAIN COMPLEXED WITH PEPTIDE WEYIPNV ESCHERICHIA COLI SURVIVAL PROTEIN A PEPTIDYL-PROLYL CIS-TRANS ISOMERASE DOMAIN PEPTIDE COMPLEX
Ref.: THE PERIPLASMIC BACTERIAL MOLECULAR CHAPERONE SURA ADAPTS ITS STRUCTURE TO BIND PEPTIDES IN DIFFERENT CONFORMATIONS TO ASSERT A SEQUENCE PREFERENCE FOR AROMATIC RESIDUES. J.MOL.BIOL. V. 373 367 2007
Ligand
Ligand Chain:Residue Validity Ligand Warnings Binding Data NGL Viewer Molecular Weight (Da) Formula SMILES
TRP GLU TYR ILE PRO ASN VAL B:1;
Valid;
none;
Kd = 0.073 uM
919.026 n/a O=C([...
View in 3D viewer
90% Homology Family
Leader
PDB id Resolution Class Description Source Keywords
2PV1 1.3 Å EC: 5.2.1.8 CRYSTALLOGRAPHIC STRUCTURE OF SURA FIRST PEPTIDYL-PROLYL ISOMERASE DOMAIN COMPLEXED WITH PEPTIDE WEYIPNV ESCHERICHIA COLI SURVIVAL PROTEIN A PEPTIDYL-PROLYL CIS-TRANS ISOMERASE DOMAIN PEPTIDE COMPLEX
Ref.: THE PERIPLASMIC BACTERIAL MOLECULAR CHAPERONE SURA ADAPTS ITS STRUCTURE TO BIND PEPTIDES IN DIFFERENT CONFORMATIONS TO ASSERT A SEQUENCE PREFERENCE FOR AROMATIC RESIDUES. J.MOL.BIOL. V. 373 367 2007
Members (1)
No: PDB id Binding Data Representative ligand Formula Smiles
The Class containing this family consists of a total of 21 families.
1 2PV1 Kd = 0.073 uM TRP GLU TYR ILE PRO ASN VAL n/a n/a
70% Homology Family (1)
No: PDB id Binding Data Representative ligand Formula Smiles
The Class containing this family consists of a total of 15 families.
1 2PV1 Kd = 0.073 uM TRP GLU TYR ILE PRO ASN VAL n/a n/a
50% Homology Family (1)
No: PDB id Binding Data Representative ligand Formula Smiles
The Class containing this family consists of a total of 10 families.
1 2PV1 Kd = 0.073 uM TRP GLU TYR ILE PRO ASN VAL n/a n/a
Polypharmacology
Similar Ligands
Ligand no: 1; Ligand: TRP GLU TYR ILE PRO ASN VAL; Similar ligands found: 172
No: Ligand ECFP6 Tc MDL keys Tc
1 TRP GLU TYR ILE PRO ASN VAL 1 1
2 LYS GLN TRP ASP ASN TYR GLU PHE ILE TRP 0.575949 0.808824
3 PHE GLU ALA ILE PRO ALA GLU TYR LEU 0.574194 0.895522
4 MET TYR TRP TYR PRO TYR 0.56 0.830986
5 ASN ASP LYS TYR GLU PRO PHE TRP GLU 0.552326 0.897059
6 MET VAL TRP GLY PRO ASP PRO LEU TYR VAL 0.539773 0.863014
7 ASP TYR GLU PRO ILE PRO GLU GLU ALA PHE 0.537037 0.897059
8 LYS VAL PRO ARG ASN GLN ASP TRP LEU 0.534884 0.813333
9 ASP PHE GLU GLU ILE PRO GLY GLU TYR LEU 0.533333 0.911765
10 SER ASN TRP SER HIS PRO GLN PHE GLU LYS 0.532164 0.830986
11 ASP SER LYS ASP VAL LYS GLU TRP TYR VAL ZN 0.531646 0.756757
12 ASN ASP TRP LEU LEU PRO SER TYR 0.526946 0.929577
13 ASP PHE GLU GLU ILE PRO GLU GLU TYS 0.515528 0.740741
14 THR ASN GLU TYR TYR VAL 0.515385 0.686567
15 SER PRO LEU ASP SER LEU TRP TRP ILE 0.509317 0.873239
16 GLU PRO GLN ALA PRO TRP MET GLU GLN 0.509202 0.780822
17 PHE ALA PRO GLY ASN TYR PRO ALA TRP 0.508671 0.914286
18 TYR MET PHE PRO ASN ALA PRO TYR LEU 0.50303 0.876712
19 ALA PRO ALA TRP LEU PHE GLU ALA 0.50303 0.852941
20 LYS PRO ILE VAL GLN TYR ASP ASN PHE 0.502959 0.955882
21 ARG ILE PRO SER TYR ARG TYR ARG TYR 0.5 0.792208
22 PRO GLN PRO VAL ASP SER TRP VAL 0.497041 0.84507
23 ASP TRP GLU ILE VAL 0.496504 0.701493
24 LYS TYR TYR SER ILE ILE PRO HIS SER ILE 0.493827 0.875
25 TYR TYR SER ILE ILE PRO HIS SER ILE 0.493827 0.875
26 ALA VAL PRO TRP 0.492857 0.80597
27 TYR GLU TRP 0.492647 0.686567
28 ARG GLN PHE GLY PRO ASP TRP ILE VAL ALA 0.491979 0.824324
29 ACE GLN PM3 GLU GLU ILE PRO 0.489933 0.72973
30 THR ASN GLU TYR LYS VAL 0.489209 0.716418
31 ILE ARG TYR PRO LYS THR PHE GLY TRP 0.48913 0.866667
32 TRP GLU GLU LEU 0.488722 0.686567
33 THR PRO TYR ASP ILE ASN GLN MET LEU 0.488235 0.849315
34 ASP PHE GLU GLU ILE PRO GLY GLU TYS LEU 0.488235 0.743902
35 VAL SER GLN ASN TYR PRO ILE VAL GLN ASN 0.4875 0.859155
36 ALA ILE ALA TYR PHE ILE PRO ASP GLN ALA 0.4875 0.895522
37 GLY TYR GLN ASP TYR GLU PRO GLU ALA 0.486486 0.820895
38 ARG GLN TRP GLY PRO ASP PRO ALA ALA VAL 0.486188 0.773333
39 ALA ASN SER ARG TRP PRO ALY SER ILE ILE 0.484848 0.819444
40 ASN ARG PRO VAL TYR ILE PRO ARG PRO PRO 0.484472 0.773333
41 PHE TYR ALA PRO GLU PRO ILE THR SER LEU 0.482353 0.875
42 LYS GLN TRP ASP ASN TYR GLU PTR ILE TRP 0.480226 0.76
43 LYS LEU PRO ALA GLN PHE TYR ILE LEU 0.47929 0.925373
44 TYR GLN PHE GLY PRO ASP PHE PRO ILE ALA 0.477012 0.898551
45 LYS LEU TYR GLN ASN PRO THR THR TYR ILE 0.476471 0.927536
46 MET LEU TRP GLY TYR LEU GLN TYR VAL 0.47561 0.763889
47 GLN ASN TYR PRO ILE VAL GLN 0.474359 0.925373
48 GLU TYR LEU GLY LEU ASP VAL PRO VAL 0.472393 0.852941
49 GLU PRO GLN ALA PRO TRP MET GLU 0.470238 0.780822
50 ARG TYR PRO LEU THR PHE GLY TRP 0.469945 0.866667
51 PRO GLN PTR GLU GLU ILE PRO ILE 0.46988 0.773333
52 ASP ARG VAL TYR ILE HIS PRO PHE 0.469613 0.878378
53 SER ILE TYR PHE TPO PRO GLU LEU TYR ASP 0.469274 0.794872
54 ARG MET PHE PRO ASN ALA PRO TYR LEU 0.468571 0.8
55 ACE TYR PRO ILE GLN GLU THR 0.468354 0.84058
56 TYR PRO ASN VAL ASN ILE HIS ASN PHE 0.468208 0.956522
57 LYS PRO PHE PTR VAL ASN VAL GLU PHE 0.468208 0.826667
58 PRO GLN PTR GLU PTR ILE PRO ALA 0.467066 0.8
59 ASP PHE GLU GLU ILE PRO GLU GLU TYS LEU 0.465909 0.743902
60 GLY GLU GLU TRP GLY PRO TRP VAL NH2 0.464968 0.838235
61 ASN GLY TYR GLU ASN PRO THR TYR LYS 0.461538 0.871429
62 LYS GLN GLU PRO GLN GLU ILE ASP PHE 0.461078 0.820895
63 TRP MET ASP PHE ASP ASP ASP ILE PRO PHE 0.460993 0.776119
64 TRP ASP ILE PRO PHE 0.460993 0.776119
65 ARG LEU TYR GLN ASN PRO THR THR TYR ILE 0.460227 0.842105
66 PHE GLN PRO GLN ASN GLY GLN PHE ILE 0.460123 0.867647
67 ALA ASN SER ARG TRP PRO THR THR ARG LEU 0.460123 0.802632
68 ALA PRO GLN PRO ALA PRO GLU ASN ALA TYR 0.460123 0.869565
69 ALA LEU TRP GLY PHE VAL PRO VAL LEU 0.456647 0.852941
70 TRP PRO TRP 0.456522 0.776119
71 ILE MET ASP GLN VAL PRO PHE SER VAL 0.45614 0.76
72 PHE ASN PHE PRO GLN ILE THR 0.455696 0.869565
73 TYR TYR SER ILE ALA PRO HIS SER ILE 0.455621 0.849315
74 GLU GLY PRO ARG ASN GLN ASP TRP LEU 0.455556 0.813333
75 ALA GLN TRP GLY PRO ASP PRO ALA ALA ALA 0.454023 0.826087
76 ASN PHE ASP ASN PRO VAL TYR ARG LYS THR 0.453039 0.828947
77 LYS ARG LYS SER ARG TRP ASP GLU THR PRO 0.453039 0.779221
78 GLU SER ASP PRO ILE VAL ALA GLN TYR 0.452941 0.859155
79 ASP ASP TRP ASN TRP GLU VAL GLU ASP 0.452703 0.735294
80 GLY SER ASP PRO TRP LYS 0.452229 0.788732
81 ALA ASN SER ARG TRP PRO THR SER FAK ILE 0.452128 0.777778
82 TRP ASN TRP PHE ASP ILE THR ASN LYS 0.451807 0.753623
83 SER VAL TYR ASP PHE PHE VAL TRP LEU 0.45 0.732394
84 GLU GLU PRO THR VAL ILE LYS LYS TYR 0.449704 0.897059
85 ILE THR ASP GLN VAL PRO PHE SER VAL 0.449704 0.816901
86 ALA ASN SER ARG TRP PRO THR SER 2KK ILE 0.447917 0.790123
87 ASP PHE GLU GLU ILE PRO GLY GLU PTR 0.446328 0.789474
88 LEU PHE GLY TYR PRO VAL TYR VAL 0.445122 0.867647
89 GLU GLU TYR LEU LYS ALA TRP THR PHE 0.445087 0.838235
90 PHE LEU TRP GLY PRO ARG ALA LEU VAL 0.444444 0.797297
91 PHE SER ASP PRO TRP GLY GLY 0.443114 0.802817
92 GLN MET PRO THR GLU ASP GLU TYR 0.443114 0.821918
93 ALA ASN SER ARG TRP PRO THR SER 2KP ILE 0.441026 0.790123
94 SER PHE PHE GLU ASP ASN PHE VAL PRO GLU 0.440252 0.830986
95 HIS SER ILE THR TYR LEU LEU PRO VAL 0.44 0.875
96 MET ASN TRP ASN ILE 0.439716 0.705882
97 LEU LEU PHE GLY LYS PRO VAL TYR VAL 0.439306 0.882353
98 ALA ASN SER ARG TYR PRO THR SER ILE ILE 0.439306 0.792208
99 GLN VAL PRO SER ASP PRO TYR ASN TYR 0.439024 0.859155
100 VAL TYR ILE HIS PRO PHE 0.43787 0.897059
101 PHE GLN TRP MET GLY TYR GLU LEU TRP 0.4375 0.777778
102 ASP VAL GLN THR GLY ARG ARG PRO TYR GLU 0.4375 0.789474
103 ARG PHE PRO LEU THR PHE GLY TRP 0.437158 0.84
104 GLU VAL ALA PRO PRO GLU TYR HIS ARG LYS 0.436842 0.802632
105 GLY TYR GLU ASN PRO THR TYR LYS PHE PHE 0.436782 0.884058
106 ASN TRP SER HIS PRO GLN PHE GLU LYS 0.436364 0.794118
107 SER SER LEU GLU ASN PHE ALA ALA TYR VAL 0.435583 0.690141
108 LEU LEU PHE GLY PHE PRO VAL TYR VAL 0.435294 0.867647
109 LEU LEU PHE GLY TYR PRO VAL TYR VAL 0.435294 0.867647
110 ALA PRO SER PTR VAL ASN VAL GLN ASN 0.434524 0.759494
111 ALA LEU TRP GLY PHE PHE PRO VAL LEU 0.434286 0.852941
112 TYR LEU LYS GLU PRO VAL HIS GLY VAL 0.432584 0.884058
113 SER SER VAL ILE GLY VAL TRP TYR LEU 0.431953 0.760563
114 ARG TYR PRO LEU THR LEU GLY TRP CYS PHE 0.431472 0.844156
115 PHE LEU PRO SER ASP PHE PHE PRO SER VAL 0.43125 0.830986
116 PRO ARG PRO ILE LEU LEU PRO TRP ARG NH2 0.431034 0.746667
117 ALA TRP ARG HIS PRO GLN PHE GLY GLY 0.430108 0.77027
118 ALA ASN SER ARG TRP PRO THR SER ALY ILE 0.427778 0.772152
119 SER SER TYR ARG ARG PRO VAL GLY ILE 0.425287 0.792208
120 ASN ARG PRO VAL TYR ILE PRO PRO PRO PRO 0.425 0.838235
121 PHE ALA PRO GLY ASN TYR PRO ALA LEU 0.424419 0.914286
122 ARG GLN PHE GLY PRO ASP PHE PRO THR ILE 0.423913 0.802632
123 ARG ILE ILE PRO ARG HIS LEU GLN LEU 0.423729 0.76
124 GLY LEU MET TRP LEU SER TYR PHE VAL 0.423529 0.743243
125 SER ARG TYR TRP ALA ILE ARG THR ARG 0.422857 0.727273
126 PHE SER HIS PRO GLN ASN THR 0.422619 0.819444
127 LEU TYR ALA SER PRO GLN LEU GLU GLY PHE 0.422222 0.871429
128 ARG TYR PRO LEU THR PHE GLY TRP CYS PHE 0.422111 0.831169
129 ASN TYR THR PRO GLY PRO GLY ILE ARG PHE 0.421622 0.828947
130 ACE TRP ARG VAL PRO 0.421384 0.746667
131 TYR LEU GLU PRO GLY PRO VAL THR VAL 0.420118 0.857143
132 ALA SER ASN GLU ASN TRP GLU THR MET 0.419753 0.693333
133 MET HIS PRO ALA GLN THR SER GLN TRP 0.419355 0.815789
134 TYR PRO LYS ARG ILE ALA 0.418182 0.783784
135 TYR LEU GLU PRO ALA PRO VAL THR ALA 0.418182 0.857143
136 DVA DPR GLY DSN DGN DHI DTY DAS DSN 0.418079 0.875
137 ASP ASN ARG LEU GLY LEU VAL TYR TRP PHE 0.417808 0.701493
138 LYS PRO ILE VAL VAL LEU HIS GLY TYR 0.416667 0.898551
139 GLU GLN TYR LYS PHE TYR SER VAL 0.415584 0.728571
140 SER TRP PHE PRO 0.414474 0.8
141 LYS PRO PHE PTR VAL ASN VAL NH2 0.412791 0.813333
142 LEU PRO PHE GLU LYS SER THR VAL MET 0.412429 0.76
143 SER LEU LEU MET TRP ILE THR GLN VAL 0.411765 0.706667
144 THR LYS ASN TYR LYS GLN THR SER VAL 0.411392 0.704225
145 THR ASN GLU PHE TYR PHE 0.411348 0.641791
146 PHE ASN ARG PRO VAL 0.410256 0.743243
147 ARG PHE MET ASP TYR TRP GLU GLY LEU 0.409836 0.717949
148 TYR LEU GLY GLY PRO ASP PHE PRO THR ILE 0.409836 0.9
149 ABA SER LEU TRP ASN GLY PRO HIS LEU 0.409836 0.875
150 ILE SER PRO ARG THR LEU ASP ALA TRP 0.409326 0.818182
151 LEU PRO PHE GLU ARG ALA THR ILE MET 0.408602 0.746835
152 GLY SER HIS LEU GLU VAL GLN GLY TYR TRP 0.408602 0.830986
153 ARG PHE PRO LEU THR PHE GLY TRP CYS PHE 0.408163 0.818182
154 ARG THR TYR SEP GLY PRO MET ASN LYS VAL 0.408163 0.712644
155 SER SER VAL VAL GLY VAL TRP TYR LEU 0.407186 0.746479
156 PRO ALA TRP LEU PHE GLU ALA 0.405882 0.776119
157 ALA ILE MET PRO ALA ARG PHE TYR PRO LYS 0.405263 0.759494
158 ACE ASN TRP GLU THR PHE 0.404908 0.714286
159 ILE PRO ALA TYR GLY VAL LEU THR ILE 0.404624 0.869565
160 DHI PRO PHE HIS LEU LEU VAL TYR 0.404372 0.897059
161 GLU ASN GLN LYS GLU TYR PHE PHE 0.403974 0.716418
162 THR LYS ASN TYR LYS GLN PHE SER VAL 0.403846 0.71831
163 ALA TRP LEU PHE GLU ALA 0.403846 0.686567
164 THR LEU PRO TRP ASP LEU TRP THR THR 0.403509 0.898551
165 ALA VAL ALA PHE TYR ILE PRO ASP GLN ALA 0.402516 0.865672
166 LEU PRO PRO LEU ASP ILE THR PRO TYR 0.402299 0.869565
167 GLU ARG THR ILE PRO ILE THR ARG GLU 0.401235 0.736842
168 GLN ALA SER GLN GLU VAL LYS ASN TRP 0.4 0.760563
169 LEU PRO PHE GLU ARG ALA THR VAL MET 0.4 0.734177
170 PHE ALA PRO GLY PHE PHE PRO TYR LEU 0.4 0.857143
171 MET TRP ARG PRO TRP 0.4 0.692308
172 ASN TYR THR PRO GLY PRO GLY THR ARG PHE 0.4 0.815789
Similar Binding Sites (Proteins are less than 50% similar to leader)
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