Receptor
PDB id Resolution Class Description Source Keywords
5WOU 1.55 Å NON-ENZYME: OTHER CRYSTAL STRUCTURE OF DROSOPHILA MELANOGASTER SCRIBBLE PDZ1 D COMPLEX WITH GUK-HOLDER DROSOPHILA MELANOGASTER SCRIBBLE PDZ DOMAIN GUK-HOLDER CELL POLARITY CELL ADHESI
Ref.: DROSOPHILA MELANOGASTERGUK-HOLDER INTERACTS WITH TH SCRIBBLED PDZ1 DOMAIN AND REGULATES EPITHELIAL DEVE WITH SCRIBBLED AND DISCS LARGE. J. BIOL. CHEM. V. 293 4519 2018
Ligand
Ligand Chain:Residue Validity Ligand Warnings Binding Data NGL Viewer Molecular Weight (Da) Formula SMILES
EDO A:102;
A:103;
A:101;
A:105;
A:104;
A:106;
A:107;
 Invalid;
Invalid;
Invalid;
Invalid;
Invalid;
Invalid;
Invalid;
 none;
none;
none;
none;
none;
none;
none;
 submit data
62.068 C2 H6 O2 C(CO)...
LEU PRO SER PHE GLU THR ALA LEU V:98;
 Valid;
 none;
 Kd = 664 nM
875.998 n/a O=C([...
PGE A:108;
 Invalid;
 none;
 submit data
150.173 C6 H14 O4 C(COC...
View in 3D viewer
90% Homology Family
Leader
PDB id Resolution Class Description Source Keywords
5WOU 1.55 Å NON-ENZYME: OTHER CRYSTAL STRUCTURE OF DROSOPHILA MELANOGASTER SCRIBBLE PDZ1 D COMPLEX WITH GUK-HOLDER DROSOPHILA MELANOGASTER SCRIBBLE PDZ DOMAIN GUK-HOLDER CELL POLARITY CELL ADHESI
Ref.: DROSOPHILA MELANOGASTERGUK-HOLDER INTERACTS WITH TH SCRIBBLED PDZ1 DOMAIN AND REGULATES EPITHELIAL DEVE WITH SCRIBBLED AND DISCS LARGE. J. BIOL. CHEM. V. 293 4519 2018
Members (1)
No: PDB id Binding Data Representative ligand Formula Smiles
The Class containing this family consists of a total of 1610 families.
1 5WOU Kd = 664 nM LEU PRO SER PHE GLU THR ALA LEU 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 1331 families.
1 5WOU Kd = 664 nM LEU PRO SER PHE GLU THR ALA LEU n/a n/a
50% Homology Family (15)
No: PDB id Binding Data Representative ligand Formula Smiles
The Class containing this family consists of a total of 181 families.
1 6MS1 Kd = 5970 nM GLY SER TYR LEU VAL THR SER VAL n/a n/a
2 3DIW Kd = 0.19 uM ASN GLN LEU ALA TRP PHE ASP THR ASP LEU n/a n/a
3 2AWX - HIS HIS n/a n/a
4 2AWU - ALA HIS HIS n/a n/a
5 6Q0U - TYR TYR GLU SER GLY TRP LEU n/a n/a
6 1MFL Kd ~ 128 uM GLU PTR LEU GLY LEU ASP VAL PRO VAL n/a n/a
7 6Q0M - TYR TYR GLU SER ASP TRP LEU n/a n/a
8 6Q0N - THR GLY TYR GLU THR TRP VAL n/a n/a
9 1MFG Kd ~ 50 uM GLU TYR LEU GLY LEU ASP VAL PRO VAL n/a n/a
10 5WOU Kd = 664 nM LEU PRO SER PHE GLU THR ALA LEU n/a n/a
11 6MTU Kd = 6083 nM PRO HIS THR ASN GLU THR SEP LEU n/a n/a
12 5VWK - PRO ALA TRP ASP GLU THR ASN LEU n/a n/a
13 5VWI - PRO ALA TRP ASP GLU THR ASN LEU n/a n/a
14 2I0L - ARG ARG ARG GLU THR GLN VAL n/a n/a
15 1N7F - ALA THR VAL ARG THR TYR SER CYS n/a n/a
Polypharmacology
Similar Ligands (2D)
Ligand no: 1; Ligand: LEU PRO SER PHE GLU THR ALA LEU; Similar ligands found: 261
No: Ligand ECFP6 Tc MDL keys Tc
1 LEU PRO SER PHE GLU THR ALA LEU 1 1
2 LEU PRO PHE GLU LYS SER THR VAL MET 0.643357 0.924242
3 LEU PRO PHE GLU ARG ALA THR VAL MET 0.637584 0.819444
4 LEU PRO PHE GLU ARG ALA THR ILE MET 0.629139 0.808219
5 PHE TYR ALA PRO GLU PRO ILE THR SER LEU 0.616438 0.884058
6 GLY ARG PRO ARG THR THR SER PHE ALA GLU 0.612245 0.867647
7 PHE GLU ALA ILE PRO ALA GLU TYR LEU 0.605634 0.820895
8 ILE PRO LEU THR GLU GLU ALA GLU LEU 0.596899 0.888889
9 ALA THR PRO PHE GLN GLU 0.592308 0.901639
10 PHE PRO THR LYS ASP VAL ALA LEU 0.576389 0.967742
11 ARG PRO MET THR PHE LYS GLY ALA LEU 0.566038 0.808219
12 LEU PRO PHE ASP LYS SER THR ILE MET 0.564935 0.910448
13 ASP TYR GLU PRO ILE PRO GLU GLU ALA PHE 0.563758 0.823529
14 LEU PRO PHE ASP LYS THR THR ILE MET 0.56 0.895522
15 SER GLY ILE PHE LEU GLU THR SER 0.555556 0.758065
16 LEU PRO PHE ASP ARG THR THR ILE MET 0.551948 0.821918
17 LEU TYR ALA SER PRO GLN LEU GLU GLY PHE 0.548387 0.893939
18 VAL PRO LEU THR GLU ASP ALA GLU LEU 0.548148 0.934426
19 PHE LEU PRO SER ASP PHE PHE PRO SER VAL 0.542857 0.923077
20 VAL MET ALA PRO ARG THR LEU PHE LEU 0.542484 0.794521
21 ALA PHE ARG ILE PRO LEU THR ARG 0.540541 0.855072
22 ILE THR ASP GLN VAL PRO PHE SER VAL 0.536913 0.983871
23 SER PRO ILE VAL PRO SER PHE ASP MET 0.530201 0.882353
24 ALA PRO ALA TRP LEU PHE GLU ALA 0.526316 0.779412
25 ARG THR PHE SER PRO THR TYR GLY LEU 0.522581 0.847222
26 GLY GLN VAL PRO PHE SER LYS GLU GLU CYS 0.52 0.921875
27 ARG ARG LEU PRO ILE PHE SER ARG LEU 0.516556 0.855072
28 LYS LEU PRO ALA GLN PHE TYR ILE LEU 0.515924 0.823529
29 ASP PHE GLN GLU SER ALA ASP SER PHE LEU 0.514706 0.734375
30 ASP PHE ALA ASN THR PHE LEU PRO 0.514085 0.907692
31 THR THR ALA PRO PHE LEU SER GLY LYS 0.513158 0.968254
32 ARG PRO MET THR TYR LYS GLY ALA LEU 0.506024 0.776316
33 ASP ILE ALA TYR TYR THR SER GLU PRO 0.503497 0.895522
34 LEU PRO PHE GLU LEU ARG GLY HIS LEU VAL 0.503067 0.75
35 LYS THR PHE PRO PRO THR GLU PRO LYS 0.5 0.920635
36 ASP PHE GLU GLU ILE PRO GLY GLU TYS LEU 0.496855 0.686747
37 LEU SER SER PRO VAL THR LYS SER PHE 0.496644 0.951613
38 SER SER ILE GLU PHE ALA ARG LEU 0.496552 0.705882
39 SER ALA GLU PRO VAL PRO LEU GLN LEU 0.496454 0.920635
40 LEU ASP GLU GLU THR GLY GLU PHE LEU 0.49635 0.803279
41 GLY ILE LEU GLU PHE VAL PHE THR LEU 0.49635 0.71875
42 ASP PHE GLU GLU ILE PRO GLU GLU TYS 0.493421 0.662651
43 GLU GLU TYR LEU GLN ALA PHE THR TYR 0.493056 0.666667
44 LYS PRO PHE PTR VAL ASN VAL GLU PHE 0.490683 0.76
45 SER ILE TYR PHE TPO PRO GLU LEU TYR ASP 0.487952 0.824324
46 GLU PRO VAL GLU THR THR ASP TYR 0.486111 0.90625
47 SER GLU ILE GLU PHE ALA ARG LEU 0.486111 0.691176
48 PHE ASN PHE PRO GLN ILE THR 0.482759 0.892308
49 TYR MET PHE PRO ASN ALA PRO TYR LEU 0.480769 0.794521
50 TYR LEU GLU PRO ALA PRO VAL THR ALA 0.47973 0.893939
51 GLY TYR GLU ASN PRO THR TYR LYS PHE PHE 0.478261 0.838235
52 ASP PHE GLU GLU ILE PRO GLY GLU TYR LEU 0.478261 0.838235
53 GLU SER ASP PRO ILE VAL ALA GLN TYR 0.477707 0.938462
54 SER GLU CYS THR THR PRO CYS 0.477612 0.919355
55 ASP ASP LEU ASP VAL PRO SER PHE LEU GLN 0.47651 0.967742
56 SER ALA ASN SER PHE THR LEU ILE GLY GLU 0.47619 0.790323
57 SER LEU PHE ASN THR VAL ALA THR LEU 0.47482 0.725806
58 LYS GLN GLU PRO GLN GLU ILE ASP PHE 0.474359 0.857143
59 ALA PRO SER PTR VAL ASN VAL GLN ASN 0.473684 0.821918
60 LEU PRO PRO VAL VAL ALA LYS GLU ILE 0.469799 0.828125
61 GLU PHE SER PRO 0.468254 0.885246
62 LEU LEU PHE GLY PHE PRO VAL TYR VAL 0.467532 0.848485
63 LEU LEU PHE GLY TYR PRO VAL TYR VAL 0.467532 0.848485
64 ALA ARG THR GLU LEU TYR ARG SER LEU 0.465753 0.690141
65 ILE MET ASP GLN VAL PRO PHE SER VAL 0.465409 0.909091
66 ARG PRO PRO ILE PHE ILE ARG ARG LEU 0.464516 0.771429
67 ASP TYR ASN PRO TYR LEU LEU PHE LEU LYS 0.464052 0.867647
68 DPN PRO DAR DTH NH2 0.463235 0.80597
69 SER SER LEU GLU ASN PHE ALA ALA TYR VAL 0.463087 0.701493
70 THR PRO TYR ASP ILE ASN GLN MET LEU 0.4625 0.842857
71 ALA GLU THR PHE 0.462185 0.672131
72 PHE SER HIS PRO GLN ASN THR 0.461039 0.865672
73 TYR PRO PHE PHE NH2 0.460938 0.742424
74 GLN LEU SER PRO PHE PRO PHE ASP LEU 0.460526 0.907692
75 GLY TYR GLN ASP TYR GLU PRO GLU ALA 0.460432 0.828125
76 PHE SER ALA PTR PRO SER GLU GLU ASP 0.459459 0.767123
77 ACE GLY LYS SER PHE SER LYS PRO ARG 0.459459 0.90625
78 ASN LEU VAL PRO GLN VAL ALA THR VAL 0.458904 0.919355
79 ILE PRO ALA TYR GLY VAL LEU THR ILE 0.458065 0.907692
80 TYR LEU GLU PRO GLY PRO VAL THR ALA 0.458065 0.923077
81 THR PRO PRO SER PRO PHE 0.458015 0.888889
82 PRO ALA PRO PHE ALA SER ALA 0.457746 0.859375
83 LEU ASN PHE PRO ILE SER PRO 0.457746 0.923077
84 LEU PHE GLY TYR PRO VAL TYR VAL 0.456954 0.848485
85 ALA ASN SER ARG PHE PRO THR SER ILE ILE 0.45679 0.869565
86 LEU LEU PHE GLY LYS PRO VAL TYR VAL 0.455696 0.823529
87 ASP ILE ASN TYR TYR ALA SER GLU PRO 0.454545 0.882353
88 ASN LEU VAL PRO SER VAL ALA THR VAL 0.454545 0.951613
89 DHI PRO PHE HIS LEU LEU VAL TYR 0.453988 0.771429
90 ALA PRO GLN PRO ALA PRO GLU ASN ALA TYR 0.453947 0.835821
91 ARG MET PHE PRO ASN ALA PRO TYR LEU 0.452381 0.746835
92 LYS PRO SEP GLN GLU LEU 0.451852 0.797101
93 PRO GLU ALA THR ALA PRO PRO GLU GLU 0.451389 0.875
94 ARG ILE PRO SER TYR ARG TYR ARG TYR 0.450331 0.783784
95 TYR LEU GLU PRO GLY PRO VAL THR VAL 0.448718 0.923077
96 ASP PHE GLU GLU ILE PRO GLY GLU PTR 0.448485 0.746667
97 LYS PRO ILE VAL GLN TYR ASP ASN PHE 0.448485 0.855072
98 ASP ILE ASN TYR TYR THR SER GLU PRO 0.448052 0.882353
99 HIS SER ILE THR TYR LEU LEU PRO VAL 0.447853 0.857143
100 PHE ALA PRO GLY ASN TYR PRO ALA LEU 0.446541 0.855072
101 ALA LEU TRP GLY PHE PHE PRO VAL LEU 0.445122 0.80597
102 ASN GLY TYR GLU ASN PRO THR TYR LYS 0.444444 0.838235
103 PRO SER TYR SEP PRO THR SEP PRO SER 0.443709 0.791667
104 ALA ILE MET PRO ALA ARG PHE TYR PRO LYS 0.443182 0.705128
105 PRO GLN PTR GLU GLU ILE PRO ILE 0.442308 0.753425
106 SER ASN TRP SER HIS PRO GLN PHE GLU LYS 0.44186 0.797101
107 GLU VAL PTR GLU SER PRO 0.441379 0.830986
108 ALA ILE ALA TYR PHE ILE PRO ASP GLN ALA 0.440559 0.776119
109 THR PRO GLN ASP LEU ASN THR MET LEU 0.44 0.850746
110 HIS SER LEU PHE HIS PUK THR PRO 0.439759 0.882353
111 TYR GLN PHE GLY PRO ASP PHE PRO ILE ALA 0.439759 0.838235
112 PRO GLN PTR GLU PTR ILE PRO ALA 0.43949 0.733333
113 ARG PHE PRO LEU THR PHE GLY TRP 0.439306 0.808219
114 SER PHE PHE GLU ASP ASN PHE VAL PRO GLU 0.439189 0.907692
115 ARG GLN PHE GLY PRO ASP PHE PRO THR ILE 0.438596 0.819444
116 ARG PRO GLY ASN PHE LEU GLN SER ARG LEU 0.438596 0.855072
117 SER ILE ILE ASN PHE GLU LYS LEU 0.438356 0.777778
118 GLY ASN TYR SER PHE TYR ALA LEU 0.437956 0.701493
119 ALA VAL ALA PHE TYR ILE PRO ASP GLN ALA 0.4375 0.791045
120 LYS LEU TYR GLN ASN PRO THR THR TYR ILE 0.436364 0.855072
121 GLU ASP GLU ASP PHE GLU ILE LEU SER LEU 0.436242 0.746032
122 SER ILE ILE GLN PHE GLU HIS LEU 0.436242 0.735294
123 ASP ALA ASP GLU TYR LEU 0.43609 0.65625
124 GLU ASP GLU ASP PHE GLU ILE LEU SEP LEU 0.435897 0.652174
125 ACE GLY PHE GLY VAL VAL PRO SER PHE TYR 0.435374 0.888889
126 LEU PRO GLU THR GLY 0.435115 0.934426
127 GLY THR SER SER PRO SER ALA ASP 0.433824 0.918033
128 ALA LEU TRP GLY PHE VAL PRO VAL LEU 0.433735 0.80597
129 THR THR ALA PRO SER LEU SER GLY LYS 0.433333 0.936508
130 ALA LEU MET PRO GLY GLN PHE PHE VAL 0.433121 0.80597
131 GLY SER ASP PRO PHE LYS 0.432624 0.903226
132 SIN ALA LEU PRO PHE NIT 0.432432 0.697368
133 GLN ASN GLY PTR GLU ASN PRO THR TYR 0.432258 0.791667
134 VAL PRO LEU ARG PRO MET THR TYR 0.432099 0.786667
135 ARG LEU TYR GLN ASN PRO THR THR TYR ILE 0.431953 0.786667
136 TRP ASP ILE PRO PHE 0.431818 0.854839
137 ALA GLU THR PHE TYR VAL ASP GLY 0.431655 0.651515
138 ARG PRO GLY ASN PHE LEU GLN SER ARG PRO 0.431138 0.842857
139 ALA MET ALA PRO ARG THR LEU LEU LEU 0.430464 0.767123
140 ILE GLY PRO GLY ARG ALA PHE TYR THR ILE 0.430233 0.794521
141 ARG TYR PRO LEU THR PHE GLY TRP 0.430168 0.786667
142 GLY PHE GLU PRO 0.429688 0.819672
143 PHE ALA PRO GLY ASN TYI PRO ALA LEU 0.429448 0.797297
144 ILE LEU ALA LYS PHE LEU HIS THR LEU 0.428571 0.75
145 ILE ARG ALA ALA PRO PRO PRO LEU PHE 0.427673 0.760563
146 LYS PRO PHE PTR VAL ASN VAL NH2 0.427673 0.746667
147 ILE LEU ALA LYS PHE LEU HIS GLU LEU 0.427632 0.691176
148 SER LEU TYR LEU THR VAL ALA THR LEU 0.427536 0.6875
149 TYR SEP PRO THR SEP PRO SER 0.426573 0.791667
150 ALA LEU TYR ASN THR ALA ALA ALA LEU 0.426471 0.646154
151 GLU GLU TYR LEU LYS ALA TRP THR PHE 0.426035 0.753623
152 TYR LEU GLY GLY PRO ASP PHE PRO THR ILE 0.426035 0.882353
153 ASP ILE ASN TYS TYS THR SER GLU PRO 0.425806 0.722892
154 PRO GLU PRO THR ALA PRO PRO GLU GLU 0.425676 0.875
155 TRP GLU TYR ILE PRO ASN VAL 0.42515 0.802817
156 ARG PHE PRO LEU THR PHE GLY TRP CYS PHE 0.423913 0.810811
157 ACE TYR PRO ILE GLN GLU THR 0.423841 0.833333
158 N7P THR SEP PRO SER TYR SET 0.423841 0.77027
159 ASN LEU VAL PRO MET VAL ALA THR VAL 0.423841 0.863636
160 LYS PRO VAL LEU ARG THR ALA 0.423841 0.823529
161 ARG GLN ALA SEP ILE GLU LEU PRO SER MET 0.423729 0.734177
162 ALA ALA SER LEU TYR GLU LYS LYS ALA ALA 0.423611 0.753846
163 BOC HIS PRO PHE ALA LOV ILE HIS 0.423529 0.72973
164 GLU ALA ASP PRO THR GLY HIS SER TYR 0.423529 0.855072
165 ALA DAL PRO PHE NIT 0.423358 0.644737
166 VAL SER PHE ASN FRD PRO GLN ILE THR ALA 0.423313 0.909091
167 GLU GLU PRO THR VAL ILE LYS LYS TYR 0.423313 0.893939
168 TYR GLN GLU SER THR ASP PHE THR PHE LEU 0.423077 0.666667
169 ILE GLY PRO GLY ARG ALA PHE TYR THR 0.422619 0.767123
170 ACE LEU TYR ALA SER SER ASN PRO ALA PTR 0.42236 0.813333
171 ILE SER PRO ARG THR LEU ASP ALA TRP 0.422222 0.835616
172 ASP LEU PRO PHE 0.422222 0.885246
173 ASN PRO ARG ALA MET GLN ALA LEU LEU 0.422078 0.739726
174 GLU ILE ILE ASN PHE GLU LYS LEU 0.421769 0.703125
175 DPN PRO DAR ILE NH2 0.421429 0.735294
176 VAL ORN LEU DPN PRO VAL ORN LEU DPN PRO 0.42 0.8
177 HIS PRO PHE 0.419847 0.701493
178 1IP CYS PHE SER LYS PRO ARG 0.419753 0.802817
179 ARG VAL SER PRO SER THR SER TYR THR PRO 0.41958 0.890625
180 ASP VAL GLN THR GLY ARG ARG PRO TYR GLU 0.419162 0.830986
181 LYS ARG LYS SER ARG TRP ASP GLU THR PRO 0.418994 0.819444
182 ALA ALA TRP LEU PHE GLU ALA 0.418919 0.636364
183 VAL GLN GLN GLU SER SER PHE VAL MET 0.41844 0.723077
184 SER SER LEU GLU ASN PHE ARG ALA TYR VAL 0.418182 0.671233
185 ACE ILE TYR GLU SER LEU 0.41791 0.692308
186 GLU TYR LEU GLY LEU ASP VAL PRO VAL 0.417722 0.890625
187 MET THR SER ALA ILE GLY ILE LEU PRO VAL 0.417722 0.893939
188 PHE GLN PRO GLN ASN GLY GLN PHE ILE 0.417722 0.833333
189 SER LEU PHE HIS 22G THR PRO 0.417647 0.857143
190 ASN ASP TRP LEU LEU PRO SER TYR 0.417647 0.871429
191 ASP ALA ASP GLU GLU ASP PHE 0.417323 0.629032
192 GLY ASP CYS PHE SER LYS PRO ARG 0.417178 0.811594
193 ACE VAL PHE PHE ALA GLU ASP NH2 0.416667 0.603175
194 ALA ASN SER ARG TRP PRO THR THR ARG LEU 0.416667 0.835616
195 DPN PRO ARG 0.416667 0.716418
196 SER PRO LEU ASP SER LEU TRP TRP ILE 0.416149 0.882353
197 SER ILE ILE GLY PHE GLU LYS LEU 0.416107 0.790323
198 SER THR SEP PRO THR PHE ASN LYS 0.415663 0.828571
199 GLY GLU ARG THR ILE PRO ILE THR ARG GLU 0.415584 0.826087
200 TYR LEU ALA PRO GLY PRO VAL THR ALA 0.415584 0.909091
201 GLU GLU PHE GLY ARG ALA PHE SER PHE 0.414474 0.652174
202 ALA GLN PHE SER ALA SER ALA SER ARG 0.414286 0.686567
203 ACE PRO ALA PRO PHE 0.414062 0.753846
204 PRO THR PRO SER ALA PRO VAL PRO LEU 0.413043 0.90625
205 TYR MET ASP PHE ASP ASP ASP ILE PRO PHE 0.412698 0.806452
206 LEU PRO PRO LEU ASP ILE THR PRO TYR 0.4125 0.878788
207 GLN MET PRO THR GLU ASP GLU TYR 0.4125 0.84058
208 PTR VAL PRO MET LEU 0.412162 0.72
209 GLU THR VAL ARG PHE GLN SER ASP 0.411765 0.701493
210 SER SER PHE TYR PRO SEP ALA GLU GLY 0.411392 0.767123
211 ACE PRO GLN GLN ALA THR ASP ASP 0.411348 0.859375
212 ACE ASP PTR ALA GLU PRO MET ASP ALA NH2 0.411043 0.723684
213 GLY GLY CYS PHE SER LYS PRO LYS MYR 0.410714 0.878788
214 ARG TYR PRO LEU THR LEU GLY TRP CYS PHE 0.410526 0.789474
215 ARG GLY PRO GLY CYS ALA PHE VAL THR ILE 0.410405 0.869565
216 THR GLU ASN LEU TYR PHE GLN SER GLY THR 0.410256 0.746269
217 TYR PRO LYS ARG ILE ALA 0.410256 0.75
218 MET HIS PRO ALA GLN THR SER GLN TRP 0.410112 0.833333
219 MET CYS PRO ARG MET THR ALA VAL MET 0.409938 0.791667
220 ARG ILE ILE PRO ARG HIS LEU GLN LEU 0.409639 0.75
221 LEU GLU PHE GLN GLY 0.409091 0.704918
222 GLN VAL PRO LEU ARG PRO MET THR TYR LYS 0.40884 0.8
223 LYS ALA PRO ARG ALY GLN LEU ALA THR LYS 0.408537 0.814286
224 PRO ALA PRO PHE ALA ALA ALA 0.408451 0.765625
225 PRO PRO THR LEU HIS GLU LEU TYR ASP LEU 0.408284 0.869565
226 ALA ILE PHE GLN SER SER MET THR LYS 0.407895 0.731343
227 TYR PRO ASN VAL ASN ILE HIS ASN PHE 0.407186 0.816901
228 ASN LEU VAL PRO THR VAL ALA THR VAL 0.406897 0.919355
229 PHE LEU PRO HIS ALY TYR ASP VAL LYS LEU 0.40678 0.75
230 ASP PHE GLU GLU ILE 0.40625 0.629032
231 PHE ALA PRO GLY PHE PHE PRO TYR LEU 0.40625 0.823529
232 ALA LEU PRO HIS ALA ILE LEU ARG LEU 0.406061 0.722222
233 LEU GLU LYS ALA ARG GLY SER THR TYR 0.406061 0.71831
234 ALA THR ALA ALA ALA THR GLU ALA TYR 0.406015 0.65625
235 BOC HIS PRO PHE HIS LOV ILE HIS 0.405882 0.72973
236 PRO ALA TRP ASP GLU THR ASN LEU 0.404908 0.80597
237 ALA VAL PRO ILE ALA GLN 0.404412 0.822581
238 THR PRO ASP TYR PHE LEU 0.404412 0.772727
239 ASN LEU VAL PRO VAL VAL ALA THR VAL 0.40411 0.919355
240 SER LEU TYR ASN THR VAL ALA THR LEU 0.40411 0.692308
241 ASN GLN LEU ALA TRP PHE ASP THR ASP LEU 0.403727 0.727273
242 ARG SEP PRO VAL PHE SER 0.403727 0.767123
243 ACE GLY LYS SER PHE SER LYS PRO ARG MYR 0.403509 0.907692
244 SIN ALA ALA PRO PHE NIT 0.402685 0.684211
245 SER LEU PHE ASN THR VAL ALA THR LEU TYR 0.402597 0.656716
246 PRO ALA TRP LEU PHE GLU ALA 0.402516 0.716418
247 SER LEU TYR ASN VAL VAL ALA THR LEU 0.401361 0.692308
248 GLU VAL ASN 1OL ALA GLU PHE 0.401316 0.709677
249 GLY ALA GLU THR PHE TYR VAL ASP GLY ALA 0.401316 0.701493
250 GLN VAL PRO SER ASP PRO TYR ASN TYR 0.401274 0.909091
251 LEU GLN ARG VAL LEU SEP ALA PRO PHE 0.401235 0.77027
252 ASP PHE GLU GLU ILE PRO GLU GLU TYS LEU 0.40113 0.695122
253 GLU LYS PRO SER SER SER 0.4 0.870968
254 PRO ALA ILE LEU TYR ALA LEU LEU SER SER 0.4 0.830769
255 DPN PRO DAR CYS NH2 0.4 0.705882
256 ACE LEU PHE PHE GLK CF0 GLU 0.4 0.6
257 ALA ASN SER ARG TYR PRO THR SER ILE ILE 0.4 0.833333
258 ILE ARG TYR PRO LYS THR PHE GLY TRP 0.4 0.763158
259 TYR PRO TYR ASP VAL PRO ASP TYR ALA 0.4 0.835821
260 GLY ALA PHE THR PHE ASN GLU ASP PHE 0.4 0.630769
261 LYS LEU THR PRO LEU CYS VAL THR LEU 0.4 0.904762
Similar Ligands (3D)
Ligand no: 1; Ligand: LEU PRO SER PHE GLU THR ALA LEU; Similar ligands found: 0
No: Ligand Similarity coefficient
Similar Binding Sites (Proteins are less than 50% similar to leader) APoc FAQ
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