Receptor
PDB id Resolution Class Description Source Keywords
5ZYS 1.78 Å EC: 2.-.-.- STRUCTURE OF NEPHRIN/MAGI1 COMPLEX MUS MUSCULUS SLIT DIAPHRAGM NEPHROTIC SYNDROME MAGI1- NEPHRIN COMPLEX ADHESION
Ref.: STRUCTURAL BASIS OF HIGHLY SPECIFIC INTERACTION BET NEPHRIN AND MAGI1 IN SLIT DIAPHRAGM ASSEMBLY AND SI J. AM. SOC. NEPHROL. V. 29 2362 2018
Ligand
Ligand Chain:Residue Validity Ligand Warnings Binding Data NGL Viewer Molecular Weight (Da) Formula SMILES
LEU PRO PHE GLU LEU ARG GLY HIS LEU VAL B:1247;
 Valid;
 none;
 Kd = 0.54 uM
1180.42 n/a O=C([...
View in 3D viewer
90% Homology Family
Leader
PDB id Resolution Class Description Source Keywords
5ZYS 1.78 Å EC: 2.-.-.- STRUCTURE OF NEPHRIN/MAGI1 COMPLEX MUS MUSCULUS SLIT DIAPHRAGM NEPHROTIC SYNDROME MAGI1- NEPHRIN COMPLEX ADHESION
Ref.: STRUCTURAL BASIS OF HIGHLY SPECIFIC INTERACTION BET NEPHRIN AND MAGI1 IN SLIT DIAPHRAGM ASSEMBLY AND SI J. AM. SOC. NEPHROL. V. 29 2362 2018
Members (1)
No: PDB id Binding Data Representative ligand Formula Smiles
The Class containing this family consists of a total of 313 families.
1 5ZYS Kd = 0.54 uM LEU PRO PHE GLU LEU ARG GLY HIS LEU 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 277 families.
1 5ZYS Kd = 0.54 uM LEU PRO PHE GLU LEU ARG GLY HIS LEU 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 212 families.
1 5ZYS Kd = 0.54 uM LEU PRO PHE GLU LEU ARG GLY HIS LEU VAL n/a n/a
Polypharmacology
Similar Ligands (2D)
Ligand no: 1; Ligand: LEU PRO PHE GLU LEU ARG GLY HIS LEU VAL; Similar ligands found: 220
No: Ligand ECFP6 Tc MDL keys Tc
1 LEU PRO PHE GLU LEU ARG GLY HIS LEU VAL 1 1
2 PHE PRO ARG PRO TRP LEU HIS GLY LEU 0.609195 0.955882
3 LEU PRO PHE GLU ARG ALA THR VAL MET 0.60119 0.824324
4 ARG ILE ILE PRO ARG HIS LEU GLN LEU 0.588957 0.940298
5 LEU PRO PHE GLU ARG ALA THR ILE MET 0.575581 0.813333
6 ILE LEU LYS GLU PRO VAL HIS GLY VAL 0.560241 0.878788
7 TYR LEU LYS GLU PRO VAL HIS GLY VAL 0.552326 0.869565
8 ILE LEU GLY LYS PHE LEU HIS ARG LEU 0.546584 0.893939
9 ALA TRP ARG HIS PRO GLN PHE GLY GLY 0.544444 0.925373
10 ALA LEU PRO HIS ALA ILE LEU ARG LEU 0.538922 0.939394
11 ARG ARG LEU LEU ARG GLY HIS ASN GLN TYR 0.524096 0.805556
12 LEU TYR ALA SER PRO GLN LEU GLU GLY PHE 0.522988 0.767123
13 LEU LEU PHE GLY LYS PRO VAL TYR VAL 0.517857 0.777778
14 LEU TYR LEU VAL CYS GLY GLU ARG GLY PHE 0.517857 0.708333
15 LEU PRO PHE ASP ARG THR THR ILE MET 0.517241 0.802632
16 ARG PRO GLY ASN PHE LEU GLN SER ARG LEU 0.513967 0.859155
17 ARG PHE PRO LEU THR PHE GLY TRP 0.513812 0.888889
18 LEU LEU PHE GLY TYR PRO VAL TYR VAL 0.512048 0.8
19 LEU LEU PHE GLY PHE PRO VAL TYR VAL 0.512048 0.8
20 SER HIS PRO ARG PRO ILE ARG VAL 0.512048 0.861111
21 LEU TYR LEU VAL CYS GLY GLU ARG VAL 0.509091 0.704225
22 PHE LEU TRP GLY PRO ARG ALA LEU VAL 0.508287 0.955224
23 ALA PHE ARG ILE PRO LEU THR ARG 0.505952 0.833333
24 ALA VAL TYR ASP GLY ARG GLU HIS THR VAL 0.505814 0.780822
25 LEU PRO SER PHE GLU THR ALA LEU 0.503067 0.75
26 GLY VAL TYR ASP GLY ARG GLU HIS THR VAL 0.50289 0.780822
27 LYS PRO ILE VAL VAL LEU HIS GLY TYR 0.502825 0.857143
28 ARG TYR PRO LEU THR PHE GLY TRP 0.502674 0.864865
29 ARG THR PHE SER PRO THR TYR GLY LEU 0.5 0.826667
30 ARG PRO GLY ASN PHE LEU GLN SER ARG PRO 0.5 0.847222
31 ARG PRO MET THR PHE LYS GLY ALA LEU 0.497268 0.813333
32 ASP VAL GLN THR GLY ARG ARG PRO TYR GLU 0.497143 0.835616
33 ALA LEU MET PRO GLY GLN PHE PHE VAL 0.497006 0.785714
34 ARG PHE PRO LEU THR PHE GLY TRP CYS PHE 0.494792 0.864865
35 LEU PRO PHE GLU LYS SER THR VAL MET 0.494253 0.723684
36 ILE GLY PRO GLY ARG ALA PHE TYR VAL 0.491525 0.873239
37 ASP ALA GLU PHE ARG HIS ASP SER 0.490683 0.818182
38 DHI PRO PHE HIS LEU LEU VAL TYR 0.488636 0.828571
39 ARG ARG LEU PRO ILE PHE SER ARG LEU 0.48538 0.833333
40 LEU PHE GLY TYR PRO VAL TYR VAL 0.484848 0.8
41 PHE ASN ARG PRO VAL 0.484076 0.895522
42 ARG LEU TYR HIS SEP LEU PRO ALA 0.483333 0.797468
43 VAL MET ALA PRO ARG THR LEU PHE LEU 0.482955 0.8
44 THR THR ALA PRO PHE LEU SER GLY LYS 0.482558 0.753425
45 LEU PRO PRO GLU GLU ARG LEU ILE 0.48125 0.909091
46 GLY ARG PRO ARG THR THR SER PHE ALA GLU 0.480226 0.819444
47 ARG TYR PRO LEU THR LEU GLY TRP CYS PHE 0.479798 0.842105
48 PHE SER HIS PRO GLN ASN THR 0.47929 0.791667
49 LEU TYR LEU VAL CYS GLY GLU ARG GLY 0.479042 0.704225
50 ARG PRO ARG PRO ASP ASP LEU GLU ILE 0.478788 0.882353
51 SER ARG ASP HIS SER ARG THR PRO MET 0.477778 0.815789
52 ILE ARG TYR PRO LYS THR PHE GLY TRP 0.477157 0.84
53 GLY HIS ARG PRO 0.47651 0.907692
54 DPN PRO DAR DTH NH2 0.473684 0.785714
55 DPN PRO DAR ILE NH2 0.473684 0.848485
56 ARG PRO PRO ILE PHE ILE ARG ARG LEU 0.473684 0.910448
57 GLU TYR LEU GLY LEU ASP VAL PRO VAL 0.473373 0.785714
58 PHE LEU PRO HIS ALY TYR ASP VAL LYS LEU 0.473118 0.805556
59 GLY LEU LEU GLY SER PRO VAL ARG ALA 0.472393 0.84058
60 ASP PHE GLU GLU ILE PRO GLY GLU TYS LEU 0.469274 0.674419
61 ALA THR PRO PHE GLN GLU 0.468354 0.73913
62 GLU GLU ASN LEU LEU ASP PHE VAL ARG PHE 0.467066 0.73913
63 ARG PRO PRO GLY PHE SER PRO PHE ALA 0.465517 0.830986
64 LEU GLN ARG VAL LEU SEP ALA PRO PHE 0.465116 0.776316
65 GLY LEU LEU GLY SEP PRO VAL ARG ALA 0.464706 0.773333
66 ALA LEU TRP GLY PHE PHE PRO VAL LEU 0.463687 0.865672
67 DPN PRO DAR CYS NH2 0.463576 0.791045
68 SER LEU ARG PHE LEU TYR GLU GLY 0.462963 0.689189
69 ARG TYR PRO LEU THR PHE GLY TRP CYS PHE 0.462687 0.828947
70 DPN PRO ARG 0.462069 0.830769
71 ARG ARG GLU VAL HIS THR TYR TYR 0.461988 0.756757
72 SER THR GLY GLY VAL M3L LYS PRO HIS ARG 0.461538 0.794872
73 ALA LEU TRP GLY PHE VAL PRO VAL LEU 0.461111 0.865672
74 ALA LYS PHE ARG HIS ASP 0.459119 0.833333
75 HIS SER LEU PHE HIS PUK THR PRO 0.458564 0.808219
76 LYS ARG ARG ARG HIS PRO SER GLY 0.458333 0.816901
77 ILE LEU ALA LYS PHE LEU HIS GLU LEU 0.457831 0.80303
78 ARG GLN PHE GLY PRO ASP PHE PRO THR ILE 0.456989 0.849315
79 ILE ARG ALA ALA PRO PRO PRO LEU PHE 0.456647 0.897059
80 BOC HIS PRO PHE HIS STA LEU PHE 0.456647 0.810811
81 PHE GLN PRO GLN ASN GLY GLN PHE ILE 0.45614 0.811594
82 ARG GLN TRP GLY PRO ASP PRO ALA ALA VAL 0.455959 0.926471
83 HIS PRO PHE 0.455172 0.815385
84 GLY HIS LYS ILE LEU HIS ARG LEU LEU GLN 0.45509 0.878788
85 PCA PHE ARG HIS ASP SER 0.454545 0.80597
86 ARG MET PHE PRO ASN ALA PRO TYR LEU 0.454054 0.820513
87 HIS HIS ALA SER PRO ARG LYS 0.454023 0.855072
88 ILE LEU ALA LYS PHE LEU HIS ARG LEU 0.453488 0.833333
89 TYR PRO ASN VAL ASN ILE HIS ASN PHE 0.452514 0.797297
90 BOC HIS PRO PHE HIS LOV ILE HIS 0.450549 0.808219
91 ILE GLY PRO GLY ARG ALA PHE TYR THR 0.450549 0.847222
92 HIS SER ILE THR TYR LEU LEU PRO VAL 0.45 0.786667
93 ARG SER HIS SEP SER PRO ALA SER LEU GLN 0.449735 0.805195
94 ASP ARG VAL GLU LEU ASN ALA PRO ARG GLN 0.449102 0.882353
95 SER ILE ILE GLN PHE GLU HIS LEU 0.448485 0.71831
96 ASP PHE GLU GLU ILE PRO GLU GLU TYS 0.448276 0.651163
97 LYS PRO PHE PTR VAL ASN VAL GLU PHE 0.448087 0.74359
98 PHE LEU ARG GLY ARG ALA TYR VAL LEU 0.447674 0.71831
99 ARG PRO MET THR TYR LYS GLY ALA LEU 0.447368 0.805195
100 HIS LYS ILE LEU HIS ARG LEU LEU GLN GLU 0.446328 0.863636
101 GLY GLN VAL PRO PHE SER LYS GLU GLU CYS 0.445714 0.739726
102 SER LEU PHE HIS 22G THR PRO 0.445652 0.786667
103 LYS VAL PRO ARG ASN GLN ASP TRP LEU 0.445596 0.942029
104 ASP PHE GLU GLU ILE PRO GLY GLU TYR LEU 0.445055 0.791667
105 ASP PHE GLU GLU ILE PRO GLU GLU TYS LEU 0.444444 0.662791
106 SER ASN TRP SER HIS PRO GLN PHE GLU LYS 0.444444 0.777778
107 ALA PRO ALA TRP LEU PHE GLU ALA 0.44382 0.838235
108 PHE GLU ASP LEU ARG VAL LEU SER PHE 0.443787 0.680556
109 PHE GLU ASP LEU ARG VAL SER SER PHE 0.443787 0.680556
110 ARG LEU TYR GLN ASN PRO THR THR TYR ILE 0.443243 0.84
111 ILE THR ASP GLN VAL PRO PHE SER VAL 0.443182 0.739726
112 LYS ARG ARG ARG HIS PRO SER 0.443114 0.826087
113 ASP PHE GLU GLU ILE PRO GLY GLU PTR 0.442623 0.730769
114 LYS ILE LEU HIS ARG LEU LEU GLN ASP 0.442529 0.835821
115 ILE MET ASP GLN VAL PRO PHE SER VAL 0.441341 0.710526
116 ACE GLN GLU ARG GLU VAL PRO CYS 0.440994 0.865672
117 PRO HIS PRO PHE HIS LAV ILE HIS LYS 0.44086 0.850746
118 ARG GLY PHE ALA LEU M3L SER THR HIS GLY 0.44086 0.782051
119 PHE LEU ARG GLY ARG ALA TYR GLY LEU 0.439759 0.71831
120 ASP TYR ASN PRO TYR LEU LEU PHE LEU LYS 0.439306 0.794521
121 SER ILE TYR PHE TPO PRO GLU LEU TYR ASP 0.439153 0.695122
122 LYS ALA PRO ARG ALY GLN LEU ALA THR LYS 0.438202 0.819444
123 ALA ARG SER HIS SEP TYR PRO ALA 0.437838 0.7625
124 PHE GLU ALA ILE PRO ALA GLU TYR LEU 0.4375 0.774648
125 PRO PRO THR LEU HIS GLU LEU TYR ASP LEU 0.437158 0.821918
126 GLU GLU PHE GLY ARG ALA PHE SER PHE 0.437126 0.661972
127 GLY SER HIS LEU GLU VAL GLN GLY TYR TRP 0.436842 0.706667
128 ILE GLY PRO GLY ARG ALA PHE TYR ALA 0.436464 0.859155
129 ASN TYR THR PRO GLY PRO GLY THR ARG PHE 0.43617 0.837838
130 PHE GLU ASP LEU ARG LEU LEU SER PHE 0.435583 0.680556
131 GLU ALA ASP PRO THR GLY HIS SER TYR 0.435484 0.783784
132 BOC HIS PRO PHE ALA LOV ILE HIS 0.435484 0.808219
133 ASN PRO ARG ALA MET GLN ALA LEU LEU 0.435294 0.84507
134 HIS LYS ILE LEU HIS ARG LEU LEU GLN ASP 0.435028 0.850746
135 PHE LEU PRO SER ASP PHE PHE PRO SER VAL 0.434524 0.791667
136 ARG SEP PRO VAL PHE SER 0.434286 0.75
137 ILE GLY PRO GLY ARG ALA PHE TYR THR ILE 0.433862 0.824324
138 PCA PHE ARG HIS ASP SER GLY TYR GLU VAL 0.433526 0.771429
139 ASP TYR GLU PRO ILE PRO GLU GLU ALA PHE 0.433333 0.753425
140 GLY PHE ARG PRO 0.433333 0.861538
141 PRO LEU GLU PSA ARG LEU 0.432749 0.785714
142 TYR PRO LYS ARG ILE ALA 0.432749 0.857143
143 TYR GLU LEU ASP GLU LYS PHE ASP ARG LEU 0.432749 0.722222
144 ARG HIS ARG MLZ VAL LEU ARG ASP ASN TYR 0.432432 0.763158
145 ACE PHE HIS PRO ALA NH2 0.432258 0.818182
146 ILE ARG LYS ILE LEU PHE LEU ASP GLY ILE 0.431818 0.75
147 ARG HIS LYS ALY LEU MET PHE LYS 0.431818 0.785714
148 LEU PRO PHE ASP LYS THR THR ILE MET 0.430939 0.723684
149 SER SER TYR ARG ARG PRO VAL GLY ILE 0.430168 0.813333
150 TRP GLU TYR ILE PRO ASN VAL 0.429348 0.783784
151 ASN TYR THR PRO GLY PRO GLY ILE ARG PHE 0.429319 0.84
152 PHE CYS HIS PRO GLN ASN THR NH2 0.428571 0.777778
153 LYS PRO VAL LEU ARG THR ALA 0.428571 0.828571
154 ARG GLN PHE GLY PRO ASP TRP ILE VAL ALA 0.428571 0.927536
155 ARG HIS ARG MLY VAL LEU ARG ASP TYR 0.427778 0.813333
156 PRO LYS ARG PRO THR THR LEU ASN LEU PHE 0.426316 0.873239
157 ILE PRO ALA TYR GLY VAL LEU THR ILE 0.426136 0.753425
158 ARG PRO GLN VAL PRO LEU ARG PRO MET 0.425287 0.857143
159 LYS GLN GLU PRO GLN GLU ILE ASP PHE 0.424581 0.80597
160 ARG LEU GLN ARG ARG ARG GLU THR GLN VAL 0.423077 0.647887
161 LYS ILE LEU HIS ARG LEU LEU GLN ASP SER 0.423077 0.8
162 SER SER LEU GLU ASN PHE ARG ALA TYR VAL 0.423077 0.68
163 ASN GLY TYR GLU ASN PRO THR TYR LYS 0.423077 0.743243
164 LEU PRO PHE ASP LYS SER THR ILE MET 0.42246 0.714286
165 ACE GLU HIS PHE ILE VAL PRO ASP LEU TYR 0.422222 0.880597
166 GLU GLY PRO ARG ASN GLN ASP TRP LEU 0.421875 0.942029
167 GLY GLU ARG THR ILE PRO ILE THR ARG GLU 0.421053 0.805556
168 TYR TYR SER ILE ILE PRO HIS SER ILE 0.420455 0.763158
169 HIS ALA TPO PRO PRO LYS LYS GLU ALA ASP 0.420213 0.76
170 ARG HIS ARG MLY VAL LEU ARG ASP ASN 0.41954 0.819444
171 GLN LEU SER PRO PHE PRO PHE ASP LEU 0.41954 0.802817
172 LYS VAL ALA PRO PRO ILE PRO HIS ARG 0.419355 0.882353
173 SER PRO LYS ARG ILE ALA 0.41875 0.8
174 ARG ILE PRO SER TYR ARG TYR ARG TYR 0.418605 0.789474
175 ALA ASN SER ARG PHE PRO THR SER ILE ILE 0.418478 0.821918
176 PHE ARG TYR LEU GLY 0.417722 0.728571
177 ARG GLY PRO GLY CYS ALA PHE VAL THR ILE 0.415789 0.821918
178 HIS MET THR GLU VAL VAL ARG HIS CYS 0.41573 0.746667
179 SER SER ILE GLU PHE ALA ARG LEU 0.415205 0.666667
180 ASP ALA GLU PHE ARG HIS ASP 0.415094 0.69697
181 GLY ASP CYS PHE SER LYS PRO ARG 0.414365 0.791667
182 SER GLU ILE GLU PHE ALA ARG LEU 0.414201 0.676056
183 GLY TYR GLU ASN PRO THR TYR LYS PHE PHE 0.413978 0.743243
184 ALA ILE LEU HIS ARG LEU LEU GLN 0.413174 0.80303
185 ACE GLY PHE GLY VAL VAL PRO SER PHE TYR 0.413174 0.732394
186 GLY ASN PHE LEU GLN SER ARG 0.412121 0.704225
187 ARG PRO LYS ARG ILE ALA 0.412121 0.850746
188 ARG GLY TYR LEU TYR GLN GLY LEU 0.412121 0.728571
189 LEU GLU LYS ALA ARG GLY SER THR TYR 0.412088 0.702703
190 VAL PRO LEU ARG PRO MET THR TYR 0.412088 0.792208
191 ARG ARG ARG TRP HIS ARG TRP ARG LEU 0.410714 0.823529
192 ARG GLY PRO GLY ARG ALA PHE VAL THR ILE 0.410526 0.833333
193 GLY HIS ARG PRO NH2 0.410256 0.876923
194 LEU LEU TYR GLY PHE VAL ASN TYR VAL 0.409639 0.611111
195 PHE GLU ALA ASN GLY ASN LEU ILE 0.409639 0.637681
196 HCI PRO LEU HIS SER TPO ALA NH2 0.40884 0.769231
197 5JP PRO LYS ARG ILE ALA 0.408537 0.777778
198 ASN TRP SER HIS PRO GLN PHE GLU LYS 0.408537 0.771429
199 GLN VAL PRO LEU ARG PRO MET THR TYR LYS 0.407035 0.805195
200 ARG ARG LEU ILE PHE NH2 0.406452 0.671642
201 LEU ARG ASN GLN SER VAL PHE ASN PHE 0.405882 0.708333
202 ILE SER PRO ARG THR LEU ASP ALA TRP 0.405 0.864865
203 MET SER LEU PRO GLY ARG TRP LYS PRO LYS 0.404878 0.842105
204 GLU LEU PRO PRO VAL LYS ILE HIS CYS 0.404145 0.852941
205 ARG PHE MET ASP TYR TRP GLU GLY LEU 0.404145 0.736842
206 PHE PRO ARG 0.403974 0.8
207 VAL MET LEU PRO GLY ARG GLY VAL PRO 0.403315 0.828571
208 LEU LEU TRP ASN GLY PRO MET GLN VAL 0.403141 0.819444
209 LYS PRO HIS SER ASP 0.402439 0.760563
210 GLU GLY GLN PTR GLN PRO GLN PRO ALA 0.402235 0.72
211 TYR LEU GLU PRO GLY PRO VAL THR VAL 0.402235 0.767123
212 ALA ILE MET PRO ALA ARG PHE TYR PRO LYS 0.40201 0.802632
213 ALA MET ALA PRO ARG THR LEU LEU LEU 0.401163 0.773333
214 ABA SER LEU TRP ASN GLY PRO HIS LEU 0.4 0.821918
215 ARG ARG LYS TRP ARG ARG TRP HIS LEU 0.4 0.838235
216 TYR LEU GLY GLY PRO ASP PHE PRO THR ILE 0.4 0.76
217 ASN LEU VAL PRO GLN VAL ALA THR VAL 0.4 0.732394
218 LYS PRO PHE PTR VAL ASN VAL NH2 0.4 0.730769
219 PRO ARG PRO ILE LEU LEU PRO TRP ARG NH2 0.4 0.897059
220 VAL MET ALA PRO ARG ALA LEU LEU LEU 0.4 0.828571
Similar Ligands (3D)
Ligand no: 1; Ligand: LEU PRO PHE GLU LEU ARG GLY HIS LEU VAL; Similar ligands found: 0
No: Ligand Similarity coefficient
Similar Binding Sites (Proteins are less than 50% similar to leader)
Pocket No.: 1; Query (leader) PDB : 5ZYS; Ligand: LEU PRO PHE GLU LEU ARG GLY HIS LEU VAL; Similar sites found with APoc: No similar binding sites found, or similarity not calculated due to duplicate pocket.
This union binding pocket(no: 1) in the query (biounit: 5zys.bio1) has 14 residues
No: Leader PDB Ligand Sequence Similarity
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