Receptor
PDB id Resolution Class Description Source Keywords
4X3H 2.4 Å NON-ENZYME: OTHER CRYSTAL STRUCTURE OF ARC N-LOBE COMPLEXED WITH STARGAZIN PEP RATTUS NORVEGICUS ENDOCYTOSIS MEDIATOR SIGNALING PROTEIN
Ref.: STRUCTURAL BASIS OF ARC BINDING TO SYNAPTIC PROTEIN IMPLICATIONS FOR COGNITIVE DISEASE. NEURON V. 86 490 2015
Ligand
Ligand Chain:Residue Validity Ligand Warnings Binding Data NGL Viewer Molecular Weight (Da) Formula SMILES
ARG ILE PRO SER TYR ARG TYR ARG TYR B:225;
Valid;
Atoms found LESS than expected: % Diff = 0;
Ki = 96 uM
1261.5 n/a O=C(N...
View in 3D viewer
90% Homology Family
Leader
PDB id Resolution Class Description Source Keywords
4X3H 2.4 Å NON-ENZYME: OTHER CRYSTAL STRUCTURE OF ARC N-LOBE COMPLEXED WITH STARGAZIN PEP RATTUS NORVEGICUS ENDOCYTOSIS MEDIATOR SIGNALING PROTEIN
Ref.: STRUCTURAL BASIS OF ARC BINDING TO SYNAPTIC PROTEIN IMPLICATIONS FOR COGNITIVE DISEASE. NEURON V. 86 490 2015
Members (2)
No: PDB id Binding Data Representative ligand Formula Smiles
The Class containing this family consists of a total of 1579 families.
1 4X3H Ki = 96 uM ARG ILE PRO SER TYR ARG TYR ARG TYR n/a n/a
2 4X3I - ALA THR ARG ASN PHE SER GLY n/a n/a
70% Homology Family (2)
No: PDB id Binding Data Representative ligand Formula Smiles
The Class containing this family consists of a total of 1312 families.
1 4X3H Ki = 96 uM ARG ILE PRO SER TYR ARG TYR ARG TYR n/a n/a
2 4X3I - ALA THR ARG ASN PHE SER GLY n/a n/a
50% Homology Family (2)
No: PDB id Binding Data Representative ligand Formula Smiles
The Class containing this family consists of a total of 1130 families.
1 4X3H Ki = 96 uM ARG ILE PRO SER TYR ARG TYR ARG TYR n/a n/a
2 4X3I - ALA THR ARG ASN PHE SER GLY n/a n/a
Polypharmacology
Similar Ligands
Ligand no: 1; Ligand: ARG ILE PRO SER TYR ARG TYR ARG TYR; Similar ligands found: 236
No: Ligand ECFP6 Tc MDL keys Tc
1 ARG ILE PRO SER TYR ARG TYR ARG TYR 1 1
2 SER SER TYR ARG ARG PRO VAL GLY ILE 0.666667 0.945205
3 ASN ARG PRO VAL TYR ILE PRO ARG PRO PRO 0.647059 0.902778
4 ARG ARG LEU PRO ILE PHE SER ARG LEU 0.594406 0.890411
5 ARG LEU TYR GLN ASN PRO THR THR TYR ILE 0.585526 0.945946
6 ALA ASN SER ARG TYR PRO THR SER ILE ILE 0.578231 0.918919
7 ALA PHE ARG ILE PRO LEU THR ARG 0.576389 0.890411
8 TYR PRO LYS ARG ILE ALA 0.57554 0.888889
9 PRO PRO ARG PRO ILE TYR ASN ARG ASN 0.568493 0.917808
10 GLU ARG THR ILE PRO ILE THR ARG GLU 0.568182 0.887324
11 ARG THR PHE SER PRO THR TYR GLY LEU 0.556291 0.932432
12 GLN VAL PRO SER ASP PRO TYR ASN TYR 0.553191 0.813333
13 GLU VAL ALA PRO PRO GLU TYR HIS ARG LYS 0.547619 0.831169
14 ARG SEP PRO VAL PHE SER 0.541096 0.782051
15 DTY ILE ARG LEU LPD 0.540741 0.875
16 ALA ARG SER HIS SEP TYR PRO ALA 0.538462 0.860759
17 ARG PRO GLY ASN PHE LEU GLN SER ARG LEU 0.53125 0.864865
18 ALA GLN ASP ILE TYR ARG ALA SER TYR 0.530612 0.794521
19 ARG VAL SER PRO SER THR SER TYR THR PRO 0.530303 0.833333
20 ARG ARG ARG GLU ARG SER PRO THR ARG 0.528571 0.835616
21 ASN PHE ASP ASN PRO VAL TYR ARG LYS THR 0.527607 0.906667
22 ALA ILE MET PRO ALA ARG PHE TYR PRO LYS 0.524096 0.881579
23 ARG ILE ILE PRO ARG HIS LEU GLN LEU 0.522876 0.789474
24 ASP PHE GLU GLU ILE PRO GLY GLU TYR LEU 0.519231 0.824324
25 ARG PRO PRO ILE PHE ILE ARG ARG LEU 0.516779 0.835616
26 ASP PHE GLU GLU ILE PRO GLU GLU TYS 0.516779 0.701149
27 LYS TYR TYR SER ILE ILE PRO HIS SER ILE 0.513514 0.891892
28 TYR TYR SER ILE ILE PRO HIS SER ILE 0.513514 0.891892
29 DPN PRO DAR ILE NH2 0.51145 0.802817
30 ASN ALA LEU LEU ARG TYR LEU LEU ASP 0.511111 0.706667
31 ARG MET PHE PRO ASN ALA PRO TYR LEU 0.509317 0.85
32 ARG PRO MET THR TYR LYS GLY ALA LEU 0.509091 0.835443
33 ARG LEU TYR HIS SEP LEU PRO ALA 0.50625 0.85
34 CYS THR PRO SER ARG 0.503817 0.821918
35 ARG TYR PRO LEU THR PHE GLY TRP CYS PHE 0.497207 0.907895
36 ASN TYR THR PRO GLY PRO GLY ILE ARG PHE 0.49697 0.945946
37 THR PRO ARG ARG SER MLZ SER ALA 0.496296 0.84
38 ASP VAL GLN THR GLY ARG ARG PRO TYR GLU 0.49375 0.891892
39 PHE GLU ALA ILE PRO ALA GLU TYR LEU 0.493421 0.783784
40 SER ILE TYR PHE TPO PRO GLU LEU TYR ASP 0.490909 0.8125
41 TYR TYR SER ILE ALA PRO HIS SER ILE 0.490196 0.891892
42 ARG PRO LYS ARG ILE ALA 0.489209 0.805556
43 DPN PRO DAR DTH NH2 0.488722 0.84507
44 ALA ASN SER ARG PHE PRO THR SER ILE ILE 0.487342 0.878378
45 VAL SER GLN ASN TYR PRO ILE VAL GLN ASN 0.486486 0.837838
46 SER ARG ASP HIS SER ARG THR PRO MET 0.481481 0.822785
47 ILE GLY PRO GLY ARG ALA PHE TYR ALA 0.481013 0.890411
48 ASN TYR THR PRO GLY PRO GLY THR ARG PHE 0.478788 0.918919
49 ILE GLY PRO GLY ARG ALA PHE TYR VAL 0.478261 0.878378
50 ILE GLY PRO GLY ARG ALA PHE TYR THR 0.478261 0.90411
51 LEU PRO PHE ASP ARG THR THR ILE MET 0.478261 0.833333
52 ASP TYR GLU PRO ILE PRO GLU GLU ALA PHE 0.477707 0.835616
53 TYR PRO SER LYS PRO ASP ASN PRO GLY GLU 0.477612 0.830986
54 DPN PRO DAR CYS NH2 0.477273 0.75
55 GLN VAL PRO LEU ARG PRO MET THR TYR LYS 0.476744 0.858974
56 ARG ILE PHE SER 0.476562 0.690141
57 GLY GLU ARG THR ILE PRO ILE THR ARG GLU 0.47619 0.863014
58 GLY ARG PRO ARG THR THR SER PHE ALA GLU 0.475 0.876712
59 LYS LEU TYR GLN ASN PRO THR THR TYR ILE 0.475 0.864865
60 ARG ARG ILE TYR ASP LEU ILE GLU LEU 0.472973 0.72973
61 LYS ARG ARG ARG HIS PRO SER 0.472603 0.808219
62 ACE GLY PHE GLY VAL VAL PRO SER PHE TYR 0.471831 0.767123
63 TYR PRO TYR ASP VAL PRO ASP TYR ALA 0.471831 0.797297
64 VAL PRO LEU ARG PRO MET THR TYR 0.471338 0.87013
65 LYS ARG ARG ARG HIS PRO SER GLY 0.469799 0.824324
66 ALA ARG THR GLU LEU TYR ARG SER LEU 0.468966 0.756757
67 ARG PRO PRO GLY PHE SER PRO PHE ALA 0.467949 0.888889
68 SER PRO LYS ARG ILE ALA 0.467153 0.833333
69 ARG GLN PHE GLY PRO ASP PHE PRO THR ILE 0.467066 0.931507
70 ILE GLY PRO GLY ARG ALA PHE TYR THR ILE 0.467066 0.931507
71 ALA ASN SER ARG VAL PRO THR SER ILE ILE 0.465753 0.863014
72 N7P THR SEP PRO SER TYR SET 0.465753 0.78481
73 PRO THR SEP PRO SER TYR 0.465753 0.792208
74 DMG PRO ARG ARG ARG SER ARG LYS PRO 0.465116 0.8
75 ASN ARG PRO VAL TYR ILE PRO PRO PRO PRO 0.464789 0.819444
76 HIS HIS ALA SER PRO ARG LYS 0.464516 0.835616
77 LYS LEU PRO ALA GLN PHE TYR ILE LEU 0.462963 0.810811
78 TRP GLU TYR ILE PRO ASN VAL 0.462963 0.792208
79 GLY TYR GLU ASN PRO THR TYR LYS PHE PHE 0.462963 0.824324
80 GLN ARG SER THR SEP THR PRO ASN VAL HIS 0.461039 0.7625
81 ARG THR TYR SEP GLY PRO MET ASN LYS VAL 0.460674 0.8
82 ALA ASN SER ARG ALA PRO THR SER ILE ILE 0.460526 0.84
83 ASP PHE GLU GLU ILE PRO GLY GLU PTR 0.460123 0.78481
84 LEU PRO PHE GLU ARG ALA THR ILE MET 0.458333 0.820513
85 ASP ILE ASN TYR TYR ALA SER GLU PRO 0.457516 0.864865
86 ARG TYR PRO LEU THR PHE GLY TRP 0.457143 0.894737
87 PHQ LEU VAL ARG TYR 0.457143 0.72
88 ILE ARG TYR PRO LYS THR PHE GLY TRP 0.456044 0.92
89 ALA ASN SER ARG LEU PRO THR SER ILE ILE 0.455172 0.863014
90 SER PRO ILE VAL PRO SER PHE ASP MET 0.455128 0.769231
91 ARG PRO GLY ASN PHE LEU GLN SER ARG PRO 0.45509 0.866667
92 5JP PRO LYS ARG ILE ALA 0.454545 0.797297
93 GLU THR VAL ARG PHE GLN SER ASP 0.452703 0.675676
94 SER ASP TYR GLN ARG LEU 0.451852 0.689189
95 ILE PRO ALA TYR GLY VAL LEU THR ILE 0.451613 0.810811
96 SER LEU SER ARG THR PRO ALA ASP GLY ARG 0.451613 0.849315
97 LEU PRO PRO LEU ASP ILE THR PRO TYR 0.451613 0.810811
98 PHE TYR ALA PRO GLU PRO ILE THR SER LEU 0.450617 0.866667
99 VAL MET ALA PRO ARG THR LEU PHE LEU 0.450617 0.807692
100 GLN ALA SER TPO PRO ARG NIT 0.450617 0.755814
101 LEU PRO SER PHE GLU THR ALA LEU 0.450331 0.783784
102 ARG ARG ALA SEP ALA PRO LEU PRO 0.450331 0.772152
103 ARG PRO MET THR PHE LYS GLY ALA LEU 0.450292 0.797468
104 1IP CYS PHE SER LYS PRO ARG 0.449367 0.815789
105 ARG GLY PRO GLY ARG ALA PHE VAL THR ILE 0.449102 0.890411
106 ASP ILE ALA TYR TYR THR SER GLU PRO 0.44898 0.876712
107 ARG THR PRO SEP LEU PRO THR 0.44898 0.807692
108 LEU GLN ARG VAL LEU SEP ALA PRO PHE 0.448718 0.7625
109 ASN ARG PRO ILE LEU SER LEU 0.448276 0.826667
110 ALA ALA ARG KCR SER ALA PRO ALA 0.447368 0.810811
111 SER SER LEU GLU ASN PHE ARG ALA TYR VAL 0.447205 0.76
112 GLY TYR GLN ASP TYR GLU PRO GLU ALA 0.446809 0.739726
113 ALA THR VAL ARG THR TYR SER CYS 0.446809 0.72973
114 VAL PRO TYR SER SER ALA GLN NAG 0.446667 0.78481
115 LEU PRO PHE GLU ARG ALA THR VAL MET 0.446429 0.807692
116 SER LEU ARG PHE LEU TYR GLU GLY 0.445205 0.77027
117 ACE GLU LEU LEU MET VAL PRO ASP MET TYR 0.444444 0.705128
118 SER HIS PRO ARG PRO ILE ARG VAL 0.442308 0.866667
119 SER TYR SEP PRO THR SEP PRO SEP TYR SER 0.442177 0.779221
120 TYR PRO PHE PHE NH2 0.44186 0.760563
121 ASP ILE ASN TYR TYR THR SER GLU PRO 0.441558 0.864865
122 ACE GLN PM3 GLU GLU ILE PRO 0.440559 0.692308
123 ALA VAL ALA PHE TYR ILE PRO ASP GLN ALA 0.440559 0.805556
124 ALA ASN SER ARG HIS PRO THR SER ILE ILE 0.43871 0.891892
125 GLU TYR LEU GLY LEU ASP VAL PRO VAL 0.43871 0.77027
126 THR PRO TYR ASP ILE ASN GLN MET LEU 0.438272 0.759494
127 ALA ASN SER ARG ALY PRO THR SER ILE ILE 0.438272 0.842105
128 SER SER ARG LYS GLU TYR TYR ALA 0.437956 0.726027
129 PRO SER TYR SEP PRO THR SEP PRO SER 0.437086 0.782051
130 LYS PRO VAL LEU ARG THR ALA 0.436242 0.835616
131 GLN ASN TYR PRO ILE VAL GLN 0.436242 0.773333
132 ARG TYR PRO LEU THR LEU GLY TRP CYS PHE 0.435484 0.896104
133 ALA LEU PRO HIS ALA ILE LEU ARG LEU 0.434783 0.786667
134 GLU SER ASP PRO ILE VAL ALA GLN TYR 0.434783 0.837838
135 PHE ARG TYR LEU GLY 0.434783 0.716216
136 ALA ASN SER ARG TRP PRO THR THR ARG LEU 0.434524 0.87013
137 ARG VAL ALA GLN LEU GLU GLN VAL TYR ILE 0.434211 0.689189
138 GLU LEU ARG SER ARG TYR TRP ALA ILE 0.433735 0.828947
139 LYS PRO ILE VAL GLN TYR ASP ASN PHE 0.433735 0.84
140 ALA ILE ALA TYR PHE ILE PRO ASP GLN ALA 0.433566 0.816901
141 ALA ARG MLZ SER ALA PRO ALA THR 0.433333 0.828947
142 HIS SER ILE THR TYR LEU LEU PRO VAL 0.432927 0.866667
143 SER PRO ARG LEU PRO LEU LEU GLU SER 0.432624 0.777778
144 ILE SER PRO ARG THR LEU ASP ALA TRP 0.432584 0.894737
145 ALA ASN SER ARG TRP PRO ALY SER ILE ILE 0.432584 0.858974
146 LEU SER SER PRO VAL THR LYS SER PHE 0.432258 0.819444
147 TRP MET ASP PHE ASP ASP ASP ILE PRO PHE 0.431818 0.712329
148 TRP ASP ILE PRO PHE 0.431818 0.712329
149 PRO SER ILE ASP ARG SER THR LYS PRO 0.43125 0.890411
150 DPN PRO ARG 0.430769 0.736111
151 PHE PRO ARG 0.430769 0.732394
152 ARG VAL ALA SER PRO THR SER GLY VAL 0.42953 0.824324
153 LYS VAL PRO ARG ASN GLN ASP TRP LEU 0.429379 0.818182
154 SER ARG ILE ARG ILE ARG GLY TYR VAL ARG 0.428571 0.783784
155 VAL ALA PHE ARG SER 0.428571 0.652778
156 PHE ASN ARG PRO VAL 0.427586 0.773333
157 PHE ALA PRO GLY PHE PHE PRO TYR LEU 0.426752 0.810811
158 ACE TYR PRO ILE GLN GLU THR 0.426667 0.77027
159 ARG GLN ALA SEP ILE GLU LEU PRO SER MET 0.426136 0.75
160 GLU GLU PRO THR VAL ILE LYS LYS TYR 0.425926 0.824324
161 PHE LEU PRO HIS ALY TYR ASP VAL LYS LEU 0.425287 0.789474
162 TYR GLN PHE GLY PRO ASP PHE PRO ILE ALA 0.42515 0.849315
163 ARG PRO ARG PRO ASP ASP LEU GLU ILE 0.424837 0.810811
164 PRO LYS ARG PRO THR THR LEU ASN LEU PHE 0.424419 0.878378
165 PRO GLN PTR GLU PTR ILE PRO ALA 0.424051 0.772152
166 MET TRP ARG PRO TRP 0.424051 0.766234
167 ARG GLY TYR VAL TYR GLN GLY LEU 0.422819 0.716216
168 ALA PRO ASP THR ARG PRO 0.422535 0.837838
169 ILE ARG ALA ALA PRO PRO PRO LEU PHE 0.421384 0.824324
170 ARG GLU ARG SER PRO THR ARG 0.421053 0.794521
171 ACE GLN GLU ARG GLU VAL PRO CYS 0.42069 0.723684
172 GLU LEU LYS ARG LYS MET ILE TYR MET 0.420382 0.679487
173 SER ALA PRO ASP THR ARG PRO ALA 0.42 0.851351
174 SER PRO THR SER PRO SEP TYR SER PRO PRO 0.419355 0.792208
175 PRO ARG PRO ILE LEU LEU PRO TRP ARG NH2 0.418182 0.824324
176 ARG GLY TYR LEU TYR GLN GLY LEU 0.417808 0.716216
177 PRO GLN PTR GLU GLU ILE PRO ILE 0.417722 0.746835
178 ARG PHE PRO LEU THR PHE GLY TRP 0.417143 0.868421
179 ALA ASN SER ARG TRP PRO THR SER ALY ILE 0.416667 0.871795
180 GLU LEU ARG ARG LYS MET MET TYR MET 0.416107 0.679487
181 GLY GLY ARG LYS LYS TYR LYS LEU 0.415493 0.716216
182 GLY GLY LYS LYS LYS TYR ARG LEU 0.415493 0.716216
183 VAL LYS VAL VAL ALA LYS LYS TYR ARG ASN 0.415493 0.706667
184 GLY GLY LYS LYS ARG TYR LYS LEU 0.415493 0.716216
185 SER THR GLY GLY VAL M3L LYS PRO HIS ARG 0.415301 0.802469
186 DVA DPR GLY DSN DGN DHI DTY DAS DSN 0.414634 0.828947
187 ALA ILE ARG SER 0.414634 0.647887
188 SER GLU LEU GLU ILE LYS ARG TYR 0.414474 0.77027
189 ARG LEU PRO ALA LYS ALA PRO LEU LEU 0.414474 0.783784
190 PHE LEU PRO SER ASP PHE PHE PRO SER VAL 0.414474 0.824324
191 LEU TYR ALA SER PRO GLN LEU GLU GLY PHE 0.414201 0.824324
192 LEU LEU PHE GLY LYS PRO VAL TYR VAL 0.41358 0.786667
193 PRO PRO LYS ARG ILE ALA 0.413333 0.805556
194 3BY PRO LYS ARG ILE ALA 0.413333 0.776316
195 ARG ARG ARG ARG SER TRP TYR 0.413043 0.753425
196 LEU PHE GLY TYR PRO VAL TYR VAL 0.412903 0.783784
197 TYR HIS SEP VAL VAL ARG TYR ALA 0.4125 0.7625
198 ASN GLY TYR GLU ASN PRO THR TYR LYS 0.412121 0.824324
199 LYS PRO ILE VAL VAL LEU HIS GLY TYR 0.411765 0.789474
200 ASN ASP TRP LEU LEU PRO SER TYR 0.411765 0.831169
201 ARG GLN PHE GLY PRO ASP TRP ILE VAL ALA 0.411765 0.828947
202 GLY ALA ALA ARG ALA GLU VAL TYR LEU ARG 0.411392 0.693333
203 ALA PRO ASP THR ARG PRO ALA PRO 0.410959 0.837838
204 ARG GLN PRO ALA LYS ALA PRO LEU LEU 0.410256 0.773333
205 TYR SEP PRO THR SEP PRO SER 0.409722 0.782051
206 ASN ASP LYS TYR GLU PRO PHE TRP GLU 0.40884 0.776316
207 ARG VAL ALA SEP PRO THR SER GLY VAL 0.408805 0.7625
208 LEU ASP PRO ARG 0.408759 0.756757
209 ARG PRO LYS PRO LEU VAL ASP PRO 0.408451 0.791667
210 GLY LEU LEU GLY SER PRO VAL ARG ALA 0.407895 0.797297
211 ALA ASN SER ARG TRP PRO THR SER FAK ILE 0.407609 0.85
212 ILE THR ASP GLN VAL PRO PHE SER VAL 0.407407 0.797297
213 LEU PRO PRO GLU GLU ARG LEU ILE 0.406667 0.783784
214 LEU LEU PHE GLY PHE PRO VAL TYR VAL 0.40625 0.783784
215 LEU LEU PHE GLY TYR PRO VAL TYR VAL 0.40625 0.783784
216 ILE MET ASP GLN VAL PRO PHE SER VAL 0.406061 0.74359
217 GLU LEU ASN ARG LYS MET ILE TYR MET 0.406061 0.696203
218 ALA MET ALA PRO ARG THR LEU LEU LEU 0.405229 0.782051
219 ALA ASN SER ARG TRP PRO THR SER 2KK ILE 0.404255 0.8625
220 PRO ARG ARG PRO VAL ILE MET ARG ARG 0.403846 0.763158
221 MET CYS PRO ARG MET THR ALA VAL MET 0.403727 0.805195
222 LEU PRO PHE ASP LYS SER THR ILE MET 0.403509 0.769231
223 ARG PHE PRO LEU THR PHE GLY TRP CYS PHE 0.403226 0.87013
224 ARG PRO PRO GLY PHE 0.402778 0.777778
225 SER SER ILE GLU PHE ALA ARG LEU 0.402597 0.702703
226 ALA PRO SER PTR VAL ASN VAL GLN ASN 0.402516 0.743902
227 TYR MET PHE PRO ASN ALA PRO TYR LEU 0.402439 0.7625
228 ASP PHE GLU GLU ILE PRO GLY GLU TYS LEU 0.402367 0.704545
229 LYS ARG LYS SER ARG TRP ASP GLU THR PRO 0.402367 0.855263
230 ASN TRP SER HIS PRO GLN PHE GLU LYS 0.401361 0.77027
231 LYS ALA PRO ARG ALY GLN LEU ALA THR LYS 0.401361 0.733333
232 ASP ARG VAL GLU LEU ASN ALA PRO ARG GLN 0.401274 0.763158
233 GLY GLN VAL PRO PHE SER LYS GLU GLU CYS 0.401235 0.75
234 MET SER LEU PRO GLY ARG TRP LYS PRO LYS 0.40107 0.825
235 ALA THR ARG ASN PHE SER GLY 0.4 0.712329
236 THR PRO ARG VAL THR GLY GLY GLY ALA MET 0.4 0.78481
Similar Binding Sites (Proteins are less than 50% similar to leader)
Pocket No.: 1; Query (leader) PDB : 4X3H; Ligand: ARG ILE PRO SER TYR ARG TYR ARG TYR; 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: 4x3h.bio1) has 22 residues
No: Leader PDB Ligand Sequence Similarity
APoc FAQ
Feedback