Receptor
PDB id Resolution Class Description Source Keywords
4IKN 1.85 Å NON-ENZYME: OTHER CRYSTAL STRUCTURE OF ADAPTOR PROTEIN COMPLEX 3 (AP-3) MU3A S TERMINAL DOMAIN, IN COMPLEX WITH A SORTING PEPTIDE FROM TGN RATTUS NORVEGICUS IMMUNOGLOBULIN-LIKE BETA-SANDWICH SIGNAL RECOGNITION CYTOSOF TRANSMEMBRANE PROTEINS ADAPTOR PROTEIN PROTEIN TRANSPO
Ref.: STRUCTURAL BASIS FOR THE RECOGNITION OF TYROSINE-BA SORTING SIGNALS BY THE MU 3A SUBUNIT OF THE AP-3 AD COMPLEX. J.BIOL.CHEM. V. 288 9563 2013
Ligand
Ligand Chain:Residue Validity Ligand Warnings Binding Data NGL Viewer Molecular Weight (Da) Formula SMILES
SER ASP TYR GLN ARG LEU B:1;
Valid;
none;
Kd = 14 uM
693.759 n/a O=C([...
View in 3D viewer
90% Homology Family
Leader
PDB id Resolution Class Description Source Keywords
4IKN 1.85 Å NON-ENZYME: OTHER CRYSTAL STRUCTURE OF ADAPTOR PROTEIN COMPLEX 3 (AP-3) MU3A S TERMINAL DOMAIN, IN COMPLEX WITH A SORTING PEPTIDE FROM TGN RATTUS NORVEGICUS IMMUNOGLOBULIN-LIKE BETA-SANDWICH SIGNAL RECOGNITION CYTOSOF TRANSMEMBRANE PROTEINS ADAPTOR PROTEIN PROTEIN TRANSPO
Ref.: STRUCTURAL BASIS FOR THE RECOGNITION OF TYROSINE-BA SORTING SIGNALS BY THE MU 3A SUBUNIT OF THE AP-3 AD COMPLEX. J.BIOL.CHEM. V. 288 9563 2013
Members (1)
No: PDB id Binding Data Representative ligand Formula Smiles
The Class containing this family consists of a total of 1256 families.
1 4IKN Kd = 14 uM SER ASP TYR GLN ARG 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 1068 families.
1 4IKN Kd = 14 uM SER ASP TYR GLN ARG LEU 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 922 families.
1 4IKN Kd = 14 uM SER ASP TYR GLN ARG LEU n/a n/a
Polypharmacology
Similar Ligands
Ligand no: 1; Ligand: SER ASP TYR GLN ARG LEU; Similar ligands found: 204
No: Ligand ECFP6 Tc MDL keys Tc
1 SER ASP TYR GLN ARG LEU 1 1
2 GLY GLY ARG LYS LYS TYR LYS LEU 0.638095 0.929825
3 GLY GLY LYS LYS LYS TYR ARG LEU 0.638095 0.929825
4 GLY GLY LYS LYS ARG TYR LYS LEU 0.638095 0.929825
5 TYR GLU LEU ASP GLU LYS PHE ASP ARG LEU 0.627119 0.915254
6 ARG ARG ILE TYR ASP LEU ILE GLU LEU 0.618644 0.947368
7 ARG GLY TYR LEU TYR GLN GLY LEU 0.612613 0.929825
8 GLY GLY LYS LYS LYS TYR GLN LEU 0.609524 0.824561
9 ASP ALA ASP GLU TYR LEU 0.607843 0.781818
10 ALA ARG THR GLU LEU TYR ARG SER LEU 0.603448 0.915254
11 SER GLN TYR TYR TYR ASN SER LEU 0.601942 0.754098
12 PHE ARG TYR LEU GLY 0.587156 0.929825
13 ARG GLY TYR VAL TYR GLN GLY LEU 0.586207 0.929825
14 GLU LEU ARG ARG LYS MET MET TYR MET 0.578947 0.868852
15 SER SER ARG LYS GLU TYR TYR ALA 0.575472 0.87931
16 ALA ASN SER ARG TRP GLN ASP THR ARG LEU 0.572581 0.8
17 TYR GLN SER LYS LEU 0.567308 0.827586
18 ARG ARG LEU LEU ARG GLY HIS ASN GLN TYR 0.565891 0.830769
19 VAL LYS VAL VAL ALA LYS LYS TYR ARG ASN 0.563636 0.913793
20 PHE TYR ARG ALA LEU MET 0.559322 0.866667
21 ASP LEU TYR CYS TYR GLU GLN LEU ASN 0.547826 0.783333
22 PHE TYR ARG TYR GLY PHE VAL ALA ASN PHE 0.546219 0.864407
23 SER GLU LEU GLU ILE LYS ARG TYR 0.545455 0.9
24 GLU ASN GLN LYS GLU TYR PHE PHE 0.545455 0.728814
25 ASP ASN ARG LEU GLY LEU VAL TYR GLN PHE 0.54 0.75
26 THR ARG ARG GLU THR GLN LEU 0.537736 0.827586
27 GLY GLY LYS LYS LYS TYR LYS LEU 0.533333 0.807018
28 PHE LEU ARG GLY ARG ALA TYR GLY LEU 0.532787 0.913793
29 GLU LEU LYS ARG LYS MET ILE TYR MET 0.531746 0.868852
30 ARG VAL ALA GLN LEU GLU GLN VAL TYR ILE 0.528 0.963636
31 LEU TYR LEU VAL CYS GLY GLU ARG VAL 0.527559 0.929825
32 GLU ALA GLN THR ARG LEU 0.527273 0.857143
33 TYR ASP GLN ILE LEU 0.522936 0.8
34 GLU LEU ASN ARG LYS MET ILE TYR MET 0.518797 0.857143
35 PHE LEU ARG GLY ARG ALA TYR VAL LEU 0.515385 0.913793
36 SER SER LEU GLU ASN PHE ARG ALA TYR VAL 0.514706 0.885246
37 THR ASN GLU TYR LYS VAL 0.513761 0.821429
38 SER GLU ILE GLU PHE ALA ARG LEU 0.512195 0.862069
39 GLU LEU LYS TPO GLU ARG TYR 0.512 0.830769
40 THR ASN GLU PHE TYR PHE 0.509615 0.701754
41 GLY ASN PHE LEU GLN SER ARG 0.508333 0.833333
42 LEU TYR LEU VAL CYS GLY GLU ARG GLY 0.507812 0.929825
43 LEU TYR LEU VAL CYS GLY GLU ARG GLY PHE 0.507463 0.898305
44 THR ASN GLU TYR TYR VAL 0.504854 0.754386
45 ALA ARG THR MLY GLN THR ALA ARG TYR 0.5 0.818182
46 SER SER ILE GLU PHE ALA ARG LEU 0.5 0.847458
47 ASP ALA GLU PHE ARG HIS ASP SER 0.496 0.758065
48 GLU ASN LEU TYR PHE GLN 0.495575 0.775862
49 ACE ILE TYR GLU SER LEU 0.495413 0.775862
50 ASP PHE GLU ASP TYR GLU PHE ASP 0.495413 0.701754
51 ASP ASP LEU TYR GLY 0.490385 0.803571
52 ARG PHE MET ASP TYR TRP GLU GLY LEU 0.489655 0.80597
53 ARG HIS ARG MLZ VAL LEU ARG ASP ASN TYR 0.489362 0.782609
54 GLU THR VAL ARG PHE GLN SER ASP 0.488372 0.862069
55 ASP GLU LEU GLU ILE LYS ALA TYR 0.487805 0.807018
56 SER GLN ASN TYR 0.485149 0.711864
57 ARG LEU GLN ARG ARG ARG GLU THR GLN VAL 0.482456 0.827586
58 ALA GLN PHE SER ALA SER ALA SER ARG 0.482456 0.827586
59 GLU ASN PRO THR TYR LYS PHE PHE GLU GLN 0.482456 0.733333
60 THR TYR LYS PHE PHE GLU GLN 0.482456 0.733333
61 ARG ARG ARG TRP HIS ARG TRP ARG LEU 0.479675 0.738462
62 GLU GLN TYR LYS PHE TYR SER VAL 0.478992 0.770492
63 GLY ARG PHE GLN VAL THR 0.477477 0.818182
64 ASP PHE GLU GLU ILE 0.47619 0.690909
65 SER ARG ILE ARG ILE ARG GLY TYR VAL ARG 0.47619 0.885246
66 ALA TYR ARG 0.475248 0.888889
67 ASP ALA GLU PHE ARG HIS ASP 0.475 0.758065
68 TYR GLY GLY PHE LEU 0.472727 0.758621
69 GLU GLU TYR LEU GLN ALA PHE THR TYR 0.472441 0.775862
70 ALA THR VAL ARG THR TYR SER CYS 0.471074 0.881356
71 LEU GLU LYS ALA ARG GLY SER THR TYR 0.471014 0.885246
72 GLU GLU ASN LEU LEU ASP PHE VAL ARG PHE 0.469231 0.847458
73 LYS TYR LYS 0.46875 0.714286
74 SER ARG TYR TRP ALA ILE ARG THR ARG 0.468085 0.764706
75 ARG HIS ARG MLY VAL LEU ARG ASP TYR 0.467626 0.760563
76 TYR GLN PHE 0.465347 0.696429
77 ASP VAL GLN THR GLY ARG ARG PRO TYR GLU 0.465278 0.757143
78 THR PRO ASP TYR PHE LEU 0.464912 0.741935
79 ARG ARG LYS TRP ARG ARG TRP HIS LEU 0.464567 0.727273
80 THR PHE GLN ALA PSA LEU ARG GLU 0.463768 0.836066
81 GLY ALA ALA ARG ALA GLU VAL TYR LEU ARG 0.462687 0.929825
82 THR LYS ASN TYR LYS GLN THR SER VAL 0.459677 0.770492
83 SER ILE ILE ASN PHE GLU LYS LEU 0.459677 0.721311
84 ASN ALA LEU LEU ARG TYR LEU LEU ASP 0.459459 0.75
85 GLU LEU ASP LYS TYR ALA SER 0.458333 0.810345
86 HIS LYS ILE LEU HIS ARG LEU LEU GLN ASP 0.456522 0.765625
87 LEU ASP GLU GLU THR GLY GLU PHE LEU 0.455285 0.758621
88 LYS MET ASP SEP PHE LEU ASP MET GLN LEU 0.455224 0.628571
89 LYS LYS ALA THR GLN ALA SEP GLN GLU TYR 0.454545 0.6875
90 ARG LEU TYR GLN ASN PRO THR THR TYR ILE 0.452703 0.716216
91 ARG MET PHE PRO ASN ALA PRO TYR LEU 0.452703 0.701299
92 THR LYS ASN TYR LYS GLN PHE SER VAL 0.45082 0.758065
93 GLU ILE ILE ASN PHE GLU LYS LEU 0.448 0.711864
94 ARG ILE PRO SER TYR ARG TYR ARG TYR 0.445255 0.689189
95 ASN PHE ASP ASN PRO VAL TYR ARG LYS THR 0.444444 0.726027
96 ARG PRO GLY ASN PHE LEU GLN ASN ARG PRO 0.444444 0.824561
97 ARG ARG LEU PRO ILE PHE SER ARG LEU 0.442857 0.680556
98 GLN PHE LYS ASP ASN VAL ILE LEU LEU 0.442748 0.728814
99 ALA LYS PHE ARG HIS ASP 0.442623 0.746032
100 VAL ARG SER ARG ARG ABA LEU ARG LEU 0.441441 0.766667
101 LEU GLU PHE GLN GLY 0.441441 0.763636
102 SER ILE ILE GLY PHE GLU LYS LEU 0.440945 0.716667
103 LYS ILE LEU HIS ARG LEU LEU GLN ASP 0.440945 0.774194
104 GLY VAL TYR ASP GLY ARG GLU HIS THR VAL 0.440559 0.80303
105 SEP GLN GLU TYR NH2 0.440367 0.671875
106 LEU GLY GLY ALA LYS GLN ARG GLY ASP VAL 0.439655 0.789474
107 ALA PTR ARG 0.439252 0.774194
108 MET LEU TRP GLY TYR LEU GLN TYR VAL 0.438849 0.701493
109 ARG ASP ARG ALA ALA LYS LEU 0.438095 0.785714
110 ILE LEU GLY LYS PHE LEU HIS ARG LEU 0.437956 0.753846
111 SER LEU ASN TYR ILE ILE LYS VAL LYS GLU 0.437037 0.774194
112 VAL ARG SER ARG ARG CYS LEU ARG LEU 0.436364 0.766667
113 ARG ARG LEU ILE PHE NH2 0.435897 0.803571
114 ASP ARG VAL TYR ILE HIS PRO PHE 0.435897 0.75
115 THR ASN GLU PHE TYR ALA 0.435897 0.7
116 VAL ALA PHE ARG SER 0.434783 0.821429
117 ACE ALA ARG THR GLU VAL TYR NH2 0.434426 0.946429
118 DTY ILE ARG LEU LPD 0.434109 0.761194
119 ASP GLU THR ASN LEU 0.433962 0.672414
120 THR GLU ASN LEU TYR PHE GLN SER GLY THR 0.433824 0.774194
121 ASP ALA ASP GLU FTY LEU NH2 0.433628 0.609375
122 LYS ILE LEU HIS ARG LEU LEU GLN ASP SER 0.433566 0.769231
123 GLY ASN TYR SER PHE TYR ALA LEU 0.433333 0.725806
124 GLU GLU GLN GLU GLU TYR 0.43299 0.722222
125 PRO LEU GLU PSA ARG LEU 0.432836 0.809524
126 ALA ARG LYS LEU ASP 0.432692 0.821429
127 VAL LEU ARG ASP ASP LEU LEU GLU ALA 0.432432 0.854545
128 LYS VAL PRO ARG ASN GLN ASP TRP LEU 0.432258 0.684932
129 ALA LEU TYR ASN THR ALA ALA ALA LEU 0.432203 0.724138
130 CYS THR GLU LEU LYS LEU ASN ASP TYR 0.430769 0.8
131 ARG ILE ILE PRO ARG HIS LEU GLN LEU 0.428571 0.676056
132 SER VAL TYR ASP PHE PHE VAL TRP LEU 0.428571 0.666667
133 ARG TYR GLY PHE VAL ALA ASN PHE 0.428571 0.898305
134 ASN TYR THR PRO GLY PRO GLY THR ARG PHE 0.427632 0.712329
135 GLU GLU PHE GLY ARG ALA PHE SER PHE 0.427481 0.783333
136 PHE LEU SER TYR LYS 0.42735 0.766667
137 PHE LEU ALA TYR LYS 0.42735 0.77193
138 ARG ARG ARG TRP ARG ARG LEU THR VAL 0.426357 0.784615
139 ASN TYR THR PRO GLY PRO GLY ILE ARG PHE 0.425806 0.726027
140 TYR HIS SEP VAL VAL ARG TYR ALA 0.425532 0.69863
141 PHE ALA GLY LEU ARG GLN ALA VAL THR GLN 0.425 0.842105
142 LEU ALA ILE TYR SER 0.424779 0.736842
143 LYS LEU PRO ALA GLN PHE TYR ILE LEU 0.424658 0.657143
144 ALA ASN SER ARG TRP GLN THR SER ILE ILE 0.42446 0.772727
145 ALA LEU ASP LEU PHE 0.424242 0.666667
146 SER LEU TYR ASN THR ILE ALA THR LEU 0.424 0.75
147 GLY TYR GLN ASP TYR GLU PRO GLU ALA 0.424 0.651515
148 ASP SEP TYR GLU VAL LEU ASP LEU 0.422222 0.703125
149 SER SER LEU GLU ASN PHE ALA ALA TYR VAL 0.422222 0.754098
150 GLU ARG GLU SEP GLU PHE ASP ILE GLU ASP 0.421429 0.727273
151 ILE GLN GLN SER ILE GLU ARG ILE 0.420168 0.779661
152 SER GLU ASP GLU PHE TYR ASP ALA LEU SER 0.419847 0.779661
153 ARG ARG ARG ARG ARG ARG ARG ARG ARG ARG 0.419355 0.714286
154 GLU GLY PRO ARG ASN GLN ASP TRP LEU 0.419355 0.684932
155 SER HIS PHE ASN GLU TYR GLU 0.41791 0.656716
156 ALA ASN SER ARG TYR PRO THR SER ILE ILE 0.417808 0.736111
157 ASP TYR GLU PRO ILE PRO GLU GLU ALA PHE 0.417808 0.633803
158 ASP PHE GLU GLU ILE PRO GLY GLU TYR LEU 0.416107 0.671429
159 THR PRO TYR ASP ILE ASN GLN MET LEU 0.416107 0.626667
160 SER LEU TYR ASN THR VAL ALA THR LEU 0.416 0.745763
161 ALA ALA SER LEU TYR GLU LYS LYS ALA ALA 0.416 0.79661
162 GLU ASP GLU ASP PHE GLU ILE LEU SER LEU 0.415385 0.728814
163 ASN PRO ARG ALA MET GLN ALA LEU LEU 0.414815 0.652778
164 SER ARG ARG TRP ARG ARG TRP ASN ARG 0.414634 0.691176
165 PHE ARG SER LYS GLY GLU GLU LEU PHE THR 0.414286 0.836066
166 ARG ARG ARG ARG SER TRP TYR 0.414062 0.716418
167 GLY ALA GLN THR PHE TYR VAL ASP GLY ALA 0.414062 0.766667
168 GLY HIS LYS ILE LEU HIS ARG LEU LEU GLN 0.413534 0.738462
169 SER SER THR ARG GLY ILE SER GLN LEU TRP 0.413333 0.776119
170 ALA ARG THR M3L GLN THR ALA ARG 0.413223 0.705882
171 SER LEU TYR ASN VAL VAL ALA THR LEU 0.412698 0.745763
172 HIS LYS ILE LEU HIS ARG LEU LEU GLN GLU 0.412587 0.75
173 ASP PHE M3L THR ASP 0.411765 0.656716
174 ASP PHE SER ILE 0.411215 0.644068
175 ALA ARG THR ALY GLN THR ALA 0.410256 0.737705
176 ARG PRO MET THR TYR LYS GLY ALA LEU 0.410256 0.72973
177 ARG ARG ARG GLU THR GLN VAL 0.409091 0.839286
178 SER SER VAL VAL GLY VAL TRP TYR LEU 0.408759 0.681818
179 ASP SER LYS ASP VAL LYS GLU TRP TYR VAL ZN 0.408451 0.647887
180 SER LEU TYR LEU THR VAL ALA THR LEU 0.408333 0.724138
181 ARG LEU TRP SER 0.408333 0.777778
182 ASN ARG LEU MET LEU THR GLY 0.408333 0.774194
183 LYS ARG LYS ARG LYS ARG LYS ARG LYS ARG 0.408163 0.701754
184 BP4 CYS DAR TYR PEA 0.407692 0.8
185 PHQ LEU VAL ARG TYR 0.407692 0.866667
186 ALA ARG THR M3L GLN THR ALA 0.40678 0.691176
187 ALA ARG THR M3L GLN THR ALA 2MR LYS 0.40678 0.691176
188 ALA ARG THR M3L GLN THR ALA ARG LYS SER 0.40678 0.691176
189 PHE GLN TRP MET GLY TYR GLU LEU TRP 0.406667 0.691176
190 PRO GLU GLY ASP PM3 GLU GLU VAL LEU 0.40625 0.693548
191 CYS THR GLU LEU LYS LEU SER ASP TYR 0.406015 0.783333
192 TRP GLU GLU LEU 0.405405 0.639344
193 ILE ARG LYS ILE LEU PHE LEU ASP GLY ILE 0.404255 0.830508
194 ALA ARG THR MLY GLN 0.403509 0.738462
195 PHE GLU ALA ILE PRO ALA GLU TYR LEU 0.402778 0.652174
196 ARG PRO GLY ASN PHE LEU GLN SER ARG LEU 0.402597 0.671233
197 LYS ARG LYS 0.402062 0.714286
198 THR ASN GLU PHE ALA PHE 0.401786 0.631579
199 ALA LYS ARG HIS ARG LYS VAL LEU ARG ASP 0.401515 0.777778
200 TYR PRO LYS ARG ILE ALA 0.40146 0.75
201 SER SER TYR ARG ARG PRO VAL GLY ILE 0.401361 0.736111
202 ACE ASP ALA ASP GLU FTY LEU NH2 0.4 0.625
203 ALA ASN SER ARG TRP PRO THR THR ARG LEU 0.4 0.69863
204 THR GLU ASP ASN ASP ASP ASP LEU TYR GLY 0.4 0.781818
Similar Binding Sites (Proteins are less than 50% similar to leader)
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