Receptor
PDB id Resolution Class Description Source Keywords
4WYU 2.5 Å NON-ENZYME: OTHER CRYSTAL STRUCTURE OF SCRIBBLE PDZ34 TANDEM IN COMPLEX WITH I PEPTIDE HOMO SAPIENS PDZ TANDEM PBM STRUCTURAL PROTEIN-PEPTIDE COMPLEX
Ref.: INTERDOMAIN INTERFACE-MEDIATED TARGET RECOGNITION B SCRIBBLE PDZ34 SUPRAMODULE. BIOCHEM.J. V. 468 133 2015
Ligand
Ligand Chain:Residue Validity Ligand Warnings Binding Data NGL Viewer Molecular Weight (Da) Formula SMILES
IOD B:303;
A:301;
A:302;
B:304;
A:303;
B:301;
B:302;
Invalid;
Invalid;
Invalid;
Invalid;
Invalid;
Invalid;
Invalid;
none;
none;
none;
none;
none;
none;
none;
submit data
126.904 I [I-]
SER TRP PHE GLN THR ASP LEU C:-6;
D:-6;
Valid;
Valid;
none;
none;
Kd = 7.3 uM
894.96 n/a O=C([...
View in 3D viewer
90% Homology Family
Leader
PDB id Resolution Class Description Source Keywords
4WYU 2.5 Å NON-ENZYME: OTHER CRYSTAL STRUCTURE OF SCRIBBLE PDZ34 TANDEM IN COMPLEX WITH I PEPTIDE HOMO SAPIENS PDZ TANDEM PBM STRUCTURAL PROTEIN-PEPTIDE COMPLEX
Ref.: INTERDOMAIN INTERFACE-MEDIATED TARGET RECOGNITION B SCRIBBLE PDZ34 SUPRAMODULE. BIOCHEM.J. V. 468 133 2015
Members (1)
No: PDB id Binding Data Representative ligand Formula Smiles
The Class containing this family consists of a total of 1579 families.
1 4WYU Kd = 7.3 uM SER TRP PHE GLN THR ASP 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 1312 families.
1 4WYU Kd = 7.3 uM SER TRP PHE GLN THR ASP 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 1130 families.
1 4WYU Kd = 7.3 uM SER TRP PHE GLN THR ASP LEU n/a n/a
Polypharmacology
Similar Ligands
Ligand no: 1; Ligand: SER TRP PHE GLN THR ASP LEU; Similar ligands found: 174
No: Ligand ECFP6 Tc MDL keys Tc
1 SER TRP PHE GLN THR ASP LEU 1 1
2 ASN GLN LEU ALA TRP PHE ASP THR ASP LEU 0.75 0.946429
3 SER VAL TYR ASP PHE PHE VAL TRP LEU 0.71875 0.948276
4 ACE ASN TRP GLU THR PHE 0.645669 0.87931
5 ALA ASN SER ARG TRP GLN ASP THR ARG LEU 0.643357 0.833333
6 SER LEU LEU MET TRP ILE THR GLN LEU 0.639706 0.887097
7 TRP ASN TRP PHE ASP ILE THR ASN LYS 0.607143 0.864407
8 SER LEU LEU MET TRP ILE THR GLN SER 0.6 0.887097
9 SER LEU LEU MET TRP ILE THR GLN CYS 0.598592 0.887097
10 PRO ALA TRP ASP GLU THR ASN LEU 0.586207 0.870968
11 SER LEU LEU MET TRP ILE THR GLN ALA 0.584507 0.887097
12 TYR TYR GLU SER ASP TRP LEU 0.57971 0.948276
13 SER SER VAL VAL GLY VAL TRP TYR LEU 0.578571 0.932203
14 GLU GLU TYR LEU LYS ALA TRP THR PHE 0.56129 0.870968
15 GLY ILE TRP GLY PHE VAL PHE THR LEU 0.555556 0.898305
16 SER SER VAL ILE GLY VAL TRP TYR LEU 0.554795 0.916667
17 TYR GLN GLU SER THR ASP PHE THR PHE LEU 0.554622 0.785714
18 ALA SER ASN GLU ASN TRP GLU THR MET 0.553957 0.870968
19 SER ARG TYR TRP ALA ILE ARG THR ARG 0.54902 0.794118
20 ARG PHE MET ASP TYR TRP GLU GLY LEU 0.54375 0.732394
21 GLU LEU ASP HOX TRP ALA SER 0.542253 0.931035
22 SER LEU LEU MET TRP ILE THR GLN VAL 0.540541 0.870968
23 THR SER THR LEU GLN GLU GLN ILE GLY TRP 0.54 0.916667
24 GLU ALA ASP LYS TRP GLN SER 0.539007 0.833333
25 LEU ASP GLU GLU THR GLY GLU PHE LEU 0.537313 0.779661
26 ASP GLU ASP LYS TRP ASP ASP PHE 0.533835 0.79661
27 LEU GLU LEU ASP LYS TRP ALA SER LEU 0.530612 0.915254
28 SER SER THR ARG GLY ILE SER GLN LEU TRP 0.528662 0.833333
29 ALA ASN SER ARG TRP GLN THR SER ILE ILE 0.525974 0.818182
30 GLU GLN ASP LYS TRP ALA SER 0.524476 0.833333
31 LYS GLN TRP ASP ASN TYR GLU PHE ILE TRP 0.522876 0.836066
32 ALA ASN SER ARG TRP GLN VAL THR ARG VAL 0.521127 0.830769
33 ILE ASP TRP PHE ASP GLY LYS GLU 0.52 0.819672
34 ILE ASP TRP PHE GLU GLY LYS GLU 0.52 0.790323
35 ILE ASP TRP PHE ASP GLY LYS ASP 0.517007 0.819672
36 ASP ASN ARG LEU GLY LEU VAL TYR TRP PHE 0.515625 0.793103
37 SER LEU PHE ASN THR VAL ALA THR LEU 0.514706 0.789474
38 GLU LEU ASP ORN TRP ALA SER 0.51049 0.913793
39 TRP GLU GLU LEU 0.508197 0.807018
40 ALA LEU ASP LYS TRP ASP 0.507463 0.847458
41 SER ILE ILE ASN PHE GLU LYS LEU 0.507143 0.754098
42 PHE GLN TRP MET GLY TYR GLU LEU TRP 0.506329 0.772727
43 ASP TRP GLU ILE VAL 0.503759 0.824561
44 ACE ASN PRO ASP TRP ASP PHE ASN NH2 0.503597 0.774194
45 THR SER ASN LEU GLN GLU GLN ILE GLY TRP 0.503226 0.901639
46 SER TRP PHE PRO 0.5 0.731343
47 ASP PHE GLN GLU SER ALA ASP SER PHE LEU 0.5 0.859649
48 LYS GLN TRP ASP ASN TYR GLU PTR ILE TRP 0.5 0.728571
49 GLU LEU ASP LYS TRP ALA SER 0.496552 0.898305
50 ALA LEU ASP LYS TRP ALA SER 0.496454 0.898305
51 SER GLN TYR TYR TYR ASN SER LEU 0.496124 0.847458
52 ARG ARG ARG TRP ARG ARG LEU THR VAL 0.493056 0.815385
53 LYS VAL PRO ARG ASN GLN ASP TRP LEU 0.491228 0.689189
54 GLU GLY PRO ARG ASN GLN ASP TRP LEU 0.491018 0.689189
55 TYR TYR GLU SER GLY TRP LEU 0.489796 0.9
56 SER ARG ARG TRP ARG ARG TRP ASN ARG 0.489051 0.772727
57 MET LEU TRP GLY TYR LEU GLN TYR VAL 0.487013 0.784615
58 GLY LEU MET TRP LEU SER TYR PHE VAL 0.486842 0.859375
59 THR GLY TYR GLU THR TRP VAL 0.486301 0.883333
60 GLY ALA GLN THR PHE TYR VAL ASP GLY ALA 0.485714 0.8
61 LYS VAL ILE THR PHE ILE ASP LEU 0.485714 0.766667
62 GLU LEU ASP NRG TRP ALA SER 0.483871 0.716216
63 GLU LEU ASP LYS TRP ALA ASN 0.482993 0.85
64 GLU GLU TYR LEU GLN ALA PHE THR TYR 0.479452 0.779661
65 LEU LEU GLU LEU ASP LYS TRP ALA NH2 0.479167 0.830508
66 GLN ALA SER GLN ASP VAL LYS ASN TRP 0.477419 0.868852
67 GLU LEU ASP HIS TRP ALA SER 0.47651 0.898305
68 GLU ASN ASP LYS TRP ALA SER 0.47619 0.85
69 ASP ASP TRP ASN TRP GLU VAL GLU ASP 0.474453 0.844828
70 TYR ASP GLN ILE LEU 0.472868 0.711864
71 ASP TRP ASN 0.467213 0.77193
72 GLU ASP ASN ASP TRP ASN 0.467213 0.77193
73 GLU LEU GLU LYS TRP ALA SER 0.465753 0.85
74 MET ASN TRP ASN ILE 0.465116 0.810345
75 ARG GLN PHE GLY PRO ASP TRP ILE VAL ALA 0.461538 0.675676
76 GLN GLU GLU TRP SEP THR VAL MET 0.461039 0.782609
77 PRO GLN PHE SER LEU TRP LYS ARG 0.460526 0.868852
78 ARG LEU TRP SER 0.459854 0.78125
79 SER PRO LEU ASP SER LEU TRP TRP ILE 0.458599 0.808824
80 GLU ILE ILE ASN PHE GLU LYS LEU 0.458333 0.677419
81 ASN ASP TRP LEU LEU PRO SER TYR 0.457831 0.8
82 SER LEU TYR ASN THR ILE ALA THR LEU 0.457746 0.783333
83 ALA ILE PHE GLN SER SER MET THR LYS 0.455782 0.707692
84 GLU LEU ASP LYS TRP ALA GLY 0.455782 0.816667
85 ALA ASN SER ARG TRP PRO THR THR ARG LEU 0.45509 0.743243
86 GLU LEU ARG SER ARG TYR TRP ALA ILE 0.454545 0.823529
87 VAL ASP SER LYS ASN THR SER SER TRP 0.453947 0.9
88 ARG PHE PRO LEU THR PHE GLY TRP 0.453488 0.739726
89 LYS MET ASP SEP PHE LEU ASP MET GLN LEU 0.451613 0.625
90 ASP ASN ARG LEU GLY LEU VAL TYR GLN PHE 0.451128 0.741379
91 GLY ILE LEU GLU PHE VAL PHE THR LEU 0.450704 0.810345
92 SER LEU TYR ASN THR VAL ALA THR LEU 0.450704 0.779661
93 ILE ASN PHE ASP PHE ASN THR ILE 0.450382 0.775862
94 GLN PHE LYS ASP ASN VAL ILE LEU LEU 0.450331 0.721311
95 GLN ALA SER GLN GLU VAL LYS ASN TRP 0.449367 0.868852
96 ARG ARG ARG TRP HIS ARG TRP ARG LEU 0.44898 0.742424
97 GLY SER HIS LEU GLU VAL GLN GLY TYR TRP 0.447674 0.859375
98 SER LEU TYR ASN VAL VAL ALA THR LEU 0.447552 0.779661
99 ILE THR ASP GLN VAL PRO PHE SER VAL 0.446541 0.761194
100 TYR GLU TRP 0.446154 0.775862
101 SER PHE PHE GLU ASP ASN PHE VAL PRO GLU 0.445946 0.776119
102 LEU PRO SER PHE GLU THR ALA LEU 0.444444 0.772727
103 ARG TYR PRO LEU THR PHE GLY TRP 0.44382 0.72
104 GLU ASP GLU ASP PHE GLU ILE LEU SER LEU 0.442953 0.810345
105 SER GLU ILE GLU PHE ALA ARG LEU 0.442953 0.692308
106 ALA LEU TRP GLY PHE PHE PRO VAL LEU 0.442424 0.731343
107 GLU ASP GLU ASP PHE GLU ILE LEU SEP LEU 0.442308 0.651515
108 VAL CYS TRP GLY GLU LEU MET ASN LEU 0.4375 0.796875
109 ARG PHE PRO LEU THR PHE GLY TRP CYS PHE 0.437158 0.743243
110 SER LEU PHE ASN THR VAL ALA THR LEU TYR 0.437086 0.79661
111 MET LEU ILE TYR SER MET TRP GLY LYS 0.436047 0.808824
112 ASN ASP LYS TYR GLU PRO PHE TRP GLU 0.435754 0.714286
113 PRO GLN PRO VAL ASP SER TRP VAL 0.435583 0.791045
114 THR GLU ASN LEU TYR PHE GLN SER GLY THR 0.435065 0.806452
115 TYR GLU LEU ASP GLU LYS PHE ASP ARG LEU 0.435065 0.691176
116 SER ASP TYR GLN ARG LEU 0.434783 0.666667
117 GLU ASN LEU TYR PHE GLN 0.434783 0.75
118 SER LEU TYR LEU THR VAL ALA THR LEU 0.434783 0.775862
119 ASP ALA ASP GLU TYR LEU 0.432836 0.741379
120 GLU THR PHE TYR VAL ASP GLY 0.432624 0.8
121 THR SER THR THR SER VAL ALA SER SER TRP 0.432624 0.928571
122 SER ILE ILE GLY PHE GLU LYS LEU 0.432432 0.737705
123 SER SER LEU GLU ASN PHE ALA ALA TYR VAL 0.431373 0.847458
124 ALA LEU TRP GLY PHE VAL PRO VAL LEU 0.431138 0.731343
125 GLY ALA GLU THR PHE TYR VAL ASP GLY ALA 0.42953 0.786885
126 ASP SER TRP LYS ASP GLY CYS TYR 0.428571 0.825397
127 ACE GLU TRP TRP TRP 0.428571 0.741379
128 ALA ASN SER ARG TRP ALY THR SER ILE ILE 0.428571 0.757143
129 SER HIS PHE ASN GLU TYR GLU 0.427632 0.822581
130 ARG ARG LYS TRP ARG ARG TRP HIS LEU 0.425806 0.731343
131 ALA LEU ASP LYS TRP GLN ASN 0.425532 0.830508
132 FME TYR PHE ILE ASN ILE LEU THR LEU 0.424837 0.75
133 SER SER ILE GLU PHE ALA ARG LEU 0.424837 0.707692
134 SER LEU PHE ASN THR ILE ALA VAL LEU 0.423841 0.775862
135 ASP PHE M3L THR ASP 0.423358 0.676471
136 CYS THR PHE LYS THR LYS THR ASN 0.423358 0.709677
137 ARG TYR PRO LEU THR LEU GLY TRP CYS PHE 0.42328 0.723684
138 TRP LEU PHE VAL GLN ARG ASP SER LYS GLU 0.423077 0.767857
139 THR LYS ASN TYR LYS GLN THR SER VAL 0.422819 0.746032
140 ALA GLU THR PHE 0.422764 0.732143
141 LYS ARG LYS SER ARG TRP ASP GLU THR PRO 0.422619 0.702703
142 LYS TRP LYS 0.421875 0.716667
143 MET GLU ASP TPO GLN MSE ILE ASP TRP ASP 0.419753 0.704225
144 GLU THR VAL ARG PHE GLN SER ASP 0.418301 0.703125
145 GLY SER ASP PRO TRP LYS 0.418301 0.746269
146 ASP PHE GLU ASP TYR GLU PHE ASP 0.41791 0.688525
147 THR PHE LYS LYS THR ASN 0.41791 0.721311
148 LEU GLU PHE GLN GLY 0.416667 0.677966
149 ACE PRO TRP ALA THR CYS ASP SER NH2 0.416149 0.757143
150 THR PRO TYR ASP ILE ASN GLN MET LEU 0.415663 0.675676
151 ARG ARG LYS TRP CIR ARG TRP HIS LEU 0.415094 0.720588
152 ALA ARG THR GLU LEU TYR ARG SER LEU 0.414474 0.716418
153 TRP GLU TYR ILE PRO ASN VAL 0.414201 0.732394
154 ASP PHE GLU GLU ILE 0.414062 0.655172
155 ACE ASP LEU GLN THR SER ILE 0.413534 0.758621
156 LYS MET ASN THR GLN PHE THR ALA VAL 0.412903 0.707692
157 ILE ARG TYR PRO LYS THR PHE GLY TRP 0.412698 0.697368
158 THR PRO ASP TYR PHE LEU 0.411765 0.806452
159 MET PHE SER ILE ASP ASN ILE LEU ALA 0.411765 0.758065
160 ACE PHE MET AIB PM3 TRP GLU 1AC LEU NH2 0.411429 0.680556
161 MET ASP TRP ASN MET HIS ALA ALA 0.411392 0.765625
162 LYS ALA LEU TYR ASN PHE ALA THR MET 0.408805 0.742424
163 THR LYS ASN TYR LYS GLN PHE SER VAL 0.408163 0.790323
164 GLU GLN TYR LYS PHE TYR SER VAL 0.408163 0.774194
165 SER GLU ASP GLU PHE TYR ASP ALA LEU SER 0.407895 0.830508
166 MET HIS PRO ALA GLN THR SER GLN TRP 0.407821 0.739726
167 ILE LEU ALA LYS PHE LEU HIS THR LEU 0.407643 0.809524
168 ARG TYR PRO LEU THR PHE GLY TRP CYS PHE 0.40625 0.710526
169 SER PTR VAL ASN VAL GLN ASN 0.405594 0.701493
170 VAL GLN GLN GLU SER SER PHE VAL MET 0.405594 0.754098
171 ILE SER PRO ARG THR LEU ASP ALA TRP 0.404372 0.743243
172 ARG ABA GLN ILE PHE ALA ASN ILE 0.402685 0.683333
173 PHE TYR ALA PRO GLU PRO ILE THR SER LEU 0.402367 0.760563
174 GLU THR LEU LEU ASP LEU ASP PHE ASP PRO 0.401361 0.757576
Similar Binding Sites (Proteins are less than 50% similar to leader)
Pocket No.: 1; Query (leader) PDB : 4WYU; Ligand: SER TRP PHE GLN THR ASP LEU; 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: 4wyu.bio2) has 19 residues
No: Leader PDB Ligand Sequence Similarity
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