Receptor
PDB id Resolution Class Description Source Keywords
1L6O 2.2 Å NON-ENZYME: TRANSCRIPT_TRANSLATE XENOPUS DISHEVELLED PDZ DOMAIN XENOPUS LAEVIS DISHEVELLED WNT PATHWAY PDZ MOLECULAR RECOGNITION GENE REGULATION
Ref.: DAPPER, A DISHEVELLED-ASSOCIATED ANTAGONIST OF BETA-CATENIN AND JNK SIGNALING, IS REQUIRED FOR NOTOCHORD FORMATION DEV.CELL V. 2 449 2002
Ligand
Ligand Chain:Residue Validity Ligand Warnings Binding Data NGL Viewer Molecular Weight (Da) Formula SMILES
SER LEU LYS LEU MET THR THR VAL D:1;
E:1;
F:1;
 Valid;
Valid;
Valid;
 none;
none;
none;
 submit data
893.138 n/a S(CCC...
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90% Homology Family
Leader
PDB id Resolution Class Description Source Keywords
1L6O 2.2 Å NON-ENZYME: TRANSCRIPT_TRANSLATE XENOPUS DISHEVELLED PDZ DOMAIN XENOPUS LAEVIS DISHEVELLED WNT PATHWAY PDZ MOLECULAR RECOGNITION GENE REGULATION
Ref.: DAPPER, A DISHEVELLED-ASSOCIATED ANTAGONIST OF BETA-CATENIN AND JNK SIGNALING, IS REQUIRED FOR NOTOCHORD FORMATION DEV.CELL V. 2 449 2002
Members (1)
No: PDB id Binding Data Representative ligand Formula Smiles
The Class containing this family consists of a total of 308 families.
1 1L6O - SER LEU LYS LEU MET THR THR 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 266 families.
1 1L6O - SER LEU LYS LEU MET THR THR 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 220 families.
1 1L6O - SER LEU LYS LEU MET THR THR VAL n/a n/a
Polypharmacology
Similar Ligands (2D)
Ligand no: 1; Ligand: SER LEU LYS LEU MET THR THR VAL; Similar ligands found: 88
No: Ligand ECFP6 Tc MDL keys Tc
1 SER LEU LYS LEU MET THR THR VAL 1 1
2 LEU LYS THR LYS LEU LEU 0.588889 0.862745
3 SER LEU LYS ILE ASP ASN MET ASP 0.572727 0.907407
4 SER LEU LEU LYS LYS LEU LEU ASP 0.566667 0.865385
5 LYS THR LYS LEU LEU 0.566667 0.862745
6 SER LEU LEU LYS LYS LEU LEU LEU ALA 0.551724 0.843137
7 CYS LEU GLY GLY LEU LEU THR MET VAL 0.54717 0.923077
8 LYS LEU VAL GLN LEU LEU THR THR THR 0.54 0.882353
9 ILE LEU ASN ALA MET ILE THR LYS ILE 0.535714 0.924528
10 LEU THR THR LYS LEU THR ASN THR ASN ILE 0.514563 0.833333
11 MET ABA LEU ARG MET THR ALA VAL MET 0.508621 0.810345
12 ASN LEU VAL PRW MET VAL ALA THR VAL 0.504348 0.886792
13 ACE VAL LYS GLU SER LEU VAL 0.5 0.862745
14 MET CYS LEU ARG MET THR ALA VAL MET 0.495798 0.842105
15 SER LEU LYS ILE ASP ASN LEU ASP 0.490909 0.833333
16 ASN ARG LEU MET LEU THR GLY 0.490741 0.827586
17 THR LYS CYS VAL VAL MET 0.49 0.98
18 ILE LEU ASN ALA MET ILE VAL LYS ILE 0.486957 0.849057
19 ILE LEU ASN ALA MET ILE ALA LYS ILE 0.486486 0.849057
20 ALA LEU LYS ILE ASP ASN MET ASP 0.482456 0.851852
21 GLU ALA THR GLN LEU MET ASN 0.477064 0.882353
22 GLY SER LYS MET GLU GLU VAL ASP 0.476636 0.924528
23 HIS LYS LEU VAL GLN LEU LEU THR THR THR 0.474576 0.725806
24 SER GLN LEU LYS ASN ASN ALA LYS GLU ILE 0.473684 0.818182
25 SER LEU LEU LYS LYS LEU LEU LEU ALA PRO 0.471154 0.671875
26 SER ASP LYS ILE ASP ASN LEU ASP 0.468468 0.833333
27 ACE CSO ARG ALA THR LYS MET LEU 0.466667 0.753846
28 LYS MET LYS 0.465909 0.803922
29 ARG LEU GLN ARG ARG ARG GLU THR GLN VAL 0.464286 0.758621
30 MET CYS LEU ARG NLE THR ALA VAL MET 0.459677 0.827586
31 ASN LEU VAL PRO MET VAL ALA THR VAL 0.456 0.75
32 SER LEU LEU MET TRP ILE THR GLN LEU 0.453846 0.761905
33 SER LEU LYS ILE ASP ASN GLU ASP 0.452991 0.833333
34 LYS SER LEU LEU GLN GLN LEU LEU THR GLU 0.451327 0.884615
35 SER LEU LEU MET TRP ILE THR GLN SER 0.450382 0.761905
36 SER LEU ALA ASN THR VAL ALA THR LEU 0.448598 0.788462
37 LYS LEU LYS 0.448276 0.764706
38 SER LEU LEU MET TRP ILE THR GLN ALA 0.44697 0.761905
39 GLU LEU LYS ARG LYS MET ILE TYR MET 0.44697 0.692308
40 LYS MET ASN THR GLN PHE THR ALA VAL 0.445312 0.875
41 GLU LEU ARG ARG LYS MET MET TYR MET 0.443548 0.71875
42 SER LEU LEU MET TRP ILE THR GLN CYS 0.440298 0.761905
43 CYS THR GLU LEU LYS LEU SER ASP TYR 0.436508 0.824561
44 ALA ILE PHE GLN SER SER MET THR LYS 0.436508 0.875
45 SER ARG MET GLU GLU VAL ASP 0.432432 0.903846
46 SER ALA LYS ILE ASP ASN LEU ASP 0.432203 0.833333
47 ARG ARG ALA THR LYS MET NH2 0.429825 0.824561
48 SER GLU LEU GLU ILE LYS ARG TYR 0.429688 0.692308
49 SER ARG LYS ILE ASP ASN LEU ASP 0.427419 0.737705
50 GLN ILE LYS VAL ARG VAL ASP MET VAL 0.427419 0.745763
51 LYS THR LYS 0.426966 0.803922
52 SER LEU TYR LEU THR VAL ALA THR LEU 0.426087 0.732143
53 SER LEU ASN TYR ILE ILE LYS VAL LYS GLU 0.424242 0.766667
54 LYS CYS VAL VAL MET 0.424242 0.88
55 LEU PRO PHE GLU LYS SER THR VAL MET 0.422535 0.757576
56 ALA THR LYS ILE ASP ASN LEU ASP 0.422414 0.833333
57 ILE LEU MET GLU HIS ILE HIS LYS LEU 0.421875 0.671875
58 ASP LEU LYS ILE ASP ASN LEU ASP 0.421053 0.777778
59 THR LYS CYS VAL PHE MET 0.418803 0.924528
60 GLU LEU ASN ARG LYS MET ILE TYR MET 0.41844 0.712121
61 CYS THR GLU LEU LYS LEU ASN ASP TYR 0.417323 0.793103
62 ALA SER ASN GLU ASN MET GLU THR MET 0.416667 0.886792
63 SER LEU LEU MET TRP ILE THR GLN VAL 0.416058 0.746032
64 ALA LEU GLY ILE GLY ILE LEU THR VAL 0.415094 0.773585
65 VAL THR THR ASP ILE GLN VAL LYS VAL 0.413793 0.865385
66 ALA ALA GLY ILE GLY ILE LEU THR VAL 0.412844 0.773585
67 ASN SER THR LEU GLN 0.411765 0.807692
68 GLN ARG ALA THR LYS MET NH2 0.411765 0.793103
69 PHE LEU SER THR LYS 0.410714 0.849057
70 ACE MET LEU SER VAL GLU GLU GLU GLY 0.409091 0.867925
71 THR SER ARG HIS LYS ALY LEU MET ALA 0.408759 0.746269
72 THR LYS THR ALA THR ILE ASN ALA SER 0.408696 0.849057
73 ALA MET TYR LYS 0.40566 0.785714
74 LEU ALA GLY ILE GLY ILE LEU THR VAL 0.405405 0.773585
75 ALA LEU ALA GLY ILE GLY ILE LEU THR VAL 0.405405 0.773585
76 LYS LYS LYS ALA 0.404494 0.705882
77 ALA ARG LYS LEU ASP 0.403846 0.689655
78 LYS LEU VAL VAL VAL ALA VAL GLY VAL 0.40367 0.764706
79 LEU PRO PRO PRO GLU SER GLU SER LYS VAL 0.40367 0.758621
80 ALA LEU LYS ILE ASP ASN LEU ASP 0.403509 0.777778
81 ARG ARG ARG TRP ARG ARG LEU THR VAL 0.403101 0.647059
82 ALA THR ILE GLY THR ALA MET TYR LYS 0.402985 0.827586
83 ALA SER ASN GLU ASP MET GLU THR MET 0.401786 0.886792
84 GLU LEU ALA GLY ILE GLY ILE LEU THR VAL 0.401709 0.792453
85 LYS SER LYS THR CMT GER 0.401709 0.925926
86 ASN LEU LEU GLN LYS LYS 0.4 0.735849
87 LYS PRO VAL LEU ARG THR ALA 0.4 0.637681
88 GLY THR LEU SER ASN ARG ALA SER LYS LEU 0.4 0.88
Similar Ligands (3D)
Ligand no: 1; Ligand: SER LEU LYS LEU MET THR THR 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 : 1L6O; Ligand: SER LEU LYS LEU MET THR THR 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: 1l6o.bio1) has 19 residues
No: Leader PDB Ligand Sequence Similarity
Pocket No.: 2; Query (leader) PDB : 1L6O; Ligand: SER LEU LYS LEU MET THR THR VAL; Similar sites found with APoc: 1
This union binding pocket(no: 2) in the query (biounit: 1l6o.bio1) has 21 residues
No: Leader PDB Ligand Sequence Similarity
1 6RQP OLC None
Pocket No.: 3; Query (leader) PDB : 1L6O; Ligand: SER LEU LYS LEU MET THR THR VAL; Similar sites found with APoc: No similar binding sites found, or similarity not calculated due to duplicate pocket.
This union binding pocket(no: 3) in the query (biounit: 1l6o.bio1) has 26 residues
No: Leader PDB Ligand Sequence Similarity
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