Receptor
PDB id Resolution Class Description Source Keywords
1FO0 2.5 Å EC: 3.-.-.- MURINE ALLOREACTIVE SCFV TCR-PEPTIDE-MHC CLASS I MOLECULE CO MUS MUSCULUS T CELL RECEPTOR CLASS I MHC H-2KB TCR-PMHC COMPLEX IMMUN
Ref.: CRYSTAL STRUCTURE OF A T CELL RECEPTOR BOUND TO AN ALLOGENEIC MHC MOLECULE. NAT.IMMUNOL. V. 1 291 2000
Ligand
Ligand Chain:Residue Validity Ligand Warnings Binding Data NGL Viewer Molecular Weight (Da) Formula SMILES
ILE ASN PHE ASP PHE ASN THR ILE P:1;
Valid;
none;
Kd = 2.6 uM
982.082 n/a O=C([...
View in 3D viewer
90% Homology Family
Leader
PDB id Resolution Class Description Source Keywords
1FO0 2.5 Å EC: 3.-.-.- MURINE ALLOREACTIVE SCFV TCR-PEPTIDE-MHC CLASS I MOLECULE CO MUS MUSCULUS T CELL RECEPTOR CLASS I MHC H-2KB TCR-PMHC COMPLEX IMMUN
Ref.: CRYSTAL STRUCTURE OF A T CELL RECEPTOR BOUND TO AN ALLOGENEIC MHC MOLECULE. NAT.IMMUNOL. V. 1 291 2000
Members (1)
No: PDB id Binding Data Representative ligand Formula Smiles
The Class containing this family consists of a total of 283 families.
1 1FO0 Kd = 2.6 uM ILE ASN PHE ASP PHE ASN THR ILE 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 235 families.
1 1FO0 Kd = 2.6 uM ILE ASN PHE ASP PHE ASN THR ILE 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 193 families.
1 1FO0 Kd = 2.6 uM ILE ASN PHE ASP PHE ASN THR ILE n/a n/a
Polypharmacology
Similar Ligands
Ligand no: 1; Ligand: ILE ASN PHE ASP PHE ASN THR ILE; Similar ligands found: 101
No: Ligand ECFP6 Tc MDL keys Tc
1 ILE ASN PHE ASP PHE ASN THR ILE 1 1
2 VAL ASN ASP ILE PHE GLU ALA ILE 0.62037 0.857143
3 TYR GLN GLU SER THR ASP PHE THR PHE LEU 0.610526 0.895833
4 SER LEU PHE ASN THR VAL ALA THR LEU 0.526316 0.823529
5 ASP PHE GLU GLU ILE 0.520408 0.77551
6 TRP ASN TRP PHE ASP ILE THR ASN LYS 0.519685 0.87037
7 THR PHE LYS LYS THR ASN 0.504762 0.777778
8 LEU GLY TYR GLY PHE VAL ASN TYR ILE 0.504202 0.833333
9 THR ASN GLU PHE TYR ALA 0.5 0.9
10 LEU LEU TYR GLY PHE VAL ASN TYR ILE 0.491803 0.833333
11 LYS VAL ILE THR PHE ILE ASP LEU 0.491525 0.796296
12 SER LEU PHE ASN THR ILE ALA VAL LEU 0.487805 0.843137
13 ARG ABA GLN ILE PHE ALA ASN ILE 0.487395 0.769231
14 ARG ABA PHE ILE PHE ALA ASN ILE 0.487395 0.724138
15 MET ASN TYR ASP ILE 0.483871 0.816327
16 MET PHE SER ILE ASP ASN ILE LEU ALA 0.483871 0.785714
17 ALA VAL TYR ASN PHE ALA THR MET 0.483333 0.803571
18 CYS THR PHE LYS THR LYS THR ASN 0.481818 0.763636
19 LYS ALA VAL PHE ASN PHE ALA THR MET 0.479675 0.775862
20 VAL VAL SER HIS PHE ASN ASP 0.478632 0.741379
21 GLU THR PHE TYR VAL ASP GLY 0.478261 0.8
22 CYS VAL ASN GLY SER CYS PHE THR VAL 0.475 0.777778
23 GLU THR LEU LEU ASP LEU ASP PHE ASP PRO 0.474576 0.671875
24 GLN PHE LYS ASP ASN VAL ILE LEU LEU 0.472441 0.777778
25 ILE THR ASP GLN VAL PRO PHE SER VAL 0.466667 0.651515
26 FME TYR PHE ILE ASN ILE LEU THR LEU 0.464567 0.839286
27 ARG ABA VAL ILE PHE ALA ASN ILE 0.463415 0.677966
28 LEU ASP GLU GLU THR GLY GLU PHE LEU 0.462185 0.777778
29 LYS MET ASN THR GLN PHE THR ALA VAL 0.460938 0.728814
30 GLU ILE ILE ASN PHE GLU LYS LEU 0.459016 0.727273
31 SER LEU TYR ASN THR ILE ALA THR LEU 0.458333 0.849057
32 SER LEU PHE ASN THR VAL ALA THR LEU TYR 0.456693 0.830189
33 GLU ASN LEU TYR PHE GLN 0.45614 0.846154
34 SER PHE PHE GLU ASP ASN PHE VAL PRO GLU 0.456 0.666667
35 ASP PHE M3L THR ASP 0.455357 0.693548
36 SER ILE ILE ASN PHE GLU LYS LEU 0.455285 0.781818
37 GLY ALA GLN THR PHE TYR VAL ASP GLY ALA 0.454545 0.8
38 ALA THR ARG ASN PHE SER GLY 0.453782 0.683333
39 ASN GLN LEU ALA TRP PHE ASP THR ASP LEU 0.452555 0.818182
40 LYS ALA VAL TYR ASN PHE ALA THR MET 0.450382 0.766667
41 SER TRP PHE GLN THR ASP LEU 0.450382 0.775862
42 LEU THR THR LYS LEU THR ASN THR ASN ILE 0.449541 0.777778
43 ALA GLU THR PHE 0.444444 0.833333
44 LYS ALA LEU TYR ASN PHE ALA THR MET 0.443609 0.766667
45 ALA PHE THR SER 0.443299 0.74
46 ILE LEU ALA LYS PHE LEU HIS THR LEU 0.442748 0.721311
47 ALA LEU TYR ASN THR ALA ALA ALA LEU 0.442478 0.86
48 PHE GLU ASP ASN PHE VAL PRO 0.439024 0.646154
49 ASP PHE GLU ASP TYR GLU PHE ASP 0.436364 0.773585
50 LYS GLN TRP ASP ASN TYR GLU PHE ILE TRP 0.435714 0.807018
51 THR LYS ASN TYR LYS GLN PHE SER VAL 0.434426 0.789474
52 ACE ASP ASP PTR VAL ASN VAL 0.432432 0.677966
53 THR GLU ASN LEU TYR PHE GLN SER GLY THR 0.431818 0.807018
54 GLU ASP GLU ASP PHE GLU ILE LEU SER LEU 0.429688 0.811321
55 LEU PRO PHE ASP LYS THR THR ILE MET 0.429577 0.614286
56 ACE ASN TRP GLU THR PHE 0.427419 0.818182
57 MET ASN TRP ASN ILE 0.427273 0.811321
58 GLU GLU TYR LEU GLN ALA PHE THR TYR 0.426357 0.846154
59 ASP PHE ALA ASN THR PHE LEU PRO 0.426357 0.71875
60 PHE ASN PHE PRO GLN ILE THR 0.426357 0.730159
61 GLY ILE LEU GLU PHE VAL PHE THR LEU 0.42623 0.846154
62 SER LEU TYR ASN THR VAL ALA THR LEU 0.42623 0.811321
63 ILE ASP TRP PHE ASP GLY LYS ASP 0.425373 0.7
64 GLY ALA GLU THR PHE TYR VAL ASP GLY ALA 0.425197 0.785714
65 LYS PRO ILE VAL GLN TYR ASP ASN PHE 0.424658 0.676471
66 LEU LEU TYR GLY PHE VAL ASN TYR VAL 0.424 0.814815
67 PHE GLU ALA ASN GLY ASN LEU ILE 0.424 0.792453
68 ALA ASN SER ARG PHE PRO THR SER ILE ILE 0.423611 0.619718
69 GLU GLU ASN LEU LEU ASP PHE VAL ARG PHE 0.421053 0.728814
70 ALA GLU THR PHE TYR VAL ASP GLY 0.420561 0.8
71 ILE ARG LYS ILE LEU PHE LEU ASP GLY ILE 0.42029 0.603175
72 ARG GLN ALA ASN PHE LEU GLY LYS 0.417391 0.735849
73 ARG GLN VAL ASN PHE LEU GLY LYS ILE ASN 0.417391 0.711538
74 THR LYS ASN TYR LYS GLN THR SER VAL 0.417323 0.741379
75 MET ASN GLU ASN ILE 0.416667 0.8125
76 PHE LEU THR GLY ILE GLY ILE ILE THR VAL 0.415254 0.843137
77 ILE GLY PRO GLY ARG ALA PHE TYR THR ILE 0.414474 0.625
78 ARG GLN PHE GLY PRO ASP PHE PRO THR ILE 0.414474 0.647887
79 ACE PHE HIS THR ABA NH2 0.414414 0.763636
80 ILE MET ASP GLN VAL PRO PHE SER VAL 0.412587 0.6
81 SER LEU TYR ASN VAL VAL ALA THR LEU 0.41129 0.811321
82 ARG PRO GLY ASN PHE PHE GLN ASN ARG PRO 0.410714 0.754717
83 ILE ASP TRP PHE ASP GLY LYS GLU 0.410072 0.7
84 LEU PRO PHE ASP LYS SER THR ILE MET 0.409396 0.605634
85 PHE GLN PRO GLN ASN GLY GLN PHE ILE 0.408759 0.646154
86 GLU ASP GLU ASP PHE GLU ILE LEU SEP LEU 0.408759 0.666667
87 SER ALA ASN SER PHE THR LEU ILE GLY GLU 0.408333 0.792453
88 THR ASN GLU PHE TYR PHE 0.407407 0.82
89 SER PRO ILE VAL PRO SER PHE ASP MET 0.407143 0.605634
90 LYS VAL LEU PHE LEU ASP GLY 0.40678 0.672727
91 GLY ILE LEU GLY LEU VAL PHE THR LEU 0.406504 0.807692
92 SER SER LEU GLU ASN PHE ALA ALA TYR VAL 0.406015 0.851852
93 VAL SER PHE ASN FRD PRO GLN ILE THR ALA 0.405594 0.671642
94 ARG GLN ALA ASN PHE LEU GLY LYS ILE ASN 0.405405 0.711538
95 ACE ASP LEU GLN THR SER ILE 0.405405 0.754717
96 ACE SER LEU ASN PHE 0.403846 0.788462
97 GLY ILE ILE ASN THR LEU 0.401961 0.803922
98 GLU THR LEU GLU ASP SER VAL PHE 0.401961 0.764706
99 TYR LEU GLY GLY PRO ASP PHE PRO THR ILE 0.4 0.676471
100 CYS THR GLU LEU LYS LEU ASN ASP TYR 0.4 0.77193
101 ILE ASP TRP PHE GLU GLY LYS GLU 0.4 0.672131
Similar Binding Sites (Proteins are less than 50% similar to leader)
Pocket No.: 1; Query (leader) PDB : 1FO0; Ligand: ILE ASN PHE ASP PHE ASN THR ILE; 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: 1fo0.bio1) has 36 residues
No: Leader PDB Ligand Sequence Similarity
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