Receptor
PDB id Resolution Class Description Source Keywords
2PIE 1.35 Å EC: 6.3.2.- CRYSTAL STRUCTURE OF THE FHA DOMAIN OF RNF8 IN COMPLEX WITH OPTIMAL PHOSPHOPEPTIDE HOMO SAPIENS FHA DOMAIN PHOSPHOPEPTIDE COMPLEX LIGASE SIGNALING PROTE
Ref.: RNF8 TRANSDUCES THE DNA-DAMAGE SIGNAL VIA HISTONE UBIQUITYLATION AND CHECKPOINT PROTEIN ASSEMBLY. CELL(CAMBRIDGE,MASS.) V. 131 901 2007
Ligand
Ligand Chain:Residue Validity Ligand Warnings Binding Data NGL Viewer Molecular Weight (Da) Formula SMILES
GLU LEU LYS TPO GLU ARG TYR F:1;
 Valid;
 none;
 submit data
1016.01 n/a P(=O)...
View in 3D viewer
90% Homology Family
Leader
PDB id Resolution Class Description Source Keywords
2PIE 1.35 Å EC: 6.3.2.- CRYSTAL STRUCTURE OF THE FHA DOMAIN OF RNF8 IN COMPLEX WITH OPTIMAL PHOSPHOPEPTIDE HOMO SAPIENS FHA DOMAIN PHOSPHOPEPTIDE COMPLEX LIGASE SIGNALING PROTE
Ref.: RNF8 TRANSDUCES THE DNA-DAMAGE SIGNAL VIA HISTONE UBIQUITYLATION AND CHECKPOINT PROTEIN ASSEMBLY. CELL(CAMBRIDGE,MASS.) V. 131 901 2007
Members (1)
No: PDB id Binding Data Representative ligand Formula Smiles
The Class containing this family consists of a total of 41 families.
1 2PIE - GLU LEU LYS TPO GLU ARG TYR 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 27 families.
1 2PIE - GLU LEU LYS TPO GLU ARG TYR 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 21 families.
1 2PIE - GLU LEU LYS TPO GLU ARG TYR n/a n/a
Polypharmacology
Similar Ligands (2D)
Ligand no: 1; Ligand: GLU LEU LYS TPO GLU ARG TYR; Similar ligands found: 126
No: Ligand ECFP6 Tc MDL keys Tc
1 GLU LEU LYS TPO GLU ARG TYR 1 1
2 SER GLU LEU GLU ILE LYS ARG TYR 0.708661 0.838235
3 GLU LEU ARG ARG LYS MET MET TYR MET 0.664062 0.811594
4 GLU LEU LYS ARG LYS MET ILE TYR MET 0.654412 0.785714
5 GLU LEU ASN ARG LYS MET ILE TYR MET 0.613793 0.777778
6 LEU GLU LYS ALA ARG GLY SER THR TYR 0.59589 0.852941
7 TYR GLU LEU ASP GLU LYS PHE ASP ARG LEU 0.578571 0.850746
8 ARG ARG ILE TYR ASP LEU ILE GLU LEU 0.571429 0.848485
9 ASP GLU LEU GLU ILE LYS ALA TYR 0.57037 0.757576
10 CYS THR GLU LEU LYS LEU ASN ASP TYR 0.562044 0.75
11 ALA ARG THR GLU LEU TYR ARG SER LEU 0.557971 0.850746
12 SER SER ARG LYS GLU TYR TYR ALA 0.554688 0.791045
13 CYS THR GLU LEU LYS LEU SER ASP TYR 0.546763 0.75
14 GLU GLU ASN LEU LEU ASP PHE VAL ARG PHE 0.545455 0.73913
15 ALA ARG TPO LYS 0.533333 0.846154
16 GLU LEU ASP LYS TYR ALA SER 0.529851 0.772727
17 ARG ARG GLU VAL HIS THR TYR TYR 0.527027 0.756757
18 LEU TYR LEU VAL CYS GLY GLU ARG VAL 0.52027 0.779412
19 LEU TYR LEU VAL CYS GLY GLU ARG GLY PHE 0.519737 0.757143
20 PHE GLU ASP LEU ARG VAL LEU SER PHE 0.517241 0.753623
21 PHE GLU ASP LEU ARG VAL SER SER PHE 0.517241 0.753623
22 GLY GLY LYS LYS ARG TYR LYS LEU 0.514925 0.833333
23 GLY GLY ARG LYS LYS TYR LYS LEU 0.514925 0.833333
24 GLY GLY LYS LYS LYS TYR ARG LEU 0.514925 0.833333
25 ARG LEU GLN ARG ARG ARG GLU THR GLN VAL 0.51145 0.772727
26 PHE GLU ASP LEU ARG LEU LEU SER PHE 0.510791 0.753623
27 SER LEU ARG PHE LEU TYR GLU GLY 0.510638 0.785714
28 LEU TYR LEU VAL CYS GLY GLU ARG GLY 0.506757 0.779412
29 ARG ARG LEU LEU ARG GLY HIS ASN GLN TYR 0.506579 0.756757
30 ARG HIS ARG MLZ VAL LEU ARG ASP ASN TYR 0.50625 0.74026
31 ARG HIS ARG MLY VAL LEU ARG ASP TYR 0.503226 0.74359
32 GLU GLU TYR LEU GLN ALA PHE THR TYR 0.5 0.676471
33 ALA ARG THR MLY GLN THR ALA ARG TYR 0.496504 0.819444
34 GLU GLU TYR LEU LYS ALA TRP THR PHE 0.493827 0.689189
35 GLU ALA GLN THR ARG LEU 0.488722 0.742424
36 VAL LYS VAL VAL ALA LYS LYS TYR ARG ASN 0.485294 0.820895
37 ASN ALA LEU LEU ARG TYR LEU LEU ASP 0.482014 0.820895
38 GLU LEU ARG SER ARG TYR TRP ALA ILE 0.481481 0.75
39 GLY ALA ALA ARG ALA GLU VAL TYR LEU ARG 0.480263 0.833333
40 PTR LEU ARG VAL ALA 0.477941 0.907692
41 PHE LEU ARG GLY ARG ALA TYR GLY LEU 0.472603 0.794118
42 GLU ARG GLU SEP GLU PHE ASP ILE GLU ASP 0.470968 0.865672
43 PHE LEU ARG GLY ARG ALA TYR VAL LEU 0.470588 0.794118
44 SER LEU ASN TYR ILE ILE LYS VAL LYS GLU 0.470199 0.753623
45 GLN TYR PHE MET TPO GLU PTR VAL ALA 0.469136 0.780822
46 PHE TYR ARG ALA LEU MET 0.468966 0.732394
47 GLU GLN TYR LYS PHE TYR SER VAL 0.468085 0.724638
48 SER ASP TYR GLN ARG LEU 0.466165 0.830769
49 ACE ALA ARG THR GLU VAL TYR NH2 0.464286 0.818182
50 SER GLU ILE GLU PHE ALA ARG LEU 0.462585 0.75
51 THR ASN GLU TYR LYS VAL 0.462121 0.716418
52 ARG GLY TYR LEU TYR GLN GLY LEU 0.461538 0.779412
53 PHE ARG TYR LEU GLY 0.459854 0.779412
54 GLU GLU PHE GLY ARG ALA PHE SER PHE 0.459459 0.685714
55 GLN SER TYR TPO VAL 0.458647 0.820895
56 GLU GLU PRO THR VAL ILE LYS LYS TYR 0.45625 0.675325
57 TYR PRO LYS ARG ILE ALA 0.453947 0.710526
58 ALA ARG LYS LEU ASP 0.451613 0.738462
59 ALA ALA SER LEU TYR GLU LYS LYS ALA ALA 0.450704 0.761194
60 SER SER LEU GLU ASN PHE ARG ALA TYR VAL 0.450617 0.8
61 PHE LEU GLU LYS 0.448819 0.661538
62 GLU ASN GLN LYS GLU TYR PHE PHE 0.448529 0.666667
63 ARG VAL ALA GLN LEU GLU GLN VAL TYR ILE 0.447368 0.80303
64 THR ARG ARG GLU THR GLN LEU 0.44697 0.772727
65 TYR ALA GLY SEP TPO ASP GLU ASN 0.445161 0.785714
66 SER SER ILE GLU PHE ALA ARG LEU 0.443709 0.764706
67 LYS LYS ALA THR GLN ALA SEP GLN GLU TYR 0.44186 0.80303
68 TYR GLN SER LYS LEU 0.439394 0.746269
69 GLU ILE ILE ASN PHE GLU LYS LEU 0.438356 0.661765
70 ASP SEP TYR GLU VAL LEU ASP LEU 0.437909 0.833333
71 GLU LEU GLU LYS TRP ALA SER 0.436242 0.643836
72 ARG GLY TYR VAL TYR GLN GLY LEU 0.436242 0.779412
73 GLU LEU ASP 1OL VAL GLU PHE 0.435374 0.661538
74 GLU ASP GLU ASP PHE GLU ILE LEU SEP LEU 0.433121 0.761194
75 SER ARG ILE ARG ILE ARG GLY TYR VAL ARG 0.432432 0.826087
76 GLY HIS LYS ILE LEU HIS ARG LEU LEU GLN 0.431373 0.675676
77 LYS ARG ARG LYS SEP VAL 0.430769 0.833333
78 GLN VAL PRO LEU ARG PRO MET THR TYR LYS 0.430168 0.7375
79 HIS LYS ILE LEU HIS ARG LEU LEU GLN ASP 0.428571 0.69863
80 LYS ILE LEU HIS ARG LEU LEU GLN ASP 0.427673 0.708333
81 SER ARG LYS ILE ASP ASN LEU ASP 0.425676 0.753623
82 ILE ARG LYS ILE LEU PHE LEU ASP GLY ILE 0.425 0.75
83 GLU ASN LEU TYR PHE GLN 0.42446 0.652174
84 GLY GLY LYS LYS LYS TYR GLN LEU 0.42446 0.742424
85 VAL LEU ARG ASP ASP LEU LEU GLU ALA 0.424242 0.738462
86 HIS LYS ILE LEU HIS ARG LEU LEU GLN GLU 0.423313 0.684932
87 PHQ LEU VAL ARG TYR 0.42069 0.782609
88 PHE LEU ALA TYR LYS 0.42029 0.701493
89 GLU THR VAL ARG PHE GLN SER ASP 0.418301 0.761194
90 ARG PRO MET THR TYR LYS GLY ALA LEU 0.418079 0.716049
91 GLY GLY LYS LYS LYS TYR LYS LEU 0.41791 0.742424
92 ALA ARG LYS ILE ASP ASN LEU ASP 0.417808 0.735294
93 ACE GLU ALA GLN THR ARG LEU 0.417266 0.731343
94 PRO LEU GLU PSA ARG LEU 0.416667 0.760563
95 ARG THR TYR SEP GLY PRO MET ASN LYS VAL 0.416216 0.792683
96 ALA VAL TYR ASP GLY ARG GLU HIS THR VAL 0.415663 0.756757
97 ILE LEU GLY LYS PHE LEU HIS ARG LEU 0.415094 0.689189
98 LEU ARG ASN GLN SER VAL PHE ASN PHE 0.414474 0.757143
99 ASP PHE GLU LYS GLU GLY TYR SER LEU 0.414013 0.742857
100 SER ILE ILE GLY PHE GLU LYS LEU 0.413333 0.666667
101 GLY VAL TYR ASP GLY ARG GLU HIS THR VAL 0.413174 0.756757
102 ARG TYR GLY PHE VAL ALA ASN PHE 0.412903 0.757143
103 PRO GLU SEP LEU GLU SER CYS PHE 0.412587 0.764706
104 VAL PRO LEU ARG PRO MET THR TYR 0.412121 0.725
105 ASP ALA ASP GLU TYR LEU 0.411765 0.692308
106 GLY ASP GLU VAL LYS VAL PHE ARG 0.411765 0.757576
107 PHE LEU SER TYR LYS 0.410072 0.710145
108 ALA GLN ASP ILE TYR ARG ALA SER TYR 0.409938 0.785714
109 DTY ILE ARG LEU LPD 0.409396 0.697368
110 ARG ARG ARG GLU THR GLN VAL 0.409091 0.757576
111 ALA ARG THR M3L GLN THR ALA ALA LYS ALA 0.408163 0.739726
112 GLU GLU GLU ASP GLY TPO MET LYS ARG ASN 0.407895 0.814286
113 TYR HIS SEP VAL VAL ARG TYR ALA 0.407407 0.824324
114 ACE LYS ARG ARG LYS SEP VAL 0.407407 0.833333
115 LYS ILE LEU HIS ARG LEU LEU GLN ASP SER 0.407186 0.726027
116 LYS MET ASP SEP PHE LEU ASP MET GLN LEU 0.40625 0.8
117 2UE DLY LYS DAR 0.406015 0.712121
118 ARG ARG LEU ILE PHE NH2 0.405797 0.69697
119 ASP ALA GLU PHE ARG HIS ASP 0.405594 0.723077
120 HIS MET THR GLU VAL VAL ARG ARG CYS 0.405063 0.710526
121 ARG LYS LYS ARG TYR THR VAL VAL GLY ASN 0.405063 0.823529
122 SEP GLN GLU TYR NH2 0.40458 0.787879
123 GLN ARG SER THR SEP THR 0.404255 0.820895
124 ARG PHE MET ASP TYR TRP GLU GLY LEU 0.403409 0.692308
125 LYS ARG LYS 0.403361 0.646154
126 ALA THR ALA ALA ALA THR GLU ALA TYR 0.402985 0.666667
Similar Ligands (3D)
Ligand no: 1; Ligand: GLU LEU LYS TPO GLU ARG TYR; 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 : 2PIE; Ligand: GLU LEU LYS TPO GLU 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: 2pie.bio1) has 11 residues
No: Leader PDB Ligand Sequence Similarity
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