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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)...
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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 36 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 24 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 19 families.
1 2PIE - GLU LEU LYS TPO GLU ARG TYR n/a n/a
Polypharmacology
Similar Ligands
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 SER SER ARG LYS GLU TYR TYR ALA 0.566929 0.791045
11 CYS THR GLU LEU LYS LEU ASN ASP TYR 0.562044 0.75
12 ALA ARG THR GLU LEU TYR ARG SER LEU 0.557971 0.850746
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 GLU LEU ASP LYS TYR ALA SER 0.529851 0.772727
16 LEU TYR LEU VAL CYS GLY GLU ARG VAL 0.52027 0.779412
17 LEU TYR LEU VAL CYS GLY GLU ARG GLY PHE 0.519737 0.757143
18 ALA ARG THR MLY GLN THR ALA ARG TYR 0.51773 0.819444
19 GLY GLY LYS LYS ARG TYR LYS LEU 0.514925 0.833333
20 GLY GLY LYS LYS LYS TYR ARG LEU 0.514925 0.833333
21 GLY GLY ARG LYS LYS TYR LYS LEU 0.514925 0.833333
22 ARG LEU GLN ARG ARG ARG GLU THR GLN VAL 0.51145 0.772727
23 SER LEU ARG PHE LEU TYR GLU GLY 0.510638 0.785714
24 LEU TYR LEU VAL CYS GLY GLU ARG GLY 0.506757 0.779412
25 ARG ARG LEU LEU ARG GLY HIS ASN GLN TYR 0.506579 0.756757
26 ARG HIS ARG MLZ VAL LEU ARG ASP ASN TYR 0.50625 0.74026
27 ARG HIS ARG MLY VAL LEU ARG ASP TYR 0.503226 0.74359
28 GLU GLU GLN GLU GLU TYR 0.5 0.615385
29 SER ASP TYR GLN ARG LEU 0.5 0.830769
30 GLU GLU TYR LEU GLN ALA PHE THR TYR 0.5 0.676471
31 GLU GLU TYR LEU LYS ALA TRP THR PHE 0.493827 0.689189
32 VAL LYS VAL VAL ALA LYS LYS TYR ARG ASN 0.492647 0.820895
33 THR ASN GLU TYR LYS VAL 0.492308 0.716418
34 GLU ALA GLN THR ARG LEU 0.488722 0.742424
35 ASN ALA LEU LEU ARG TYR LEU LEU ASP 0.482014 0.820895
36 GLU LEU ARG SER ARG TYR TRP ALA ILE 0.481481 0.75
37 GLY ALA ALA ARG ALA GLU VAL TYR LEU ARG 0.480263 0.833333
38 PTR LEU ARG VAL ALA 0.477941 0.907692
39 GLU ASN GLN LYS GLU TYR PHE PHE 0.477612 0.666667
40 PHE LEU ARG GLY ARG ALA TYR GLY LEU 0.472603 0.794118
41 GLU ARG GLU SEP GLU PHE ASP ILE GLU ASP 0.470968 0.865672
42 PHE LEU ARG GLY ARG ALA TYR VAL LEU 0.470588 0.794118
43 GLN TYR PHE MET TPO GLU PTR VAL ALA 0.469136 0.780822
44 PHE TYR ARG ALA LEU MET 0.468966 0.732394
45 GLU GLN TYR LYS PHE TYR SER VAL 0.468085 0.724638
46 ACE ALA ARG THR GLU VAL TYR NH2 0.464286 0.818182
47 SER GLU ILE GLU PHE ALA ARG LEU 0.462585 0.75
48 ARG GLY TYR LEU TYR GLN GLY LEU 0.461538 0.779412
49 LYS LYS ALA THR GLN ALA SEP GLN GLU TYR 0.460938 0.80303
50 PHE ARG TYR LEU GLY 0.459854 0.779412
51 GLU GLU PHE GLY ARG ALA PHE SER PHE 0.459459 0.685714
52 GLN SER TYR TPO VAL 0.458647 0.820895
53 GLU GLU PRO THR VAL ILE LYS LYS TYR 0.45625 0.675325
54 TYR PRO LYS ARG ILE ALA 0.453947 0.710526
55 ALA PRO ALA LEU ARG VAL VAL LYS 0.453125 0.707692
56 ALA ARG LYS LEU ASP 0.451613 0.738462
57 ALA ALA SER LEU TYR GLU LYS LYS ALA ALA 0.450704 0.761194
58 SER SER LEU GLU ASN PHE ARG ALA TYR VAL 0.450617 0.8
59 PRO GLU SEP LEU GLU SER CYS PHE 0.45 0.764706
60 GLU VAL ALA PRO PRO GLU TYR HIS ARG LYS 0.447514 0.708861
61 ARG VAL ALA GLN LEU GLU GLN VAL TYR ILE 0.447368 0.80303
62 THR ARG ARG GLU THR GLN LEU 0.44697 0.772727
63 TYR ALA GLY SEP TPO ASP GLU ASN 0.445161 0.785714
64 SER SER ILE GLU PHE ALA ARG LEU 0.443709 0.764706
65 HIS GLU GLU LEU ALA LYS LEU 0.442623 0.615385
66 TYR GLN SER LYS LEU 0.439394 0.746269
67 GLU ILE ILE ASN PHE GLU LYS LEU 0.438356 0.661765
68 ASP SEP TYR GLU VAL LEU ASP LEU 0.437909 0.833333
69 ARG GLY TYR VAL TYR GLN GLY LEU 0.436242 0.779412
70 GLU LEU GLU LYS TRP ALA SER 0.436242 0.643836
71 GLU LEU ASP 1OL VAL GLU PHE 0.435374 0.661538
72 GLU ASP GLU ASP PHE GLU ILE LEU SEP LEU 0.433121 0.761194
73 SER ARG ILE ARG ILE ARG GLY TYR VAL ARG 0.432432 0.826087
74 GLY HIS LYS ILE LEU HIS ARG LEU LEU GLN 0.431373 0.675676
75 LYS ARG ARG LYS SEP VAL 0.430769 0.833333
76 GLN VAL PRO LEU ARG PRO MET THR TYR LYS 0.430168 0.7375
77 GLU ASN PRO THR TYR LYS PHE PHE GLU GLN 0.427536 0.705882
78 THR TYR LYS PHE PHE GLU GLN 0.427536 0.705882
79 SER ARG LYS ILE ASP ASN LEU ASP 0.425676 0.753623
80 ARG ASP ARG ALA ALA LYS LEU 0.425197 0.707692
81 ILE ARG LYS ILE LEU PHE LEU ASP GLY ILE 0.425 0.75
82 GLU ASN LEU TYR PHE GLN 0.42446 0.652174
83 GLY GLY LYS LYS LYS TYR GLN LEU 0.42446 0.742424
84 VAL LEU ARG ASP ASP LEU LEU GLU ALA 0.424242 0.738462
85 HIS LYS ILE LEU HIS ARG LEU LEU GLN GLU 0.423313 0.684932
86 ALA TYR ASP GLU SEP TPO ASP GLU GLU 0.422819 0.80303
87 ALA THR VAL ARG THR TYR SER CYS 0.42069 0.794118
88 PHQ LEU VAL ARG TYR 0.42069 0.782609
89 PHE LEU ALA TYR LYS 0.42029 0.701493
90 GLU GLU GLU ASP GLY TPO MET LYS ARG ASN 0.42 0.814286
91 GLU THR VAL ARG PHE GLN SER ASP 0.418301 0.761194
92 ARG PRO MET THR TYR LYS GLY ALA LEU 0.418079 0.716049
93 GLY GLY LYS LYS LYS TYR LYS LEU 0.41791 0.742424
94 ALA ARG LYS ILE ASP ASN LEU ASP 0.417808 0.735294
95 ACE GLU ALA GLN THR ARG LEU 0.417266 0.731343
96 SER GLU ASP GLU PHE TYR ASP ALA LEU SER 0.417219 0.720588
97 PRO LEU GLU PSA ARG LEU 0.416667 0.760563
98 ARG THR TYR SEP GLY PRO MET ASN LYS VAL 0.416216 0.792683
99 ILE LEU GLY LYS PHE LEU HIS ARG LEU 0.415094 0.689189
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 VAL PRO LEU ARG PRO MET THR TYR 0.412121 0.725
104 ASP ALA ASP GLU TYR LEU 0.411765 0.692308
105 GLY ASP GLU VAL LYS VAL PHE ARG 0.411765 0.757576
106 PHE LEU SER TYR LYS 0.410072 0.710145
107 ALA GLN ASP ILE TYR ARG ALA SER TYR 0.409938 0.785714
108 DTY ILE ARG LEU LPD 0.409396 0.697368
109 ARG ARG ARG GLU THR GLN VAL 0.409091 0.757576
110 HIS LYS ILE LEU HIS ARG LEU LEU GLN ASP 0.408805 0.657534
111 ASP ASN ARG LEU GLY LEU VAL TYR GLN PHE 0.408759 0.641791
112 ALA ARG THR M3L GLN THR ALA ALA LYS ALA 0.408163 0.739726
113 TYR HIS SEP VAL VAL ARG TYR ALA 0.407407 0.824324
114 PRO TYR ALA GLY GLU TPO ASP GLU 0.407407 0.802817
115 LYS ILE LEU HIS ARG LEU LEU GLN ASP SER 0.407186 0.726027
116 ACE ARG GLU PTR VAL ASN VAL 0.406667 0.882353
117 LYS MET ASP SEP PHE LEU ASP MET GLN LEU 0.40625 0.8
118 2UE DLY LYS DAR 0.406015 0.712121
119 ARG ARG LEU ILE PHE NH2 0.405797 0.69697
120 ASP ALA GLU PHE ARG HIS ASP 0.405594 0.723077
121 SEP GLN GLU TYR NH2 0.40458 0.787879
122 THR LYS ASN TYR LYS GLN THR SER VAL 0.403974 0.75
123 ARG PHE MET ASP TYR TRP GLU GLY LEU 0.403409 0.692308
124 LYS ARG LYS 0.403361 0.646154
125 ALA THR ALA ALA ALA THR GLU ALA TYR 0.402985 0.666667
126 PRO GLU GLY ASP PM3 GLU GLU VAL LEU 0.402685 0.772727
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: 40
This union binding pocket(no: 1) in the query (biounit: 2pie.bio1) has 11 residues
No: Leader PDB Ligand Sequence Similarity
1 2V1O COA None
2 3BNK FMN None
3 4B7P 9UN 2.17391
4 1Z4O GL1 2.89855
5 4OHU NAD 3.62319
6 4OHU 2TK 3.62319
7 4P5E N6P 3.62319
8 5CCM 4ZX 4.34783
9 5CCM SAM 4.34783
10 2BPM 529 4.34783
11 5HQ8 SAH 4.34783
12 3ZOK GLY 5.07246
13 1Z08 GNP 5.07246
14 5VFC 9BA 5.07246
15 3ITA AIC 5.07246
16 3S7D SAH 5.7971
17 3ELW SAM 5.7971
18 4C0R GDS 6.52174
19 3E2M E2M 7.97101
20 3DLG GWE 8.69565
21 5IE3 AMP 9.42029
22 5IE3 OXD 9.42029
23 5EKO N17 10.1449
24 5BRT FAD 10.1449
25 3UNN MET GLU ASP TPO GLN ALA ILE ASP 10.6195
26 2NU8 COA 10.8696
27 4URS C2E 10.8696
28 1IG0 VIB 10.8696
29 3GCZ SAM 10.8696
30 1XF1 CIT 11.5942
31 5N6N SUC 12.3188
32 1VLJ NAP 13.0435
33 3AL3 SER ILE TYR PHE TPO PRO GLU LEU TYR ASP 13.0435
34 4JWH SAH 13.0435
35 5E50 ALA TYR ASP GLU SEP TPO ASP GLU GLU 14.4144
36 2V0C ANZ 14.4928
37 1A5Z FBP 15.2174
38 1IG3 VIB 15.942
39 1T36 ADP 23.913
40 2W3O TYR ALA GLY SEP TPO ASP GLU ASN 35.3982
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