Receptor
PDB id Resolution Class Description Source Keywords
3AL3 2.15 Å NON-ENZYME: BINDING CRYSTAL STRUCTURE OF TOPBP1 BRCT7/8-BACH1 PEPTIDE COMPLEX HOMO SAPIENS BRCT DOMAIN-PHOSPHOPEPTIDE COMPLEX DNA BINDING PROTEIN-PROTBINDING COMPLEX
Ref.: MOLECULAR BASIS OF BACH1/FANCJ RECOGNITION BY TOPBP REPLICATION CHECKPOINT CONTROL J.BIOL.CHEM. V. 286 4292 2011
Ligand
Ligand Chain:Residue Validity Ligand Warnings Binding Data NGL Viewer Molecular Weight (Da) Formula SMILES
FMT A:1;
 Invalid;
 none;
 submit data
46.025 C H2 O2 C(=O)...
SER ILE TYR PHE TPO PRO GLU LEU TYR ASP B:1129;
 Valid;
 none;
 Kd = 2.1 uM
1308.32 n/a P(=O)...
View in 3D viewer
90% Homology Family
Leader
PDB id Resolution Class Description Source Keywords
3AL3 2.15 Å NON-ENZYME: BINDING CRYSTAL STRUCTURE OF TOPBP1 BRCT7/8-BACH1 PEPTIDE COMPLEX HOMO SAPIENS BRCT DOMAIN-PHOSPHOPEPTIDE COMPLEX DNA BINDING PROTEIN-PROTBINDING COMPLEX
Ref.: MOLECULAR BASIS OF BACH1/FANCJ RECOGNITION BY TOPBP REPLICATION CHECKPOINT CONTROL J.BIOL.CHEM. V. 286 4292 2011
Members (1)
No: PDB id Binding Data Representative ligand Formula Smiles
The Class containing this family consists of a total of 552 families.
1 3AL3 Kd = 2.1 uM SER ILE TYR PHE TPO PRO GLU LEU TYR ASP 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 426 families.
1 3AL3 Kd = 2.1 uM SER ILE TYR PHE TPO PRO GLU LEU TYR ASP 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 322 families.
1 3AL3 Kd = 2.1 uM SER ILE TYR PHE TPO PRO GLU LEU TYR ASP n/a n/a
Polypharmacology
Similar Ligands (2D)
Ligand no: 1; Ligand: SER ILE TYR PHE TPO PRO GLU LEU TYR ASP; Similar ligands found: 188
No: Ligand ECFP6 Tc MDL keys Tc
1 SER ILE TYR PHE TPO PRO GLU LEU TYR ASP 1 1
2 ASP PHE GLU GLU ILE PRO GLY GLU TYR LEU 0.568047 0.84
3 ASP PHE GLU GLU ILE PRO GLU GLU TYS 0.558282 0.797619
4 PHE GLU ALA ILE PRO ALA GLU TYR LEU 0.554878 0.824324
5 ASP TYR GLU PRO ILE PRO GLU GLU ALA PHE 0.538462 0.826667
6 PHE TYR ALA PRO GLU PRO ILE THR SER LEU 0.52907 0.881579
7 LEU TYR ALA SER PRO GLN LEU GLU GLY PHE 0.525714 0.864865
8 GLY TYR GLU ASN PRO THR TYR LYS PHE PHE 0.522988 0.815789
9 ASP PHE GLU GLU ILE PRO GLY GLU PTR 0.511364 0.92
10 TYR ASP LEU SEP LEU PRO PHE PRO 0.505814 0.946667
11 LYS LEU PRO ALA GLN PHE TYR ILE LEU 0.505682 0.826667
12 ASP TYR ASN PRO TYR LEU LEU PHE LEU LYS 0.502994 0.842105
13 ASP ASP LEU ASP VAL PRO SER PHE LEU GLN 0.49697 0.824324
14 SER LEU ILE PRO TPO PRO ASP LYS 0.493976 0.906667
15 THR PRO TYR ASP ILE ASN GLN MET LEU 0.491429 0.797468
16 ARG ILE PRO SER TYR ARG TYR ARG TYR 0.490909 0.8125
17 ASP PHE GLU GLU ILE PRO GLY GLU TYS LEU 0.488764 0.821429
18 LEU PRO SER PHE GLU THR ALA LEU 0.487952 0.824324
19 ASP PHE GLU GLU ILE PRO GLU GLU TYS LEU 0.486486 0.831325
20 HIS SER ILE THR TYR LEU LEU PRO VAL 0.485876 0.833333
21 ASP ILE ASN TYR TYR ALA SER GLU PRO 0.485207 0.88
22 SER PRO ILE VAL PRO SER PHE ASP MET 0.482558 0.78481
23 SER PHE PHE GLU ASP ASN PHE VAL PRO GLU 0.481481 0.826667
24 PRO PRO THR LEU HIS GLU LEU TYR ASP LEU 0.480447 0.820513
25 LEU PRO PRO LEU ASP ILE THR PRO TYR 0.479532 0.826667
26 ASP ILE ASN TYR TYR THR SER GLU PRO 0.47929 0.88
27 LEU LEU CYS SER TPO PRO ASN GLY LEU 0.478528 0.855263
28 GLU ASP GLU ASP PHE GLU ILE LEU SER LEU 0.478528 0.662162
29 TYR GLN PHE GLY PRO ASP PHE PRO ILE ALA 0.477778 0.84
30 LEU LEU PHE GLY LYS PRO VAL TYR VAL 0.477012 0.826667
31 GLU TYR LEU GLY LEU ASP VAL PRO VAL 0.476471 0.810811
32 GLY TYR GLN ASP TYR GLU PRO GLU ALA 0.474359 0.756757
33 PHE LYS TPO GLU GLY PRO ASP SER ASP 0.474286 0.826667
34 GLN LEU SER PRO PHE PRO PHE ASP LEU 0.473373 0.826667
35 ACE GLU LEU LEU MET VAL PRO ASP MET TYR 0.473373 0.75641
36 SER THR SEP PRO THR PHE ASN LYS 0.47191 0.855263
37 ACE GLU ASN LEU TYR PHE GLN SER GLY THR 0.471338 0.631579
38 LEU LEU PHE GLY TYR PRO VAL TYR VAL 0.47093 0.824324
39 LEU LEU PHE GLY PHE PRO VAL TYR VAL 0.47093 0.824324
40 LYS PRO ILE VAL GLN TYR ASP ASN PHE 0.469613 0.855263
41 LYS GLN GLU PRO GLN GLU ILE ASP PHE 0.468571 0.733333
42 LYS LEU TYR GLN ASN PRO THR THR TYR ILE 0.466667 0.855263
43 ACE GLU HIS PHE ILE VAL PRO ASP LEU TYR 0.465909 0.730769
44 TYR MET PHE PRO ASN ALA PRO TYR LEU 0.465909 0.777778
45 TYR TYR SER ILE ILE PRO HIS SER ILE 0.465116 0.833333
46 LEU PRO PHE ASP LYS SER THR ILE MET 0.464481 0.78481
47 TRP GLU TYR ILE PRO ASN VAL 0.464088 0.807692
48 TYR PRO ASN VAL ASN ILE HIS ASN PHE 0.463687 0.820513
49 SER ILE ILE ASN PHE GLU LYS LEU 0.462963 0.666667
50 GLN VAL PRO SER ASP PRO TYR ASN TYR 0.461538 0.828947
51 SER ILE ILE GLN PHE GLU HIS LEU 0.460606 0.679487
52 ASN ASP LYS TYR GLU PRO PHE TRP GLU 0.458763 0.769231
53 SER SER LEU GLU ASN PHE ALA ALA TYR VAL 0.458333 0.693333
54 LEU PRO PHE ASP LYS THR THR ILE MET 0.458101 0.772152
55 MET GLN SER TPO PRO LEU 0.457831 0.833333
56 SER LEU ARG PHE LEU TYR GLU GLY 0.457317 0.696203
57 ARG LEU TYR GLN ASN PRO THR THR TYR ILE 0.454054 0.814815
58 PRO GLN PTR GLU PTR ILE PRO ALA 0.454023 0.906667
59 TYR PRO TYR ASP VAL PRO ASP TYR ALA 0.453988 0.813333
60 SER SER PHE TYR PRO SEP ALA GLU GLY 0.453488 0.918919
61 ALA THR PRO PHE GLN GLU 0.453416 0.743243
62 LEU PRO PHE GLU ARG ALA THR ILE MET 0.452128 0.72619
63 LYS PRO PHE PTR VAL ASN VAL GLU PHE 0.451087 0.907895
64 GLU ASP GLU ASP PHE GLU ILE LEU SEP LEU 0.450867 0.716216
65 PRO GLN PTR ILE PTR VAL PRO ALA 0.450867 0.92
66 ACE TYR PRO ILE GLN GLU THR 0.449102 0.786667
67 ALA GLU THR PHE TYR VAL ASP GLY 0.448718 0.648649
68 SER LEU PHE HIS 22G THR PRO 0.448649 0.833333
69 PHE ALA PRO GLY PHE PHE PRO TYR LEU 0.448276 0.802632
70 ALA ILE ALA TYR PHE ILE PRO ASP GLN ALA 0.447205 0.783784
71 ALA PRO ALA TRP LEU PHE GLU ALA 0.446927 0.717949
72 ILE THR ASP GLN VAL PRO PHE SER VAL 0.446328 0.837838
73 TYR TYR SER ILE ALA PRO HIS SER ILE 0.446328 0.810127
74 ARG SEP PRO VAL PHE SER 0.445714 0.797468
75 ALA GLY SER VAL GLU GLN TPO PRO LYS LYS 0.444444 0.855263
76 SER GLU ASP GLU PHE TYR ASP ALA LEU SER 0.443114 0.702703
77 SER LEU ASN TYR ILE ILE LYS VAL LYS GLU 0.44186 0.710526
78 ALA ILE MET PRO ALA ARG PHE TYR PRO LYS 0.441026 0.738095
79 TYR LEU GLY GLY PRO ASP PHE PRO THR ILE 0.44086 0.88
80 ALA PHE ARG ILE PRO LEU THR ARG 0.440678 0.7625
81 PHE ASN PHE PRO GLN ILE THR 0.440476 0.813333
82 PRO GLN PTR GLU GLU ILE PRO ILE 0.44 0.88
83 LEU PRO PHE GLU LEU ARG GLY HIS LEU VAL 0.439153 0.695122
84 GLN ILE MET TYR ASN TYR PRO ALA MET 0.438889 0.775
85 SER MET PRO GLU LEU SER PRO VAL LEU 0.438272 0.746835
86 ARG ARG LEU PRO ILE PHE SER ARG LEU 0.438202 0.7625
87 LEU PRO PHE ASP ARG THR THR ILE MET 0.437838 0.738095
88 ARG THR PHE SER PRO THR TYR GLY LEU 0.437158 0.848101
89 ILE MET ASP GLN VAL PRO PHE SER VAL 0.436464 0.782051
90 LEU PHE GLY TYR PRO VAL TYR VAL 0.436047 0.824324
91 LEU ASN PHE PRO ILE SER PRO 0.435583 0.815789
92 LYS TYR TYR SER ILE ILE PRO HIS SER ILE 0.435028 0.833333
93 ARG PRO PRO ILE PHE ILE ARG ARG LEU 0.435028 0.7125
94 DHI PRO PHE HIS LEU LEU VAL TYR 0.434783 0.75641
95 PHE GLN PRO GLN ASN GLY GLN PHE ILE 0.434286 0.763158
96 ARG ILE ILE PRO ARG HIS LEU GLN LEU 0.434066 0.695122
97 ARG MET PHE PRO ASN ALA PRO TYR LEU 0.433862 0.755814
98 ARG VAL ILE PTR PHE VAL PRO LEU ASN ARG 0.432099 0.891892
99 ASP LEU TYR CYS TYR GLU GLN LEU ASN 0.432099 0.671053
100 LEU PRO PHE GLU LYS SER THR VAL MET 0.431694 0.772152
101 GLU SER ASP PRO ILE VAL ALA GLN TYR 0.430939 0.878378
102 GLU GLU PRO THR VAL ILE LYS LYS TYR 0.430939 0.84
103 HIS ALA TPO PRO PRO LYS LYS GLU ALA ASP 0.430851 0.807692
104 TYR LEU GLU PRO ALA PRO VAL THR ALA 0.430233 0.815789
105 ASP SEP TYR GLU VAL LEU ASP LEU 0.430233 0.756757
106 PHE LEU PRO HIS ALY TYR ASP VAL LYS LEU 0.430052 0.7375
107 PHE LEU PRO SER ASP PHE PHE PRO SER VAL 0.429412 0.84
108 PRO PRO ARG PRO ILE TYR ASN ARG ASN 0.427778 0.765432
109 TYR PRO PHE PHE NH2 0.426667 0.72973
110 SER SER LEU GLU ASN PHE ARG ALA TYR VAL 0.42623 0.6875
111 ASN TYR THR PRO GLY PRO GLY ILE ARG PHE 0.42487 0.814815
112 GLY GLN VAL PRO PHE SER LYS GLU GLU CYS 0.424581 0.766234
113 GLU GLU TYR LEU GLN ALA PHE THR TYR 0.423529 0.662162
114 TYR LEU LYS GLU PRO VAL HIS GLY VAL 0.42328 0.769231
115 ARG LEU TYR HIS SEP LEU PRO ALA 0.42328 0.841463
116 ARG PRO GLY ASN PHE LEU GLN SER ARG PRO 0.42246 0.731707
117 ASP TYR ILE ASN THR ASN VAL LEU PRO 0.421965 0.84
118 ARG ARG ILE TYR ASP LEU ILE GLU LEU 0.421965 0.6375
119 ILE PRO ALA TYR GLY VAL LEU THR ILE 0.421348 0.851351
120 SER GLY ILE PHE LEU GLU THR SER 0.420382 0.648649
121 TYR PRO LYS ARG ILE ALA 0.41954 0.7375
122 GLN TYR PHE MET TPO GLU PTR VAL ALA 0.419355 0.759494
123 LYS PRO PHE PTR VAL ASN VAL NH2 0.418994 0.894737
124 ALA VAL ALA PHE TYR ILE PRO ASP GLN ALA 0.418182 0.797297
125 LYS PRO ILE VAL VAL LEU HIS GLY TYR 0.417989 0.782051
126 GLU ASN LEU TYR PHE GLN 0.417722 0.64
127 SER SER TYR ARG ARG PRO VAL GLY ILE 0.417582 0.8125
128 VAL SER GLN ASN TYR PRO ILE VAL GLN ASN 0.417143 0.853333
129 PRO MET GLN SER TPO PRO LEU 0.417143 0.835443
130 ALA PRO GLN PRO ALA PRO GLU ASN ALA TYR 0.417143 0.766234
131 SER ILE ILE GLY PHE GLU LYS LEU 0.416667 0.675676
132 GLY ALA ASP ILE PHE TYR LEU ASP GLY ALA 0.416149 0.613333
133 ALA LEU MET PRO GLY GLN PHE PHE VAL 0.41573 0.717949
134 GLY ILE LEU GLU PHE VAL PHE THR LEU 0.414634 0.662162
135 ARG PRO GLY ASN PHE LEU GLN SER ARG LEU 0.414508 0.740741
136 VAL MET ALA PRO ARG THR LEU PHE LEU 0.413978 0.694118
137 HIS LEU TYR PHE SER SEP ASN 0.413793 0.807692
138 PIV HIS PRO PHE HIS LPL TYR TYR SER 0.413613 0.7625
139 SER LEU GLU VAL TPO GLU ALA ASP THR 0.41358 0.72973
140 TYR LEU GLU PRO GLY PRO VAL THR ALA 0.413408 0.84
141 TYR LEU GLU PRO GLY PRO VAL THR VAL 0.413408 0.84
142 GLU ILE ILE ASN PHE GLU LYS LEU 0.413174 0.605263
143 GLU VAL PTR GLU SER PRO 0.413174 0.932432
144 ASP LEU PRO PHE 0.412903 0.72973
145 SER LEU PHE ASN THR VAL ALA THR LEU TYR 0.412791 0.653333
146 SER GLU LEU GLU ILE LYS ARG TYR 0.412791 0.675
147 SER HIS SEP SER PRO ALA SER LEU GLN 0.411765 0.846154
148 TRP ASP ILE PRO PHE 0.411765 0.72973
149 THR GLU ASN LEU TYR PHE GLN SER GLY THR 0.411429 0.733333
150 ASN ARG PRO VAL TYR ILE PRO ARG PRO PRO 0.411111 0.75
151 ASN GLY TYR GLU ASN PRO THR TYR LYS 0.410811 0.815789
152 ASN ASP TRP LEU LEU PRO SER TYR 0.410526 0.846154
153 FME TYR PHE ILE ASN ILE LEU THR LEU 0.410405 0.64557
154 SER ASP PTR MET ASN MET THR PRO 0.410112 0.886076
155 ALA PRO SER PTR VAL ASN VAL GLN ASN 0.410112 0.921053
156 SER GLU ILE GLU PHE ALA ARG LEU 0.409357 0.620253
157 ASP PHE GLU LYS GLU GLY TYR SER LEU 0.409091 0.746667
158 SER PRO LEU ASP SER LEU TRP TRP ILE 0.40884 0.831169
159 SER ALA GLU PRO VAL PRO LEU GLN LEU 0.408284 0.786667
160 ACE GLY PHE GLY VAL VAL PRO SER PHE TYR 0.408284 0.783784
161 VAL TYR ARG SER LEU SEP PHE GLU 0.407407 0.716216
162 GLN ASN TYR PRO ILE VAL GLN 0.406977 0.813333
163 ASP ILE ALA TYR TYR THR SER GLU PRO 0.406977 0.891892
164 ACE LEU TYR ALA SER SER ASN PRO ALA PTR 0.406593 0.960526
165 GLN MET PRO THR GLU ASP GLU TYR 0.405556 0.772152
166 DTY ILE ARG LEU LPD 0.404762 0.746835
167 SER HIS PHE ASN GLU TYR GLU 0.404624 0.679487
168 LEU SER SER PRO VAL THR LYS SER PHE 0.404494 0.786667
169 TYR ALA GLY SEP TPO ASP GLU ASN 0.404494 0.763158
170 THR THR ALA PRO PHE LEU SER GLY LYS 0.404372 0.802632
171 PHE ALA PRO GLY ASN TYR PRO ALA LEU 0.404372 0.831169
172 LEU PRO PHE GLU ARG ALA THR VAL MET 0.404145 0.714286
173 ILE PRO LEU THR GLU GLU ALA GLU LEU 0.403614 0.76
174 VAL ORN LEU DPN PRO VAL ORN LEU DPN PRO 0.403509 0.733333
175 TYR GLU LEU ASP GLU LYS PHE ASP ARG LEU 0.403409 0.6625
176 GLU ARG GLU SEP GLU PHE ASP ILE GLU ASP 0.403315 0.675
177 GLN VAL PRO LEU ARG PRO MET THR TYR LYS 0.402985 0.761905
178 SER LEU LYS ILE ASP ASN GLU ASP 0.402439 0.64
179 SER SER ILE GLU PHE ALA ARG LEU 0.402299 0.632911
180 SER LEU PHE ASN THR ILE ALA VAL LEU 0.401163 0.613333
181 GLU PRO VAL GLU THR THR ASP TYR 0.401163 0.824324
182 ASP GLU LEU GLU ILE LYS ALA TYR 0.4 0.666667
183 TYR SEP PRO THR SEP PRO SER 0.4 0.893333
184 VAL PRO TYR SER SER ALA GLN NAG 0.4 0.822785
185 ACE ILE TYR GLU SER LEU 0.4 0.662162
186 VAL PRO LEU ARG PRO MET THR TYR 0.4 0.75
187 GLU LEU PRO PRO VAL LYS ILE HIS CYS 0.4 0.708861
188 ALA CYS SEP PRO GLN PHE GLY 0.4 0.826667
Similar Ligands (3D)
Ligand no: 1; Ligand: SER ILE TYR PHE TPO PRO GLU LEU TYR ASP; 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 : 3AL3; Ligand: SER ILE TYR PHE TPO PRO GLU LEU TYR ASP; 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: 3al3.bio1) has 24 residues
No: Leader PDB Ligand Sequence Similarity
APoc FAQ
Feedback