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 510 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 391 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 298 families.
1 3AL3 Kd = 2.1 uM SER ILE TYR PHE TPO PRO GLU LEU TYR ASP n/a n/a
Polypharmacology
Similar Ligands
Ligand no: 1; Ligand: SER ILE TYR PHE TPO PRO GLU LEU TYR ASP; Similar ligands found: 180
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 SER ASP ILE LEU PHE PRO ALA ASP SER 0.547771 0.824324
6 ASP TYR GLU PRO ILE PRO GLU GLU ALA PHE 0.538462 0.826667
7 PHE TYR ALA PRO GLU PRO ILE THR SER LEU 0.52907 0.881579
8 LEU TYR ALA SER PRO GLN LEU GLU GLY PHE 0.525714 0.864865
9 GLY TYR GLU ASN PRO THR TYR LYS PHE PHE 0.522988 0.815789
10 ASP PHE GLU GLU ILE PRO GLY GLU PTR 0.511364 0.92
11 LYS LEU PRO ALA GLN PHE TYR ILE LEU 0.505682 0.826667
12 GLY TYR GLN ASP TYR GLU PRO GLU ALA 0.496774 0.756757
13 SER LEU ILE PRO TPO PRO ASP LYS 0.493976 0.906667
14 THR PRO TYR ASP ILE ASN GLN MET LEU 0.491429 0.797468
15 ARG ILE PRO SER TYR ARG TYR ARG TYR 0.490909 0.8125
16 ASP PHE GLU GLU ILE PRO GLY GLU TYS LEU 0.488764 0.821429
17 LEU PRO SER PHE GLU THR ALA LEU 0.487952 0.824324
18 ASP PHE GLU GLU ILE PRO GLU GLU TYS LEU 0.486486 0.831325
19 HIS SER ILE THR TYR LEU LEU PRO VAL 0.485876 0.833333
20 ASP ILE ASN TYR TYR ALA SER GLU PRO 0.485207 0.88
21 SER PRO ILE VAL PRO SER PHE ASP MET 0.482558 0.78481
22 SER PHE PHE GLU ASP ASN PHE VAL PRO GLU 0.481481 0.826667
23 PRO PRO THR LEU HIS GLU LEU TYR ASP LEU 0.480447 0.820513
24 LEU PRO PRO LEU ASP ILE THR PRO TYR 0.479532 0.826667
25 ASP ILE ASN TYR TYR THR SER GLU PRO 0.47929 0.88
26 LEU LEU CYS SER TPO PRO ASN GLY LEU 0.478528 0.855263
27 GLU ASP GLU ASP PHE GLU ILE LEU SER LEU 0.478528 0.662162
28 TYR GLN PHE GLY PRO ASP PHE PRO ILE ALA 0.477778 0.84
29 LEU LEU PHE GLY LYS PRO VAL TYR VAL 0.477012 0.826667
30 GLU TYR LEU GLY LEU ASP VAL PRO VAL 0.476471 0.810811
31 GLN LEU SER PRO PHE PRO PHE ASP LEU 0.473373 0.826667
32 SER GLU ASP GLU PHE TYR ASP ALA LEU SER 0.472393 0.702703
33 SER THR SEP PRO THR PHE ASN LYS 0.47191 0.855263
34 ACE GLU ASN LEU TYR PHE GLN SER GLY THR 0.471338 0.631579
35 LEU LEU PHE GLY TYR PRO VAL TYR VAL 0.47093 0.824324
36 LEU LEU PHE GLY PHE PRO VAL TYR VAL 0.47093 0.824324
37 LYS PRO ILE VAL GLN TYR ASP ASN PHE 0.469613 0.855263
38 LYS GLN GLU PRO GLN GLU ILE ASP PHE 0.468571 0.733333
39 LYS LEU TYR GLN ASN PRO THR THR TYR ILE 0.466667 0.855263
40 TYR MET PHE PRO ASN ALA PRO TYR LEU 0.465909 0.777778
41 TYR TYR SER ILE ILE PRO HIS SER ILE 0.465116 0.833333
42 LYS TYR TYR SER ILE ILE PRO HIS SER ILE 0.465116 0.833333
43 LEU PRO PHE ASP LYS SER THR ILE MET 0.464481 0.78481
44 TRP GLU TYR ILE PRO ASN VAL 0.464088 0.807692
45 TYR PRO ASN VAL ASN ILE HIS ASN PHE 0.463687 0.820513
46 SER ILE ILE ASN PHE GLU LYS LEU 0.462963 0.666667
47 GLN VAL PRO SER ASP PRO TYR ASN TYR 0.461538 0.828947
48 ASN ASP LYS TYR GLU PRO PHE TRP GLU 0.458763 0.769231
49 SER SER LEU GLU ASN PHE ALA ALA TYR VAL 0.458333 0.693333
50 LEU PRO PHE ASP LYS THR THR ILE MET 0.458101 0.772152
51 MET GLN SER TPO PRO LEU 0.457831 0.833333
52 SER LEU ARG PHE LEU TYR GLU GLY 0.457317 0.696203
53 ARG LEU TYR GLN ASN PRO THR THR TYR ILE 0.454054 0.814815
54 PRO GLN PTR GLU PTR ILE PRO ALA 0.454023 0.906667
55 TYR PRO TYR ASP VAL PRO ASP TYR ALA 0.453988 0.813333
56 LEU PRO PHE GLU ARG ALA THR ILE MET 0.452128 0.72619
57 LYS PRO PHE PTR VAL ASN VAL GLU PHE 0.451087 0.907895
58 PRO GLN PTR ILE PTR VAL PRO ALA 0.450867 0.92
59 GLU ASP GLU ASP PHE GLU ILE LEU SEP LEU 0.450867 0.716216
60 ACE TYR PRO ILE GLN GLU THR 0.449102 0.786667
61 SER LEU PHE HIS 22G THR PRO 0.448649 0.833333
62 PHE ALA PRO GLY PHE PHE PRO TYR LEU 0.448276 0.802632
63 ALA ILE ALA TYR PHE ILE PRO ASP GLN ALA 0.447205 0.783784
64 TYR TYR SER ILE ALA PRO HIS SER ILE 0.446328 0.810127
65 ILE THR ASP GLN VAL PRO PHE SER VAL 0.446328 0.837838
66 ARG SEP PRO VAL PHE SER 0.445714 0.797468
67 ALA GLY SER VAL GLU GLN TPO PRO LYS LYS 0.444444 0.855263
68 ALA ILE MET PRO ALA ARG PHE TYR PRO LYS 0.441026 0.738095
69 TYR LEU GLY GLY PRO ASP PHE PRO THR ILE 0.44086 0.88
70 ALA PHE ARG ILE PRO LEU THR ARG 0.440678 0.7625
71 PHE ASN PHE PRO GLN ILE THR 0.440476 0.813333
72 PRO GLN PTR GLU GLU ILE PRO ILE 0.44 0.88
73 LYS GLN TRP ASP ASN TYR GLU PHE ILE TRP 0.438889 0.666667
74 SER MET PRO GLU LEU SER PRO VAL LEU 0.438272 0.746835
75 ARG VAL ILE PTR PHE VAL PRO LEU ASN ARG 0.438272 0.891892
76 ARG ARG LEU PRO ILE PHE SER ARG LEU 0.438202 0.7625
77 LEU PRO PHE ASP ARG THR THR ILE MET 0.437838 0.738095
78 GLY ALA ASP ILE PHE TYR LEU ASP GLY ALA 0.4375 0.626667
79 ARG THR PHE SER PRO THR TYR GLY LEU 0.437158 0.848101
80 TRP MET ASP PHE ASP ASP ASP ILE PRO PHE 0.437086 0.72973
81 TRP ASP ILE PRO PHE 0.437086 0.72973
82 ILE MET ASP GLN VAL PRO PHE SER VAL 0.436464 0.782051
83 LEU PHE GLY TYR PRO VAL TYR VAL 0.436047 0.824324
84 LEU ASN PHE PRO ILE SER PRO 0.435583 0.815789
85 TYR SER THR CYS TYR PHE ILE MET 0.435583 0.641026
86 ARG PRO PRO ILE PHE ILE ARG ARG LEU 0.435028 0.7125
87 DHI PRO PHE HIS LEU LEU VAL TYR 0.434783 0.75641
88 PHE GLN PRO GLN ASN GLY GLN PHE ILE 0.434286 0.763158
89 ARG ILE ILE PRO ARG HIS LEU GLN LEU 0.434066 0.695122
90 ARG MET PHE PRO ASN ALA PRO TYR LEU 0.433862 0.755814
91 GLU VAL ALA PRO PRO GLU TYR HIS ARG LYS 0.432836 0.73494
92 ASP LEU TYR CYS TYR GLU GLN LEU ASN 0.432099 0.671053
93 LEU PRO PHE GLU LYS SER THR VAL MET 0.431694 0.772152
94 GLU SER ASP PRO ILE VAL ALA GLN TYR 0.430939 0.878378
95 GLU GLU PRO THR VAL ILE LYS LYS TYR 0.430939 0.84
96 HIS ALA TPO PRO PRO LYS LYS GLU ALA ASP 0.430851 0.807692
97 ASP SEP TYR GLU VAL LEU ASP LEU 0.430233 0.756757
98 TYR LEU GLU PRO ALA PRO VAL THR ALA 0.430233 0.815789
99 PHE LEU PRO HIS ALY TYR ASP VAL LYS LEU 0.430052 0.7375
100 PHE LEU PRO SER ASP PHE PHE PRO SER VAL 0.429412 0.84
101 ASN PHE ASP ASN PRO VAL TYR ARG LYS THR 0.427835 0.802469
102 PRO PRO ARG PRO ILE TYR ASN ARG ASN 0.427778 0.765432
103 LEU GLN ARG VAL LEU SEP ALA PRO PHE 0.426966 0.8
104 ASN TRP SER HIS PRO GLN PHE GLU LYS 0.426829 0.717949
105 TYR PRO PHE PHE NH2 0.426667 0.72973
106 SER SER LEU GLU ASN PHE ARG ALA TYR VAL 0.42623 0.6875
107 ASP ILE ALA TYR TYR THR SER GLU PRO 0.426035 0.891892
108 ASN TYR THR PRO GLY PRO GLY ILE ARG PHE 0.42487 0.814815
109 GLY GLN VAL PRO PHE SER LYS GLU GLU CYS 0.424581 0.766234
110 GLU GLU TYR LEU GLN ALA PHE THR TYR 0.423529 0.662162
111 GLU THR LEU LEU ASP LEU ASP PHE ASP PRO 0.423313 0.810811
112 TYR LEU LYS GLU PRO VAL HIS GLY VAL 0.42328 0.769231
113 ARG LEU TYR HIS SEP LEU PRO ALA 0.42328 0.841463
114 ARG ARG ILE TYR ASP LEU ILE GLU LEU 0.421965 0.6375
115 ILE PRO ALA TYR GLY VAL LEU THR ILE 0.421348 0.851351
116 TYR PRO LYS ARG ILE ALA 0.41954 0.7375
117 GLN TYR PHE MET TPO GLU PTR VAL ALA 0.419355 0.759494
118 LYS PRO PHE PTR VAL ASN VAL NH2 0.418994 0.894737
119 ALA VAL ALA PHE TYR ILE PRO ASP GLN ALA 0.418182 0.797297
120 LYS PRO ILE VAL VAL LEU HIS GLY TYR 0.417989 0.782051
121 GLU ASN LEU TYR PHE GLN 0.417722 0.64
122 SER SER TYR ARG ARG PRO VAL GLY ILE 0.417582 0.8125
123 VAL SER GLN ASN TYR PRO ILE VAL GLN ASN 0.417143 0.853333
124 PRO MET GLN SER TPO PRO LEU 0.417143 0.835443
125 ALA PRO GLN PRO ALA PRO GLU ASN ALA TYR 0.417143 0.766234
126 ACE MET GLN SER TPO PRO LEU NH2 0.416667 0.822785
127 SER ILE ILE GLY PHE GLU LYS LEU 0.416667 0.675676
128 GLY ILE LEU GLU PHE VAL PHE THR LEU 0.414634 0.662162
129 ARG PRO GLY ASN PHE LEU GLN SER ARG LEU 0.414508 0.740741
130 VAL MET ALA PRO ARG THR LEU PHE LEU 0.413978 0.694118
131 GLY SER ASP PRO PHE LYS 0.41358 0.746667
132 SER LEU GLU VAL TPO GLU ALA ASP THR 0.41358 0.72973
133 TYR LEU GLU PRO GLY PRO VAL THR VAL 0.413408 0.84
134 TYR LEU GLU PRO GLY PRO VAL THR ALA 0.413408 0.84
135 GLU ILE ILE ASN PHE GLU LYS LEU 0.413174 0.605263
136 GLU VAL PTR GLU SER PRO 0.413174 0.932432
137 SER GLU LEU GLU ILE LYS ARG TYR 0.412791 0.675
138 SER LEU PHE ASN THR VAL ALA THR LEU TYR 0.412791 0.653333
139 PIV HIS PRO PHE HIS LPL TYR TYR SER 0.412371 0.7875
140 SER TYR SEP PRO THR SEP PRO SEP TYR SER 0.411765 0.866667
141 THR GLU ASN LEU TYR PHE GLN SER GLY THR 0.411429 0.733333
142 ASN GLY TYR GLU ASN PRO THR TYR LYS 0.410811 0.815789
143 ASN ASP TRP LEU LEU PRO SER TYR 0.410526 0.846154
144 FME TYR PHE ILE ASN ILE LEU THR LEU 0.410405 0.64557
145 ALA PRO SER PTR VAL ASN VAL GLN ASN 0.410112 0.921053
146 SER ASP PTR MET ASN MET THR PRO 0.410112 0.886076
147 ACE GLN PM3 GLU GLU ILE PRO 0.409639 0.8
148 SER GLU ILE GLU PHE ALA ARG LEU 0.409357 0.620253
149 SER PRO THR SER PRO SEP TYR SER PRO PRO 0.409091 0.88
150 SER PRO LEU ASP SER LEU TRP TRP ILE 0.40884 0.831169
151 SER ALA GLU PRO VAL PRO LEU GLN LEU 0.408284 0.786667
152 ACE PRO ASP PTR GLU ASN LEU 0.408284 0.87013
153 ASN ARG PRO VAL TYR ILE PRO ARG PRO PRO 0.407821 0.75
154 GLN ASN TYR PRO ILE VAL GLN 0.406977 0.813333
155 ACE LEU TYR ALA SER SER ASN PRO ALA PTR 0.406593 0.960526
156 GLN MET PRO THR GLU ASP GLU TYR 0.405556 0.772152
157 DTY ILE ARG LEU LPD 0.404762 0.746835
158 SER HIS PHE ASN GLU TYR GLU 0.404624 0.679487
159 TYR ALA GLY SEP TPO ASP GLU ASN 0.404494 0.763158
160 LEU SER SER PRO VAL THR LYS SER PHE 0.404494 0.786667
161 PHE ALA PRO GLY ASN TYR PRO ALA LEU 0.404372 0.831169
162 LEU PRO PHE GLU ARG ALA THR VAL MET 0.404145 0.714286
163 ILE PRO LEU THR GLU GLU ALA GLU LEU 0.403614 0.76
164 VAL ORN LEU DPN PRO VAL ORN LEU DPN PRO 0.403509 0.733333
165 PRO TYR ALA GLY SEP TPO ASP GLU ASN 0.403409 0.84
166 TYR GLU LEU ASP GLU LYS PHE ASP ARG LEU 0.403409 0.6625
167 GLU ARG GLU SEP GLU PHE ASP ILE GLU ASP 0.403315 0.675
168 GLN VAL PRO LEU ARG PRO MET THR TYR LYS 0.402985 0.761905
169 SER LEU LYS ILE ASP ASN GLU ASP 0.402439 0.64
170 SER SER ILE GLU PHE ALA ARG LEU 0.402299 0.632911
171 GLN ASN GLY PTR GLU ASN PRO THR TYR 0.402235 0.893333
172 SER LEU PHE ASN THR ILE ALA VAL LEU 0.401163 0.613333
173 ASP ILE ASN TYS TYS THR SER GLU PRO 0.40113 0.857143
174 VAL PRO LEU ARG PRO MET THR TYR 0.4 0.75
175 ASP GLU LEU GLU ILE LYS ALA TYR 0.4 0.666667
176 ACE ILE TYR GLU SER LEU 0.4 0.662162
177 GLU LEU PRO PRO VAL LYS ILE HIS CYS 0.4 0.708861
178 VAL PRO TYR SER SER ALA GLN NAG 0.4 0.822785
179 ALA CYS SEP PRO GLN PHE GLY 0.4 0.826667
180 TYR SEP PRO THR SEP PRO SER 0.4 0.893333
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
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