Receptor
PDB id Resolution Class Description Source Keywords
1H6W 1.9 Å NON-ENZYME: MOBILE CRYSTAL STRUCTURE OF A HEAT- AND PROTEASE-STABLE FRAGMENT OF BACTERIOPHAGE T4 SHORT FIBRE BACTERIOPHAGE T4 STRUCTURAL PROTEIN GENE PRODUCT 12 ADHESIN FIBROUS PROTEI
Ref.: CRYSTAL STRUCTURE OF A HEAT- AND PROTEASE-STABLE PA BACTERIOPHAGE T4 SHORT TAIL FIBRE J.MOL.BIOL. V. 314 1137 2001
Ligand
Ligand Chain:Residue Validity Ligand Warnings Binding Data NGL Viewer Molecular Weight (Da) Formula SMILES
SER LEU ASN TYR ILE ILE LYS VAL LYS GLU B:518;
Valid;
none;
submit data
1207.46 n/a O=C([...
View in 3D viewer
90% Homology Family
Leader
PDB id Resolution Class Description Source Keywords
1H6W 1.9 Å NON-ENZYME: MOBILE CRYSTAL STRUCTURE OF A HEAT- AND PROTEASE-STABLE FRAGMENT OF BACTERIOPHAGE T4 SHORT FIBRE BACTERIOPHAGE T4 STRUCTURAL PROTEIN GENE PRODUCT 12 ADHESIN FIBROUS PROTEI
Ref.: CRYSTAL STRUCTURE OF A HEAT- AND PROTEASE-STABLE PA BACTERIOPHAGE T4 SHORT TAIL FIBRE J.MOL.BIOL. V. 314 1137 2001
Members (1)
No: PDB id Binding Data Representative ligand Formula Smiles
The Class containing this family consists of a total of 68 families.
1 1H6W - SER LEU ASN TYR ILE ILE LYS VAL LYS GLU 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 59 families.
1 1H6W - SER LEU ASN TYR ILE ILE LYS VAL LYS GLU 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 40 families.
1 1H6W - SER LEU ASN TYR ILE ILE LYS VAL LYS GLU n/a n/a
Polypharmacology
Similar Ligands (2D)
Ligand no: 1; Ligand: SER LEU ASN TYR ILE ILE LYS VAL LYS GLU; Similar ligands found: 186
No: Ligand ECFP6 Tc MDL keys Tc
1 SER LEU ASN TYR ILE ILE LYS VAL LYS GLU 1 1
2 SER ILE ILE ASN PHE GLU LYS LEU 0.648438 0.910714
3 SER GLU LEU GLU ILE LYS ARG TYR 0.631579 0.870968
4 GLU LEU ASN ARG LYS MET ILE TYR MET 0.625 0.80303
5 SER LEU LYS ILE ASP ASN GLU ASP 0.606299 0.875
6 ASP GLU LEU GLU ILE LYS ALA TYR 0.593985 0.910714
7 SER LEU TYR ASN THR ILE ALA THR LEU 0.580153 0.910714
8 GLU ILE ILE ASN PHE GLU LYS LEU 0.578947 0.857143
9 GLN PHE LYS ASP ASN VAL ILE LEU LEU 0.57554 0.875
10 SER SER LEU GLU ASN PHE ALA ALA TYR VAL 0.57554 0.87931
11 CYS THR GLU LEU LYS LEU ASN ASP TYR 0.573529 0.929825
12 SER LEU LYS ILE ASP ASN LEU ASP 0.571429 0.875
13 SER LEU TYR ASN VAL VAL ALA THR LEU 0.568182 0.875
14 GLU LEU ASP LYS TYR ALA SER 0.564885 0.928571
15 GLU LEU LYS ARG LYS MET ILE TYR MET 0.5625 0.757576
16 SER LEU TYR ASN THR VAL ALA THR LEU 0.560606 0.875
17 SER ASP LYS ILE ASP ASN LEU ASP 0.551181 0.875
18 SER GLN TYR TYR TYR ASN SER LEU 0.544 0.87931
19 ARG ARG ILE TYR ASP LEU ILE GLU LEU 0.538462 0.822581
20 CYS THR GLU LEU LYS LEU SER ASP TYR 0.535714 0.929825
21 SER LEU LYS ILE ASP ASN MET ASP 0.533333 0.816667
22 SER GLN LEU LYS ASN ASN ALA LYS GLU ILE 0.530303 0.892857
23 SER ALA LYS ILE ASP ASN LEU ASP 0.526316 0.875
24 SER ARG ILE ARG ILE ARG GLY TYR VAL ARG 0.52518 0.857143
25 GLU ASN LEU TYR PHE GLN 0.523077 0.810345
26 THR ASN GLU TYR LYS VAL 0.519685 0.892857
27 LEU LEU TYR GLY PHE VAL ASN TYR ILE 0.51773 0.830508
28 SER ILE ILE GLY PHE GLU LYS LEU 0.514286 0.859649
29 SER HIS LYS ILE ASP ASN LEU ASP 0.513889 0.83871
30 PHE LEU SER TYR LYS 0.507692 0.87931
31 SER ARG LYS ILE ASP ASN LEU ASP 0.507143 0.806452
32 THR LYS ASN TYR LYS GLN PHE SER VAL 0.5 0.913793
33 LEU LEU TYR GLY PHE VAL ASN TYR VAL 0.5 0.813559
34 THR LYS ASN TYR LYS GLN THR SER VAL 0.5 0.964286
35 ASP LEU LYS ILE ASP ASN LEU ASP 0.496183 0.821429
36 TYR GLU LEU ASP GLU LYS PHE ASP ARG LEU 0.493243 0.796875
37 GLU GLU ASN LEU LEU ASP PHE VAL ARG PHE 0.493243 0.734375
38 GLY ILE LEU GLU PHE VAL PHE THR LEU 0.492754 0.810345
39 ACE ILE TYR GLU SER LEU 0.492188 0.875
40 LYS PRO ILE VAL GLN TYR ASP ASN PHE 0.490683 0.782609
41 GLU LEU ARG ARG LYS MET MET TYR MET 0.48951 0.757576
42 GLU GLN TYR LYS PHE TYR SER VAL 0.489209 0.896552
43 SER LEU TYR LEU THR VAL ALA THR LEU 0.488722 0.839286
44 SER SER LEU GLU ASN PHE ARG ALA TYR VAL 0.487342 0.828125
45 LYS VAL ILE THR PHE ILE ASP LEU 0.485714 0.892857
46 GLU ASP GLU ASP PHE GLU ILE LEU SER LEU 0.482759 0.875
47 SER GLU ILE GLU PHE ALA ARG LEU 0.482759 0.774194
48 SER LEU PHE ASN THR VAL ALA THR LEU 0.482014 0.821429
49 ALA ALA SER LEU TYR GLU LYS LYS ALA ALA 0.482014 0.946429
50 ALA LEU LYS ILE ASP ASN LEU ASP 0.480916 0.821429
51 SER PTR VAL ASN VAL GLN ASN 0.477941 0.78125
52 SER LEU PHE ASN THR VAL ALA THR LEU TYR 0.47619 0.827586
53 SER HIS VAL ALA VAL GLU ASN ALA LEU 0.475524 0.774194
54 ILE LEU ASN ALA MET ILE VAL LYS ILE 0.47482 0.733333
55 ALA THR LYS ILE ASP ASN LEU ASP 0.474074 0.875
56 PHE LEU ALA TYR LYS 0.473684 0.810345
57 LYS ARG GLU ALA ILE VAL LYS ALA ASP GLU 0.473684 0.767857
58 THR GLU ASN LEU TYR PHE GLN SER GLY THR 0.473333 0.898305
59 ALA ASP LYS ILE ASP ASN LEU ASP 0.473282 0.821429
60 SER SER ILE GLU PHE ALA ARG LEU 0.472973 0.790323
61 TYR ASP GLN ILE LEU 0.472868 0.803571
62 TYR GLN SER LYS LEU 0.472868 0.928571
63 ALA ARG THR GLU LEU TYR ARG SER LEU 0.472603 0.854839
64 SER LEU PHE ASN THR ILE ALA VAL LEU 0.472603 0.839286
65 SER ILE ILE GLN PHE GLU HIS LEU 0.472603 0.793651
66 GLU LEU LYS TPO GLU ARG TYR 0.470199 0.753623
67 ASP TYR ILE ASN THR ASN VAL LEU PRO 0.466667 0.791045
68 GLU GLU PRO THR VAL ILE LYS LYS TYR 0.465409 0.791045
69 LEU GLY TYR GLY PHE VAL ASN TYR ILE 0.465278 0.830508
70 FME TYR PHE ILE ASN ILE LEU THR LEU 0.463087 0.806452
71 SER GLN ASN TYR 0.46281 0.839286
72 MET LEU ILE TYR SER MET TRP GLY LYS 0.461538 0.782609
73 LEU ALA ILE TYR SER 0.460938 0.821429
74 ARG HIS ARG MLZ VAL LEU ARG ASP ASN TYR 0.460606 0.736111
75 SER LEU ARG PHE LEU TYR GLU GLY 0.458904 0.784615
76 LYS VAL LEU SER LYS ILE PHE MYR 0.458065 0.847458
77 SER HIS PHE ASN GLU TYR GLU 0.456376 0.765625
78 ALA LEU TYR ASN THR ALA ALA ALA LEU 0.455224 0.821429
79 ACE GLU ASN LEU TYR PHE GLN SER GLY THR 0.453901 0.79661
80 ASP ILE ASN TYR TYR ALA SER GLU PRO 0.451613 0.782609
81 ALA LEU LYS ILE ASP ASN MET ASP 0.45 0.766667
82 GLN ALA SER GLN GLU VAL LYS ASN TRP 0.449367 0.809524
83 SER VAL TYR ASP PHE PHE VAL TRP LEU 0.447368 0.765625
84 ASP SEP TYR GLU VAL LEU ASP LEU 0.447368 0.75
85 GLY GLY LYS LYS LYS TYR GLN LEU 0.445255 0.859649
86 ASP ILE ASN TYR TYR THR SER GLU PRO 0.445161 0.782609
87 ASP ALA ASP GLU TYR LEU 0.443609 0.803571
88 ILE ARG LYS ILE LEU PHE LEU ASP GLY ILE 0.443038 0.71875
89 LEU TYR LEU VAL CYS GLY GLU ARG VAL 0.442308 0.75
90 SER ILE TYR PHE TPO PRO GLU LEU TYR ASP 0.44186 0.710526
91 GLN VAL ASN PHE LEU GLY LYS 0.441379 0.824561
92 LYS ARG TRP ILE ILE LEU GLY LEU ASN LYS 0.440476 0.7
93 ILE LEU MET GLU HIS ILE HIS LYS LEU 0.44 0.686567
94 GLU GLU TYR LEU GLN ALA PHE THR TYR 0.44 0.810345
95 LEU THR THR LYS LEU THR ASN THR ASN ILE 0.439394 0.875
96 GLY GLY LYS LYS LYS TYR LYS LEU 0.439394 0.859649
97 SER GLY ILE PHE LEU GLU THR SER 0.437956 0.857143
98 GLU ASN GLN LYS GLU TYR PHE PHE 0.437956 0.827586
99 ARG VAL ALA GLN LEU GLU GLN VAL TYR ILE 0.437909 0.774194
100 ALA ARG LYS ILE ASP ASN LEU ASP 0.4375 0.758065
101 PHE LEU GLU LYS 0.4375 0.767857
102 SER SER VAL ILE GLY VAL TRP TYR LEU 0.436709 0.796875
103 SER LEU LEU LYS LYS LEU LEU ASP 0.434426 0.839286
104 SER ALA ASN SER PHE THR LEU ILE GLY GLU 0.434211 0.859649
105 GLU ASP GLU ASP PHE GLU ILE LEU SEP LEU 0.433121 0.703125
106 ASP TYR ASN PRO TYR LEU LEU PHE LEU LYS 0.433121 0.768116
107 THR PRO TYR ASP ILE ASN GLN MET LEU 0.432927 0.746479
108 VAL LYS VAL VAL ALA LYS LYS TYR ARG ASN 0.432624 0.822581
109 ALA THR ILE GLY THR ALA MET TYR LYS 0.432258 0.866667
110 ASN LYS ASP LYS GLU TYR TYR VAL ANS 0.432099 0.604651
111 LYS PRO ILE VAL VAL LEU HIS GLY TYR 0.431953 0.728571
112 GLU GLU TYR LEU LYS ALA TRP THR PHE 0.431953 0.8125
113 LYS LEU PRO ALA GLN PHE TYR ILE LEU 0.431138 0.724638
114 THR LYS THR ALA THR ILE ASN ALA SER 0.430657 0.857143
115 ILE LEU ASN ALA MET ILE THR LYS ILE 0.430556 0.8
116 ASP LEU TYR CYS TYR GLU GLN LEU ASN 0.430556 0.847458
117 MET PHE SER ILE ASP ASN ILE LEU ALA 0.430464 0.816667
118 ASP ARG VAL TYR ILE HIS PRO PHE 0.429487 0.75
119 THR ASN GLU TYR TYR VAL 0.428571 0.775862
120 PHE GLU ASP LEU ARG VAL SER SER PHE 0.428571 0.75
121 GLU LYS VAL HIS VAL GLN 0.428571 0.709677
122 PHE GLU ASP LEU ARG VAL LEU SER PHE 0.428571 0.75
123 ALA GLN ASP ILE TYR ARG ALA SER TYR 0.427673 0.8125
124 THR ASN GLU PHE TYR ALA 0.426471 0.793103
125 LYS ARG TRP ILE ILE MET GLY LEU ASN LYS 0.426136 0.662162
126 LEU TYR LEU VAL CYS GLY GLU ARG GLY PHE 0.425926 0.727273
127 LYS TYR LYS 0.425 0.785714
128 HIS LYS LEU VAL GLN LEU LEU THR THR THR 0.424658 0.822581
129 VAL THR THR ASP ILE GLN VAL LYS VAL 0.42446 0.839286
130 LYS VAL LEU PHE LEU ASP GLY 0.42446 0.77193
131 SER LEU LYS LEU MET THR THR VAL 0.424242 0.766667
132 LYS LEU VAL GLN LEU LEU THR THR THR 0.424242 0.821429
133 PHE LEU ARG GLY ARG ALA TYR VAL LEU 0.424051 0.738462
134 LEU ARG ASN GLN SER VAL PHE ASN PHE 0.423841 0.78125
135 CYS THR PHE LYS THR LYS THR ASN 0.423358 0.859649
136 GLY HIS LYS ILE LEU HIS ARG LEU LEU GLN 0.422078 0.666667
137 ILE LEU ASN ALA MET ILE ALA LYS ILE 0.421429 0.733333
138 SER SER ARG LYS GLU TYR TYR ALA 0.421429 0.734375
139 TYR LEU LYS GLU PRO VAL HIS GLY VAL 0.421053 0.714286
140 ARG HIS ARG MLY VAL LEU ARG ASP TYR 0.420732 0.693333
141 LEU GLU LYS ALA ARG GLY SER THR TYR 0.420732 0.857143
142 ASP ARG VAL TYR 0.420635 0.803571
143 LEU TYR LEU VAL CYS GLY GLU ARG GLY 0.420382 0.75
144 ALA SER ASN GLU ASN ILE GLU THR MET 0.42029 0.783333
145 ALA VAL TYR ASN PHE ALA THR MET 0.418919 0.774194
146 ALA MET TYR LYS 0.418605 0.766667
147 VAL ASN ASP ILE PHE GLU ALA ILE 0.417808 0.785714
148 LYS GLN TRP LEU VAL TRP LEU PHE LEU 0.417722 0.703125
149 GLY LEU TYR ALA SER LYS LEU ALA 0.417266 0.894737
150 SER PHE PHE GLU ASP ASN PHE VAL PRO GLU 0.417219 0.724638
151 LYS LEU VAL ALA LEU GLY ILE ASN ALA VAL 0.416667 0.77193
152 PRO ALA ILE LEU TYR ALA LEU LEU SER SER 0.416107 0.868852
153 ACE VAL LYS GLU SER LEU VAL 0.415385 0.803571
154 GLY ALA ALA ARG ALA GLU VAL TYR LEU ARG 0.415094 0.777778
155 ALA ILE PHE GLN SER SER MET THR LYS 0.414474 0.85
156 GLY ASN TYR SER PHE TYR ALA LEU 0.414286 0.847458
157 ASP PHE GLU LYS GLU GLY TYR SER LEU 0.414013 0.915254
158 GLN ALA SER GLN ASP VAL LYS ASN TRP 0.41358 0.809524
159 ARG ARG GLU VAL HIS THR TYR TYR 0.4125 0.753623
160 HIS LYS ILE LEU HIS ARG LEU LEU GLN ASP 0.411043 0.691176
161 ASN ALA LEU LEU ARG TYR LEU LEU ASP 0.410959 0.822581
162 SER ARG TYR TRP ALA ILE ARG THR ARG 0.410714 0.742857
163 GLY GLY ARG LYS LYS TYR LYS LEU 0.409722 0.777778
164 GLY GLY LYS LYS ARG TYR LYS LEU 0.409722 0.777778
165 GLY GLY LYS LYS LYS TYR ARG LEU 0.409722 0.777778
166 LYS PRO PHE PTR VAL ASN VAL GLU PHE 0.409357 0.671053
167 GLU VAL TYR GLU SER 0.409091 0.821429
168 SER LEU LEU MET TRP ILE THR GLN SER 0.408805 0.746269
169 GLY SER TYR LEU VAL THR SER VAL 0.408759 0.859649
170 ALA GLU THR PHE TYR VAL ASP GLY 0.408451 0.793103
171 THR PHE LYS LYS THR ASN 0.407407 0.875
172 LEU PRO PHE ASP LYS SER THR ILE MET 0.406977 0.732394
173 ACE SER HIS VAL ALA VAL GLU ASN ALA LEU 0.406667 0.761905
174 ILE LEU ALA LYS PHE LEU HIS GLU LEU 0.406452 0.746032
175 GLU LEU ASP LYS TRP ALA ASN 0.406452 0.761905
176 GLY ALA GLU VAL PHE TYR VAL ASP GLY ALA 0.405405 0.766667
177 CYS ASP PTR ALA ASN PHE LYS 0.404762 0.767857
178 ASP ASN ARG LEU GLY LEU VAL TYR GLN PHE 0.404412 0.741379
179 LYS MET ASN THR GLN PHE THR ALA VAL 0.403846 0.85
180 GLN ILE MET TYR ASN TYR PRO ALA MET 0.403614 0.69863
181 THR SER ASN LEU GLN GLU GLN ILE GLY TRP 0.403614 0.8125
182 SER LEU LEU MET TRP ILE THR GLN LEU 0.402516 0.746269
183 BE2 GLU PTR ILE ASN GLN NH2 0.401316 0.671429
184 LYS LEU TYR GLN ASN PRO THR THR TYR ILE 0.4 0.782609
185 GLU LEU ASP LYS TRP ALA SER 0.4 0.777778
186 SER LEU ALA ASN THR VAL ALA THR LEU 0.4 0.767857
Similar Ligands (3D)
Ligand no: 1; Ligand: SER LEU ASN TYR ILE ILE LYS VAL LYS GLU; 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 : 1H6W; Ligand: SER LEU ASN TYR ILE ILE LYS VAL LYS GLU; 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: 1h6w.bio1) has 29 residues
No: Leader PDB Ligand Sequence Similarity
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