Receptor
PDB id Resolution Class Description Source Keywords
2Z3N 2.5 Å EC: 2.3.2.6 COMPLEX STRUCTURE OF LF-TRANSFERASE AND PEPTIDE B ESCHERICHIA COLI LF-TRANSFERASE
Ref.: PROTEIN-BASED PEPTIDE-BOND FORMATION BY AMINOACYL-TRNA PROTEIN TRANSFERASE NATURE V. 449 867 2007
Ligand
Ligand Chain:Residue Validity Ligand Warnings Binding Data NGL Viewer Molecular Weight (Da) Formula SMILES
PHE ARG TYR LEU GLY C:301;
D:401;
Valid;
Valid;
none;
none;
submit data
655.777 n/a O=C([...
TAR A:501;
B:502;
Invalid;
Invalid;
none;
none;
submit data
150.087 C4 H6 O6 [C@H]...
View in 3D viewer
90% Homology Family
Leader
PDB id Resolution Class Description Source Keywords
2Z3N 2.5 Å EC: 2.3.2.6 COMPLEX STRUCTURE OF LF-TRANSFERASE AND PEPTIDE B ESCHERICHIA COLI LF-TRANSFERASE
Ref.: PROTEIN-BASED PEPTIDE-BOND FORMATION BY AMINOACYL-TRNA PROTEIN TRANSFERASE NATURE V. 449 867 2007
Members (1)
No: PDB id Binding Data Representative ligand Formula Smiles
The Class containing this family consists of a total of 1 families.
1 2Z3N - PHE ARG TYR LEU GLY 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 1 families.
1 2Z3N - PHE ARG TYR LEU GLY 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 1 families.
1 2Z3N - PHE ARG TYR LEU GLY n/a n/a
Polypharmacology
Similar Ligands
Ligand no: 1; Ligand: PHE ARG TYR LEU GLY; Similar ligands found: 178
No: Ligand ECFP6 Tc MDL keys Tc
1 PHE ARG TYR LEU GLY 1 1
2 TYR GLU LEU ASP GLU LYS PHE ASP ARG LEU 0.669492 0.916667
3 PHE TYR ARG ALA LEU MET 0.657895 0.9
4 PHE LEU ARG GLY ARG ALA TYR GLY LEU 0.641026 0.982456
5 PHE LEU ARG GLY ARG ALA TYR VAL LEU 0.603175 0.982456
6 PHE TYR ARG TYR GLY PHE VAL ALA ASN PHE 0.588235 0.866667
7 SER ASP TYR GLN ARG LEU 0.587156 0.929825
8 PHE ARG SER LYS GLY GLU GLU LEU PHE THR 0.573643 0.83871
9 LEU TYR LEU VAL CYS GLY GLU ARG GLY 0.571429 0.931035
10 LEU TYR LEU VAL CYS GLY GLU ARG GLY PHE 0.568182 0.965517
11 PHE LEU SER TYR LYS 0.563636 0.770492
12 GLU LEU ARG ARG LYS MET MET TYR MET 0.554622 0.84127
13 SER SER LEU GLU ASN PHE ARG ALA TYR VAL 0.551471 0.887097
14 PHE LEU ALA TYR LYS 0.54955 0.807018
15 LEU TYR LEU VAL CYS GLY GLU ARG VAL 0.542636 0.931035
16 GLY GLY LYS LYS ARG TYR LYS LEU 0.53913 0.931035
17 GLY GLY ARG LYS LYS TYR LYS LEU 0.53913 0.931035
18 GLY GLY LYS LYS LYS TYR ARG LEU 0.53913 0.931035
19 ASP ASP LEU TYR GLY 0.538462 0.775862
20 ARG GLY TYR LEU TYR GLN GLY LEU 0.533333 1
21 ARG ARG LEU ILE PHE NH2 0.530973 0.775862
22 SER SER ARG LYS GLU TYR TYR ALA 0.522124 0.913793
23 ARG ARG ILE TYR ASP LEU ILE GLU LEU 0.51938 0.883333
24 TYR GLY GLY PHE LEU 0.518182 0.824561
25 ALA ARG THR GLU LEU TYR ARG SER LEU 0.515873 0.854839
26 GLU ASN LEU TYR PHE GLN 0.513043 0.779661
27 GLU GLU ASN LEU LEU ASP PHE VAL ARG PHE 0.507692 0.85
28 SER GLU ILE GLU PHE ALA ARG LEU 0.503937 0.803279
29 SER GLU LEU GLU ILE LYS ARG TYR 0.5 0.84127
30 LYS VAL LEU PHE LEU ASP GLY 0.5 0.724138
31 TYR GLN PHE 0.5 0.732143
32 GLU THR PHE TYR VAL ASP GLY 0.495868 0.783333
33 ARG ARG LEU LEU ARG GLY HIS ASN GLN TYR 0.489209 0.833333
34 GLU LEU LYS ARG LYS MET ILE TYR MET 0.488722 0.84127
35 GLU GLU TYR LEU GLN ALA PHE THR TYR 0.488372 0.779661
36 VAL LYS VAL VAL ALA LYS LYS TYR ARG ASN 0.487395 0.852459
37 THR ASN GLU PHE TYR PHE 0.486239 0.706897
38 ILE LEU GLY LYS PHE LEU HIS ARG LEU 0.485294 0.784615
39 LEU LEU TYR GLY PHE VAL ASN TYR VAL 0.484375 0.813559
40 GLU GLN TYR LYS PHE TYR SER VAL 0.483607 0.774194
41 GLU ASN GLN LYS GLU TYR PHE PHE 0.483051 0.733333
42 SER SER ILE GLU PHE ALA ARG LEU 0.480916 0.790323
43 GLU GLU PHE GLY ARG ALA PHE SER PHE 0.476923 0.816667
44 ARG GLY TYR VAL TYR GLN GLY LEU 0.476562 1
45 GLY ASN PHE LEU GLN SER ARG 0.47619 0.806452
46 ARG VAL ALA GLN LEU GLU GLN VAL TYR ILE 0.473684 0.929825
47 ARG PHE MET ASP TYR TRP GLU GLY LEU 0.473333 0.835821
48 ILE ARG LYS ILE LEU PHE LEU ASP GLY ILE 0.471014 0.803279
49 THR GLU ASN LEU TYR PHE GLN SER GLY THR 0.470588 0.806452
50 SER SER LEU GLU ASN PHE ALA ALA TYR VAL 0.470149 0.758065
51 PHE GLN TRP MET GLY TYR GLU LEU TRP 0.469388 0.746269
52 SER ARG ILE ARG ILE ARG GLY TYR VAL ARG 0.469231 0.857143
53 ARG TYR GLY PHE VAL ALA ASN PHE 0.466165 0.932203
54 LEU LEU TYR GLY PHE VAL ASN TYR ILE 0.466165 0.8
55 GLU ASN PRO THR TYR LYS PHE PHE GLU GLN 0.462185 0.737705
56 THR TYR LYS PHE PHE GLU GLN 0.462185 0.737705
57 DTY ILE ARG LEU LPD 0.461538 0.764706
58 TYR GLN SER LYS LEU 0.46087 0.770492
59 ASP ASN ARG LEU GLY LEU VAL TYR GLN PHE 0.458716 0.785714
60 GLU LEU LYS TPO GLU ARG TYR 0.458647 0.779412
61 ARG ARG PHE AIB ALA MET LEU ALA 0.458015 0.734375
62 GLU LEU ASN ARG LYS MET ILE TYR MET 0.457746 0.80303
63 GLY ALA ALA ARG ALA GLU VAL TYR LEU ARG 0.456522 0.898305
64 PHE LEU GLU LYS 0.454545 0.701754
65 ARG ARG ARG TRP ARG ARG LEU THR VAL 0.453846 0.761194
66 ACE GLU ASN LEU TYR PHE GLN SER GLY THR 0.453125 0.766667
67 TYR GLY GLY PHE MET 0.452991 0.754098
68 VAL ALA PHE ARG SER 0.452991 0.793103
69 ALA TYR ARG 0.45283 0.857143
70 TYR HIS SEP VAL VAL ARG TYR ALA 0.450704 0.702703
71 ALA GLN PHE SER ALA SER ALA SER ARG 0.45 0.770492
72 GLU THR VAL ARG PHE GLN SER ASP 0.448529 0.803279
73 ALA LYS PHE ARG HIS ASP 0.448 0.723077
74 ARG ARG LEU PRO ILE PHE SER ARG LEU 0.447552 0.662162
75 LEU GLU PHE GLN GLY 0.447368 0.767857
76 SER GLU ASP GLU PHE TYR ASP ALA LEU SER 0.44697 0.783333
77 PHQ LEU VAL ARG TYR 0.446154 0.9
78 ACE PHE LYS PHE TA2 ALA LEU ARG NH2 0.445255 0.793651
79 ASN ARG LEU LEU LEU THR GLY 0.444444 0.783333
80 LEU GLU LYS ALA ARG GLY SER THR TYR 0.444444 0.857143
81 GLY ARG PHE GLN VAL THR 0.444444 0.821429
82 ASP ALA GLU PHE ARG HIS ASP 0.444444 0.734375
83 ASP ALA GLU PHE ARG HIS ASP SER 0.443609 0.734375
84 GLY GLY LYS LYS LYS TYR LYS LEU 0.443478 0.810345
85 LEU GLY TYR GLY PHE VAL ASN TYR ILE 0.442748 0.8
86 ASN TYR THR PRO GLY PRO GLY THR ARG PHE 0.441558 0.739726
87 THR ASN GLU TYR TYR VAL 0.441441 0.758621
88 ALA THR VAL ARG THR TYR SER CYS 0.440945 0.822581
89 THR ASN GLU TYR LYS VAL 0.440678 0.762712
90 SER GLN TYR TYR TYR ASN SER LEU 0.440678 0.758065
91 TYR LEU PHE VAL GLN ARG ASP SER LYS GLU 0.44 0.678571
92 ARG ILE PRO SER TYR ARG TYR ARG TYR 0.439716 0.716216
93 ARG PRO GLY ASN PHE LEU GLN ASN ARG PRO 0.438462 0.79661
94 ASN ARG LEU MET LEU THR GLY 0.438017 0.723077
95 GLY GLY LYS LYS LYS TYR GLN LEU 0.438017 0.827586
96 ARG MET PHE PRO ASN ALA PRO TYR LEU 0.437909 0.727273
97 PHE GLU ALA ILE PRO ALA GLU TYR LEU 0.4375 0.705882
98 ILE GLY PRO GLY ARG ALA PHE TYR ALA 0.436242 0.808824
99 ASP PHE GLU ASP TYR GLU PHE ASP 0.435897 0.706897
100 PTR LEU ARG VAL ALA 0.435484 0.796875
101 THR PRO ASP TYR PHE LEU 0.433333 0.774194
102 THR LYS ASN TYR LYS GLN PHE SER VAL 0.433071 0.761905
103 NSX 0.431818 0.847458
104 ASP ARG VAL TYR ILE HIS PRO PHE 0.43125 0.777778
105 THR LEU MET THR GLY GLN LEU GLY LEU PHE 0.431034 0.75
106 ASN PHE ASP ASN PRO VAL TYR ARG LYS THR 0.43038 0.753425
107 ASN TYR THR PRO GLY PRO GLY ILE ARG PHE 0.43038 0.753425
108 GLU THR LEU LEU ASP LEU ASP PHE LEU GLU 0.429825 0.637931
109 THR ASN GLU PHE TYR ALA 0.429752 0.704918
110 ALA THR ARG ASN PHE SER GLY 0.429688 0.774194
111 GLU GLU TYR LEU LYS ALA TRP THR PHE 0.42953 0.701493
112 GLU LEU ASP LYS TYR ALA SER 0.428571 0.754098
113 LEU LEU PHE GLY PHE PRO VAL TYR VAL 0.427586 0.731343
114 LEU LEU PHE GLY TYR PRO VAL TYR VAL 0.427586 0.731343
115 THR PHE GLN ALA PSA LEU ARG GLU 0.427586 0.868852
116 GLU ARG GLU SEP GLU PHE ASP ILE GLU ASP 0.426573 0.681159
117 BP4 CYS DAR TYR PEA 0.424242 0.864407
118 ILE GLY PRO GLY ARG ALA PHE TYR THR ILE 0.424051 0.774648
119 MET LEU TRP GLY TYR LEU GLN TYR VAL 0.423611 0.757576
120 ARG TYR PRO LEU THR PHE GLY TRP 0.423313 0.767123
121 GLY ALA GLU VAL PHE TYR VAL ASP GLY ALA 0.423077 0.810345
122 SER ARG TYR TRP ALA ILE ARG THR ARG 0.422819 0.768116
123 LEU LEU PHE GLY LYS PRO VAL TYR VAL 0.422819 0.720588
124 ASP ASP MET GLY PHE GLY LEU PHE ASP 0.422414 0.736842
125 ASP ASP ASP MET GLY PHE GLY LEU PHE ASP 0.422414 0.736842
126 GLY ALA ASP ILE PHE TYR LEU ASP GLY ALA 0.421875 0.775862
127 ACE ARG ARG B3L MEA NH2 0.421488 0.723077
128 ARG ARG ARG ARG SER TRP TYR 0.419847 0.720588
129 ILE LEU ALA LYS PHE LEU HIS ARG LEU 0.41958 0.723077
130 ARG VAL LEU PHE GLU ALA MET 0.419118 0.774194
131 ASP LEU TYR CYS TYR GLU GLN LEU ASN 0.418605 0.786885
132 ARG GLN ALA ASN PHE LEU GLY LYS 0.418033 0.683333
133 ARG ILE PHE SER 0.416667 0.779661
134 ARG TYR PRO LEU THR LEU GLY TRP CYS PHE 0.416185 0.746667
135 SER SER TYR ARG ARG PRO VAL GLY ILE 0.416107 0.716216
136 ASN ALA LEU LEU ARG TYR LEU LEU ASP 0.415254 0.694915
137 ARG HIS ARG MLZ VAL LEU ARG ASP ASN TYR 0.414474 0.760563
138 SER ILE ILE GLY PHE GLU LYS LEU 0.413534 0.693548
139 LEU TYR ALA SER PRO GLN LEU GLU GLY PHE 0.412903 0.714286
140 ALA ARG LYS LEU ASP 0.412844 0.762712
141 PHE LEU THR GLY ILE GLY ILE ILE THR VAL 0.412698 0.672131
142 ARG HIS ARG MLY VAL LEU ARG ASP TYR 0.412162 0.739726
143 PHE LEU TRP GLY PRO ARG ALA LEU VAL 0.411392 0.742857
144 LYS ALA LEU TYR ASN PHE ALA THR MET 0.411348 0.727273
145 ALA ALA SER LEU TYR GLU LYS LYS ALA ALA 0.410853 0.741935
146 PHE GLU ALA ASN GLY ASN LEU ILE 0.410448 0.704918
147 ACE PHE ALA TYR M3L SER NH2 0.409449 0.657143
148 SER ILE ILE ASN PHE GLU LYS LEU 0.409091 0.671875
149 GLY ALA GLN THR PHE TYR VAL ASP GLY ALA 0.409091 0.8
150 LEU PHE GLY TYR PRO VAL TYR VAL 0.408451 0.731343
151 ASP ALA ASP GLU TYR LEU 0.408333 0.724138
152 ARG PRO GLY ASN PHE LEU GLN SER ARG LEU 0.407643 0.653333
153 PRO LEU GLU PSA ARG LEU 0.407143 0.784615
154 GLY VAL TYR ASP GLY ARG GLU HIS THR VAL 0.406667 0.80597
155 TYR MET PHE PRO ASN ALA PRO TYR LEU 0.406667 0.636364
156 GLY ASN TYR SER PHE TYR ALA LEU 0.404762 0.758065
157 LEU ASP GLU GLU THR GLY GLU PHE LEU 0.40458 0.733333
158 ALA ARG THR MLY GLN THR ALA ARG TYR 0.404412 0.768116
159 GLY ALA GLU THR PHE TYR VAL ASP GLY ALA 0.404412 0.770492
160 GLY LEU MET TRP LEU SER TYR PHE VAL 0.40411 0.685714
161 LYS TYR LYS 0.403846 0.689655
162 ALA LEU ASP LEU PHE 0.403846 0.614035
163 PCA PHE ARG HIS ASP SER GLY TYR GLU VAL 0.403614 0.808824
164 ASP PHE GLU GLU ILE 0.403509 0.637931
165 ARG LEU GLN ARG ARG ARG GLU THR GLN VAL 0.403226 0.770492
166 ARG LEU TRP SER 0.403226 0.78125
167 SER VAL TYR ASP PHE PHE VAL TRP LEU 0.402878 0.671642
168 SER LEU PHE ASN THR VAL ALA THR LEU TYR 0.402878 0.709677
169 ALA ILE MET PRO ALA ARG PHE TYR PRO LYS 0.402439 0.72973
170 ALA GLU THR PHE TYR VAL ASP GLY 0.401575 0.716667
171 ARG ABA PHE ILE PHE ALA ASN ILE 0.401515 0.816667
172 GLN VAL ASN PHE LEU GLY LYS 0.401515 0.704918
173 LYS LEU PRO ALA GLN PHE TYR ILE LEU 0.401316 0.710145
174 VAL MET ALA PRO ARG THR LEU PHE LEU 0.401316 0.657895
175 TYR GLN PHE GLY PRO ASP PHE PRO ILE ALA 0.401274 0.690141
176 ARG LEU TYR GLN ASN PRO THR THR TYR ILE 0.401274 0.743243
177 GLY ARG PHE ALA ALA ALA ILE ALA LYS 0.4 0.813559
178 ACE ALC ARG ALA MET CY1 SER LEU NH2 0.4 0.691176
Similar Binding Sites (Proteins are less than 50% similar to leader)
Pocket No.: 1; Query (leader) PDB : 2Z3N; Ligand: PHE ARG TYR LEU GLY; Similar sites found: 1
This union binding pocket(no: 1) in the query (biounit: 2z3n.bio1) has 21 residues
No: Leader PDB Ligand P-value (APoc) PS_Score (APoc) Sequence Similarity
1 4DZ1 DAL 0.009738 0.42407 5.01931
Pocket No.: 2; Query (leader) PDB : 2Z3N; Ligand: PHE ARG TYR LEU GLY; Similar sites found: 2
This union binding pocket(no: 2) in the query (biounit: 2z3n.bio1) has 23 residues
No: Leader PDB Ligand P-value (APoc) PS_Score (APoc) Sequence Similarity
1 2XG5 EC5 0.02353 0.4077 2.75229
2 2XG5 EC2 0.02353 0.4077 2.75229
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