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(N...
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 (2D)
Ligand no: 1; Ligand: PHE ARG TYR LEU GLY; Similar ligands found: 169
No: Ligand ECFP6 Tc MDL keys Tc
1 PHE ARG TYR LEU GLY 1 1
2 SER LEU ARG PHE LEU TYR GLU GLY 0.675439 0.933333
3 PHE TYR ARG ALA LEU MET 0.675439 0.9
4 TYR GLU LEU ASP GLU LYS PHE ASP ARG LEU 0.672269 0.916667
5 PHE TYR ARG TYR GLY PHE VAL ALA ASN PHE 0.663366 0.875
6 PHE LEU ARG GLY ARG ALA TYR GLY LEU 0.649573 0.982456
7 PHE LEU ARG GLY ARG ALA TYR VAL LEU 0.611111 0.982456
8 ASN ALA LEU LEU ARG TYR LEU LEU ASP 0.6 0.883333
9 LEU TYR LEU VAL CYS GLY GLU ARG GLY 0.582677 0.931035
10 PHE GLU ASP LEU ARG LEU LEU SER PHE 0.579832 0.836066
11 LEU TYR LEU VAL CYS GLY GLU ARG GLY PHE 0.571429 0.965517
12 SER ASP TYR GLN ARG LEU 0.558559 0.929825
13 SER SER LEU GLU ASN PHE ARG ALA TYR VAL 0.554745 0.887097
14 PHE LEU SER TYR LYS 0.553571 0.786885
15 GLU LEU ARG ARG LYS MET MET TYR MET 0.552846 0.84127
16 GLY GLY ARG LYS LYS TYR LYS LEU 0.547009 0.931035
17 GLY GLY LYS LYS ARG TYR LYS LEU 0.547009 0.931035
18 GLY GLY LYS LYS LYS TYR ARG LEU 0.547009 0.931035
19 ARG GLY TYR LEU TYR GLN GLY LEU 0.545455 1
20 PHE LEU ALA TYR LYS 0.539823 0.842105
21 LEU TYR LEU VAL CYS GLY GLU ARG VAL 0.537879 0.931035
22 ARG ARG LEU ILE PHE NH2 0.535714 0.775862
23 PHE GLU ASP LEU ARG VAL SER SER PHE 0.534884 0.836066
24 PHE GLU ASP LEU ARG VAL LEU SER PHE 0.534884 0.836066
25 ARG ARG ILE TYR ASP LEU ILE GLU LEU 0.534884 0.883333
26 ALA ARG THR GLU LEU TYR ARG SER LEU 0.531746 0.854839
27 TYR GLY GLY PHE LEU 0.518182 0.842105
28 ASP ALA GLU PHE ARG HIS ASP 0.516949 0.807018
29 SER SER ARG LYS GLU TYR TYR ALA 0.512821 0.913793
30 SER GLU ILE GLU PHE ALA ARG LEU 0.507812 0.803279
31 GLU GLU ASN LEU LEU ASP PHE VAL ARG PHE 0.507576 0.85
32 PHE ARG SER LYS GLY GLU GLU LEU PHE THR 0.504425 0.725806
33 GLU ASN LEU TYR PHE GLN 0.504274 0.779661
34 ILE LEU GLY LYS PHE LEU HIS ARG LEU 0.503704 0.784615
35 SER GLU LEU GLU ILE LYS ARG TYR 0.5 0.84127
36 ARG ARG LEU LEU ARG GLY HIS ASN GLN TYR 0.5 0.833333
37 GLY ASN PHE LEU GLN SER ARG 0.496 0.806452
38 ASN ARG LEU LEU LEU THR GLY 0.495413 0.770492
39 ILE ARG LYS ILE LEU PHE LEU ASP GLY ILE 0.492754 0.803279
40 GLU LEU LYS ARG LYS MET ILE TYR MET 0.492647 0.84127
41 TYR GLN PHE 0.490196 0.732143
42 VAL LYS VAL VAL ALA LYS LYS TYR ARG ASN 0.487603 0.852459
43 SER SER ILE GLU PHE ALA ARG LEU 0.484848 0.790323
44 LEU ARG ASN GLN SER VAL PHE ASN PHE 0.484615 0.83871
45 PHQ LEU VAL ARG TYR 0.483871 0.9
46 GLU GLU PHE GLY ARG ALA PHE SER PHE 0.480916 0.816667
47 ARG GLY TYR VAL TYR GLN GLY LEU 0.476923 1
48 GLU THR PHE TYR VAL ASP GLY 0.47541 0.8
49 GLU LEU ARG SER ARG TYR TRP ALA ILE 0.472973 0.797101
50 BP4 CYS DAR TYR PEA 0.472 0.864407
51 ARG PHE MET ASP TYR TRP GLU GLY LEU 0.470588 0.835821
52 GLU GLU TYR LEU GLN ALA PHE THR TYR 0.469697 0.779661
53 DTY ILE ARG LEU LPD 0.46875 0.764706
54 ARG VAL ALA GLN LEU GLU GLN VAL TYR ILE 0.466667 0.929825
55 LYS VAL LEU PHE LEU ASP GLY 0.466667 0.741379
56 GLU THR VAL ARG PHE GLN SER ASP 0.466165 0.816667
57 ILE GLY PRO GLY ARG ALA PHE TYR ALA 0.465753 0.808824
58 THR GLU ASN LEU TYR PHE GLN SER GLY THR 0.463235 0.806452
59 ALA GLN PHE SER ALA SER ALA SER ARG 0.46281 0.770492
60 ARG THR PHE SER PRO THR TYR GLY LEU 0.462585 0.777778
61 GLU LEU ASN ARG LYS MET ILE TYR MET 0.462069 0.80303
62 SER ARG ILE ARG ILE ARG GLY TYR VAL ARG 0.461538 0.857143
63 GLY ALA ALA ARG ALA GLU VAL TYR LEU ARG 0.460432 0.898305
64 GLU LEU LYS TPO GLU ARG TYR 0.459854 0.779412
65 PHE GLN TRP MET GLY TYR GLU LEU TRP 0.459459 0.746269
66 ARG TYR GLY PHE VAL ALA ASN PHE 0.459259 0.932203
67 ARG ARG PHE AIB ALA MET LEU ALA 0.458647 0.734375
68 ALA TYR ARG 0.457944 0.857143
69 LEU LEU TYR GLY PHE VAL ASN TYR VAL 0.457364 0.813559
70 GLU GLN TYR LYS PHE TYR SER VAL 0.456693 0.774194
71 LEU GLU LYS ALA ARG GLY SER THR TYR 0.455172 0.857143
72 ASN ARG LEU MET LEU THR GLY 0.453782 0.723077
73 ILE GLY PRO GLY ARG ALA PHE TYR THR 0.453333 0.797101
74 ILE GLY PRO GLY ARG ALA PHE TYR VAL 0.453333 0.823529
75 ALA LYS PHE ARG HIS ASP 0.453125 0.723077
76 VAL ALA PHE ARG SER 0.452991 0.793103
77 ACE GLU ASN LEU TYR PHE GLN SER GLY THR 0.452381 0.766667
78 ACE PHE LYS PHE TA2 ALA LEU ARG NH2 0.451852 0.793651
79 TYR HIS SEP VAL VAL ARG TYR ALA 0.450704 0.702703
80 TYR GLY GLY PHE MET 0.449153 0.770492
81 ASP PHE GLU ASP TYR GLU PHE ASP 0.448276 0.716667
82 TYR GLN SER LYS LEU 0.448276 0.770492
83 ASP ALA GLU PHE ARG HIS ASP SER 0.447761 0.734375
84 ALA PHE ARG ILE PRO LEU THR ARG 0.447552 0.684932
85 LEU GLU PHE GLN GLY 0.447368 0.767857
86 PHE LEU GLU LYS 0.446429 0.736842
87 ARG ARG LEU PRO ILE PHE SER ARG LEU 0.444444 0.662162
88 LEU LEU TYR GLY PHE VAL ASN TYR ILE 0.443609 0.8
89 PTR LEU ARG VAL ALA 0.443548 0.796875
90 THR ASN GLU PHE TYR PHE 0.441441 0.694915
91 THR PHE GLN ALA PSA LEU ARG GLU 0.441379 0.868852
92 ALA THR ARG ASN PHE SER GLY 0.440945 0.774194
93 GLU ARG GLU SEP GLU PHE ASP ILE GLU ASP 0.440559 0.681159
94 ARG ARG ARG TRP ARG ARG LEU THR VAL 0.440298 0.761194
95 LYS LEU PHE SER PHE GLY GLY 0.439655 0.693548
96 ASP PHE GLU LYS GLU GLY TYR SER LEU 0.438849 0.793651
97 ARG MET PHE PRO ASN ALA PRO TYR LEU 0.43871 0.727273
98 SER SER LEU GLU ASN PHE ALA ALA TYR VAL 0.437956 0.758065
99 PHE GLU ALA ILE PRO ALA GLU TYR LEU 0.4375 0.720588
100 ARG ARG GLU VAL HIS THR TYR TYR 0.43662 0.80597
101 ILE LEU ALA LYS PHE LEU HIS ARG LEU 0.43662 0.723077
102 GLY GLY LYS LYS LYS TYR LYS LEU 0.435897 0.827586
103 ASN TYR THR PRO GLY PRO GLY THR ARG PHE 0.435897 0.739726
104 ARG ILE PRO SER TYR ARG TYR ARG TYR 0.434783 0.716216
105 HIS LEU TYR PHE SER SEP ASN 0.434783 0.64
106 GLU ASN GLN LYS GLU TYR PHE PHE 0.434426 0.737705
107 ALA GLN ASP ILE TYR ARG ALA SER TYR 0.433566 0.870968
108 THR ASN GLU PHE TYR ALA 0.433333 0.704918
109 ILE GLY PRO GLY ARG ALA PHE TYR THR ILE 0.433121 0.774648
110 ASP ASN ARG LEU GLY LEU VAL TYR GLN PHE 0.432203 0.803571
111 GLY GLY LYS LYS LYS TYR GLN LEU 0.430894 0.827586
112 TYR LEU PHE VAL GLN ARG ASP SER LYS GLU 0.43 0.696429
113 ACE ALA ARG THR GLU VAL TYR NH2 0.429688 0.881356
114 ASN TYR THR PRO GLY PRO GLY ILE ARG PHE 0.427673 0.743243
115 ASP ASP ASP MET GLY PHE GLY LEU PHE ASP 0.426087 0.754386
116 ARG HIS ARG MLY VAL LEU ARG ASP TYR 0.425676 0.739726
117 ASP ARG VAL TYR ILE HIS PRO PHE 0.425532 0.830769
118 SER GLN TYR TYR TYR ASN SER LEU 0.425 0.758065
119 ARG PRO GLY ASN PHE LEU GLN ASN ARG PRO 0.424242 0.79661
120 SER ARG TYR TRP ALA ILE ARG THR ARG 0.423841 0.768116
121 THR LEU MET THR GLY GLN LEU GLY LEU PHE 0.422414 0.75
122 ARG HIS ARG MLZ VAL LEU ARG ASP ASN TYR 0.422078 0.760563
123 LEU GLY TYR GLY PHE VAL ASN TYR ILE 0.421053 0.8
124 ARG PRO PRO ILE PHE ILE ARG ARG LEU 0.42069 0.7
125 ARG ILE PHE SER 0.420168 0.779661
126 ASP TYR ASN PRO TYR LEU LEU PHE LEU LYS 0.41958 0.694444
127 ARG GLN ALA ASN PHE LEU GLY LYS 0.418033 0.683333
128 ACE PHE ALA TYR M3L SER NH2 0.418033 0.661972
129 TYR PHE SER SEP ASN 0.418033 0.608696
130 LEU PRO PHE GLU LEU ARG GLY HIS LEU VAL 0.417722 0.728571
131 GLY ALA ASP ILE PHE TYR LEU ASP GLY ALA 0.417323 0.775862
132 THR PRO ASP TYR PHE LEU 0.416667 0.806452
133 ARG VAL LEU PHE GLU ALA MET 0.416058 0.774194
134 ASP LEU TYR CYS TYR GLU GLN LEU ASN 0.415385 0.786885
135 ACE LEU PHE PHE GLK CF0 GLU 0.412844 0.706897
136 ALA PTR ARG 0.412281 0.75
137 THR LYS ASN TYR LYS GLN PHE SER VAL 0.412214 0.761905
138 ARG ARG ARG ARG TRP ARG GLU ARG GLN 0.412214 0.734375
139 ALA ILE MET PRO ALA ARG PHE TYR PRO LYS 0.412121 0.72973
140 PRO LEU GLU PSA ARG LEU 0.411348 0.784615
141 SER GLY ILE PHE LEU GLU THR SER 0.41129 0.677419
142 DPN PRO DAR CYS NH2 0.41129 0.608696
143 ALA VAL TYR ASP GLY ARG GLU HIS THR VAL 0.410596 0.80597
144 PHE LEU TRP GLY PRO ARG ALA LEU VAL 0.409938 0.742857
145 ARG ARG GLY LEU NH2 0.409524 0.77193
146 SER GLU ASP GLU PHE TYR ASP ALA LEU SER 0.408759 0.8
147 ARG LYS LYS ARG TYR THR VAL VAL GLY ASN 0.408451 0.825397
148 ACE ARG ARG B3L MEA NH2 0.408333 0.723077
149 GLY ASN TYR SER PHE TYR ALA LEU 0.408 0.758065
150 GLU LEU ASP LYS TYR ALA SER 0.407692 0.770492
151 PHE LEU PRO HIS ALY TYR ASP VAL LYS LEU 0.407407 0.680556
152 ARG TYR PRO LEU THR PHE GLY TRP 0.407186 0.767123
153 ARG PRO GLY ASN PHE LEU GLN SER ARG LEU 0.40625 0.662162
154 GLY ARG PHE ALA ALA ALA ILE ALA LYS 0.406015 0.813559
155 HIS LYS ILE LEU HIS ARG LEU LEU GLN ASP 0.405405 0.742424
156 VAL MET ALA PRO ARG THR LEU PHE LEU 0.405229 0.657895
157 ASP ALA ASP GLU TYR LEU 0.404959 0.741379
158 PHE LEU THR GLY ILE GLY ILE ILE THR VAL 0.404762 0.688525
159 ALA ALA SER LEU TYR GLU LYS LYS ALA ALA 0.40458 0.758065
160 GLY ASN CYS PHE SER LYS ARG ARG ALA ALA 0.404412 0.746032
161 PHE GLU ALA ASN GLY ASN LEU ILE 0.402985 0.704918
162 LEU LEU PHE GLY LYS PRO VAL TYR VAL 0.402685 0.724638
163 TYR LEU VAL VAL VAL GLY ALA VAL GLY VAL 0.401639 0.789474
164 DPN PRO DAR DTH NH2 0.401575 0.657143
165 TYR PRO LYS ARG ILE ALA 0.401408 0.753623
166 GLU GLU TYR LEU LYS ALA TRP THR PHE 0.401274 0.731343
167 TYR MET PHE PRO ASN ALA PRO TYR LEU 0.4 0.636364
168 SER SER TYR ARG ARG PRO VAL GLY ILE 0.4 0.716216
169 TYR LEU GLY ALA ASN GLY 0.4 0.75
Similar Ligands (3D)
Ligand no: 1; Ligand: PHE ARG TYR LEU GLY; 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 : 2Z3N; Ligand: PHE ARG TYR LEU GLY; 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: 2z3n.bio1) has 21 residues
No: Leader PDB Ligand Sequence Similarity
Pocket No.: 2; Query (leader) PDB : 2Z3N; Ligand: PHE ARG TYR LEU GLY; Similar sites found with APoc: No similar binding sites found, or similarity not calculated due to duplicate pocket.
This union binding pocket(no: 2) in the query (biounit: 2z3n.bio1) has 23 residues
No: Leader PDB Ligand Sequence Similarity
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