Receptor
PDB id Resolution Class Description Source Keywords
1U9L 1.9 Å NON-ENZYME: TRANSCRIPT_TRANSLATE STRUCTURAL BASIS FOR A NUSA- PROTEIN N INTERACTION ESCHERICHIA COLI ESCHERICHIA COLI NUSA PHAGE LAMBDA PROTEIN N REGULATION OF RNA BINDING TRANSCRIPTION ANTITERMINATION X-RAY CRYSTALLOGRAPHY RNA BINDING PROTEIN
Ref.: STRUCTURAL BASIS FOR THE INTERACTION OF ESCHERICHIA COLI NUSA WITH PROTEIN N OF PHAGE LAMBDA PROC.NATL.ACAD.SCI.USA V. 101 13762 2004
Ligand
Ligand Chain:Residue Validity Ligand Warnings Binding Data NGL Viewer Molecular Weight (Da) Formula SMILES
ASN ARG PRO ILE LEU SER LEU C:34;
 Valid;
 none;
 Kd = 3.5 nM
812.991 n/a O=C([...
AU A:1001;
 Invalid;
 none;
 submit data
196.967 Au [Au+]
View in 3D viewer
90% Homology Family
Leader
PDB id Resolution Class Description Source Keywords
1U9L 1.9 Å NON-ENZYME: TRANSCRIPT_TRANSLATE STRUCTURAL BASIS FOR A NUSA- PROTEIN N INTERACTION ESCHERICHIA COLI ESCHERICHIA COLI NUSA PHAGE LAMBDA PROTEIN N REGULATION OF RNA BINDING TRANSCRIPTION ANTITERMINATION X-RAY CRYSTALLOGRAPHY RNA BINDING PROTEIN
Ref.: STRUCTURAL BASIS FOR THE INTERACTION OF ESCHERICHIA COLI NUSA WITH PROTEIN N OF PHAGE LAMBDA PROC.NATL.ACAD.SCI.USA V. 101 13762 2004
Members (1)
No: PDB id Binding Data Representative ligand Formula Smiles
The Class containing this family consists of a total of 291 families.
1 1U9L Kd = 3.5 nM ASN ARG PRO ILE LEU SER LEU 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 247 families.
1 1U9L Kd = 3.5 nM ASN ARG PRO ILE LEU SER LEU 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 209 families.
1 1U9L Kd = 3.5 nM ASN ARG PRO ILE LEU SER LEU n/a n/a
Polypharmacology
Similar Ligands
Ligand no: 1; Ligand: ASN ARG PRO ILE LEU SER LEU; Similar ligands found: 158
No: Ligand ECFP6 Tc MDL keys Tc
1 ASN ARG PRO ILE LEU SER LEU 1 1
2 ARG ARG LEU PRO ILE PHE SER ARG LEU 0.617647 0.927536
3 ALA ASN SER ARG TRP PRO THR THR ARG LEU 0.574324 0.878378
4 ALA ASN SER ARG LEU PRO THR SER ILE ILE 0.573643 0.955224
5 ALA ASN SER ARG TYR PRO THR SER ILE ILE 0.555556 0.902778
6 SER HIS PRO ARG PRO ILE ARG VAL 0.55 0.928571
7 ALA ASN SER ARG ALY PRO THR SER ILE ILE 0.541096 0.928571
8 ALA ASN SER ARG ALA PRO THR SER ILE ILE 0.539568 0.955882
9 ALA LEU PRO HIS ALA ILE LEU ARG LEU 0.537931 0.842857
10 CYS THR PRO SER ARG 0.536585 0.882353
11 ARG GLN PRO ALA LYS ALA PRO LEU LEU 0.536232 0.855072
12 ALA MET ALA PRO ARG THR LEU LEU LEU 0.533333 0.835616
13 ARG PRO ARG PRO ASP ASP LEU GLU ILE 0.532847 0.897059
14 ALA ASN SER ARG VAL PRO THR SER ILE ILE 0.525926 0.955224
15 ASN PRO ARG ALA MET GLN ALA LEU LEU 0.521739 0.859155
16 PHE ASN ARG PRO VAL 0.519084 0.882353
17 SER ALA PRO ASP THR ARG PRO ALA 0.518519 0.885714
18 ARG PRO GLN VAL PRO LEU ARG PRO MET 0.51773 0.819444
19 GLY LEU LEU GLY SER PRO VAL ARG ALA 0.514706 0.939394
20 VAL MET ALA PRO ARG ALA LEU LEU LEU 0.511111 0.791667
21 ARG LEU PRO ALA LYS ALA PRO LEU LEU 0.510949 0.84058
22 ARG ILE ILE PRO ARG HIS LEU GLN LEU 0.510067 0.871429
23 VAL VAL ARG PRO GLY SER LEU ASP LEU PRO 0.506757 0.941176
24 LYS PRO VAL LEU ARG THR ALA 0.50365 0.897059
25 ALA ASN SER ARG PHE PRO THR SER ILE ILE 0.503311 0.942029
26 ASP LEU THR ARG PRO 0.5 0.940298
27 ALA PRO ASP THR ARG PRO ALA PRO 0.5 0.871429
28 PRO ARG ARG PRO VAL ILE MET ARG ARG 0.496454 0.791667
29 ARG PRO PRO ILE PHE ILE ARG ARG LEU 0.493151 0.842857
30 ALA ASN SER ARG HIS PRO THR SER ILE ILE 0.493056 0.901408
31 SER PRO HIS ASN PRO ILE SER ASP VAL ASP 0.492063 0.895522
32 LEU ASN PHE PRO ILE SER PRO 0.488722 0.857143
33 VAL PRO LEU ARG PRO MET THR TYR 0.486667 0.805195
34 ARG PRO LYS ARG ILE ALA 0.485075 0.865672
35 ASN LEU VAL PRO SER VAL ALA THR VAL 0.485075 0.880597
36 ALA PRO ASP THR ARG PRO 0.480916 0.871429
37 PRO ARG PRO ILE LEU LEU PRO TRP ARG NH2 0.477124 0.780822
38 GLU LYS PRO SER SER SER 0.47541 0.80597
39 SER ALA GLU PRO VAL PRO LEU GLN LEU 0.474453 0.852941
40 ARG GLN ALA SEP ILE GLU LEU PRO SER MET 0.472727 0.844156
41 ASN LEU VAL PRO THR VAL ALA THR VAL 0.466165 0.850746
42 VAL MET ALA PRO ARG THR LEU PHE LEU 0.464516 0.813333
43 1IP CYS PHE SER LYS PRO ARG 0.463576 0.873239
44 PRO PRO ARG PRO ILE TYR ASN ARG ASN 0.463576 0.849315
45 PRO SER ILE ASP ARG SER THR LYS PRO 0.463576 0.927536
46 GLU ARG THR ILE PRO ILE THR ARG GLU 0.463235 0.897059
47 ASN LEU VAL PRO VAL VAL ALA THR VAL 0.462687 0.850746
48 SER PRO LYS ARG ILE ALA 0.462121 0.895522
49 GLY GLU ARG THR ILE PRO ILE THR ARG GLU 0.461538 0.926471
50 ALA ASN SER ARG TRP PRO ALY SER ILE ILE 0.461538 0.866667
51 SER SER TYR ARG ARG PRO VAL GLY ILE 0.460526 0.876712
52 ALA PHE ARG ILE PRO LEU THR ARG 0.46 0.9
53 ARG MET PHE PRO ASN ALA PRO TYR LEU 0.459627 0.7875
54 GLN PRO PRO VAL PRO PRO GLN ARG PRO MET 0.458904 0.819444
55 THR PRO ARG ARG SER MLZ SER ALA 0.458647 0.847222
56 ALA ARG MLZ SER ALA PRO ALA THR 0.457746 0.861111
57 SER ASP ILE LEU PHE PRO ALA ASP SER 0.457746 0.867647
58 LEU ASP PRO ARG 0.456693 0.893939
59 VAL ARG SER ARG ARG ABA LEU ARG LEU 0.455285 0.761194
60 TYR PRO LYS ARG ILE ALA 0.455172 0.794521
61 PHE TYR ALA PRO GLU PRO ILE THR SER LEU 0.455128 0.776316
62 ARG THR PHE SER PRO THR TYR GLY LEU 0.455128 0.864865
63 ARG PRO LYS PRO LEU VAL ASP PRO 0.454545 0.823529
64 PRO LYS ARG PRO THR THR LEU ASN LEU PHE 0.453988 0.887324
65 ARG VAL ALA SER PRO THR SER GLY VAL 0.453901 0.940298
66 LEU GLN ARG VAL LEU SEP ALA PRO PHE 0.453333 0.813333
67 GLY LEU LEU GLY SEP PRO VAL ARG ALA 0.452703 0.861111
68 VAL ARG SER ARG ARG CYS LEU ARG LEU 0.45082 0.735294
69 ARG ARG ARG GLU ARG SER PRO THR ARG 0.450704 0.897059
70 ARG PRO GLY ASN PHE LEU GLN SER ARG PRO 0.450617 0.901408
71 DTY ILE ARG LEU LPD 0.449275 0.805556
72 ARG ILE PRO SER TYR ARG TYR ARG TYR 0.448276 0.826667
73 GLN VAL PRO LEU ARG PRO MET THR TYR LYS 0.447059 0.818182
74 SER LEU SER ARG THR PRO ALA ASP GLY ARG 0.446667 0.911765
75 ALA ASN SER ARG TRP PRO THR SER ALY ILE 0.444444 0.855263
76 GLY ARG PRO ARG THR THR SER PHE ALA GLU 0.443038 0.885714
77 ASP ARG VAL GLU LEU ASN ALA PRO ARG GLN 0.442177 0.897059
78 SER ARG ASP HIS SER ARG THR PRO MET 0.440994 0.853333
79 ASN ARG PRO VAL TYR ILE PRO ARG PRO PRO 0.44 0.808219
80 ASN ARG LEU ILE LEU THR GLY 0.439024 0.712121
81 ASN LEU VAL PRO MET VAL ALA VAL VAL 0.438849 0.771429
82 ASN LEU VAL PRO MET VAL ALA ALA VAL 0.438849 0.771429
83 ILE PRO LEU THR GLU GLU ALA GLU LEU 0.437956 0.823529
84 LEU PRO PHE ASP ARG THR THR ILE MET 0.4375 0.864865
85 ASN LEU VAL PRO GLN VAL ALA THR VAL 0.43662 0.850746
86 GLU PRO GLY GLY SER ARG 0.43609 0.880597
87 LYS ALA PRO ARG ALY GLN LEU ALA THR LYS 0.434783 0.811594
88 ALA ASN SER ARG TRP PRO THR SER FAK ILE 0.434286 0.833333
89 MET CYS PRO ARG MET THR ALA VAL MET 0.434211 0.861111
90 THR LYS PRO ARG 0.433333 0.776119
91 ASN LEU VAL PRO MET VAL ALA THR VAL 0.430556 0.802817
92 PHE PRO ARG PRO TRP LEU HIS GLY LEU 0.430233 0.810811
93 ARG LEU TYR GLN ASN PRO THR THR TYR ILE 0.429448 0.853333
94 DPN PRO DAR ILE NH2 0.428571 0.808824
95 ILE SER PRO ARG THR LEU ASP ALA TRP 0.427746 0.878378
96 3BY PRO LYS ARG ILE ALA 0.426573 0.805556
97 SER PRO ARG LEU PRO LEU LEU GLU SER 0.426471 0.808824
98 5JP PRO LYS ARG ILE ALA 0.426357 0.828571
99 ILE ARG ALA ALA PRO PRO PRO LEU PHE 0.424837 0.830986
100 ARG THR PRO SEP LEU PRO THR 0.423611 0.813333
101 GLY MET PRO ARG GLY ALA 0.423358 0.791667
102 ALA ALA ARG KCR SER ALA PRO ALA 0.422819 0.869565
103 ASN TYR THR PRO GLY PRO GLY ILE ARG PHE 0.422619 0.853333
104 SER SER GLY LYS VAL PRO LEU 0.422222 0.850746
105 ALA ASN SER ARG TRP PRO THR SER 2KK ILE 0.422222 0.822785
106 LYS GLY PRO PRO LEU PRO ARG PRO ARG VAL 0.422222 0.823529
107 MET LEU LEU SER VAL PRO LEU LEU LEU GLY 0.422222 0.8
108 ARG VAL ALA SEP PRO THR SER GLY VAL 0.421053 0.863014
109 THR PRO ARG VAL THR GLY GLY GLY ALA MET 0.421053 0.863014
110 ACE ILE GLU PRO ASJ 0.420635 0.818182
111 SER SER GLY LYS VAL PRO LEU SER 0.42029 0.865672
112 LEU PRO PRO GLU GLU ARG LEU ILE 0.41958 0.867647
113 LEU PRO PHE GLU ARG ALA THR ILE MET 0.419162 0.851351
114 ARG PRO GLY ASN PHE LEU GLN SER ARG LEU 0.419162 0.927536
115 GLN ARG SER THR SEP THR PRO ASN VAL HIS 0.418301 0.863014
116 SER SER CYS PRO LEU SER LYS 0.41791 0.823529
117 THR PRO GLN ASP LEU ASN THR MET LEU 0.417808 0.791667
118 SER MET PRO GLU LEU SER PRO VAL LEU 0.417266 0.805556
119 ALA ASN SER ARG VAL GLN ASP SER ILE ILE 0.417266 0.791045
120 PRO PRO LYS ARG ILE ALA 0.416667 0.838235
121 ALA ILE MET PRO ALA ARG PHE TYR PRO LYS 0.416185 0.746835
122 ARG ARG ALA SEP ALA PRO LEU PRO 0.416107 0.8
123 ALA ASN SER ARG TRP PRO THR SER 2KP ILE 0.415301 0.822785
124 ILE LEU LYS GLU PRO VAL HIS GLY VAL 0.415094 0.785714
125 LYS PRO ILE VAL VAL LEU HIS GLY TYR 0.414634 0.746667
126 ASN ASP TRP LEU LEU PRO SER TYR 0.414634 0.766234
127 SER LEU ILE PRO TPO PRO ASP LYS 0.413333 0.8
128 HIS HIS ALA SER PRO ARG LYS 0.412903 0.816901
129 DPN PRO ARG 0.412698 0.764706
130 ARG PHE PRO LEU THR PHE GLY TRP 0.411765 0.826667
131 MET SER LEU PRO GLY ARG TRP LYS PRO LYS 0.411111 0.831169
132 GLN ASN TYR PRO ILE VAL GLN 0.410959 0.777778
133 ALA VAL PRO ILE ALA GLN 0.410853 0.787879
134 HIS SER ILE THR TYR LEU LEU PRO VAL 0.409938 0.8
135 PRO GLN ILE ILE ASN ARG PRO GLN ASN 0.409722 0.867647
136 ASN PHE ASP ASN PRO VAL TYR ARG LYS THR 0.409357 0.84
137 GLU LEU PRO LEU VAL LYS ILE 0.408451 0.791045
138 ASN ARG LEU LEU LEU THR GLY 0.408333 0.731343
139 LYS VAL PRO ARG ASN GLN ASP TRP LEU 0.408046 0.849315
140 DPN PRO DAR DTH NH2 0.407407 0.826087
141 VAL PRO PRO PRO ARG PRO PRO PRO PRO GLU 0.407407 0.797101
142 ACE ARG THR PRO SEP LEU PRO THR PIP 0.406667 0.772152
143 LYS ARG ARG ARG HIS PRO SER GLY 0.406667 0.857143
144 LYS LEU THR PRO LEU CYS VAL THR LEU 0.405594 0.811594
145 ALA PRO ASP SER ARG PRO A2G 0.405063 0.805195
146 ACE GLN GLU ARG GLU VAL PRO CYS 0.404255 0.826087
147 LEU LEU CYS SER TPO PRO ASN GLY LEU 0.40411 0.797297
148 SER PRO ILE VAL PRO SER PHE ASP MET 0.403846 0.797297
149 ALA PRO ASP THR ARG PRO A2G 0.403727 0.805195
150 GLU SER ASP PRO ILE VAL ALA GLN TYR 0.402516 0.819444
151 ARG GLN PHE GLY PRO ASP PHE PRO THR ILE 0.402367 0.863014
152 ASN ARG LEU MET LEU THR GLY 0.401515 0.71831
153 GLN ALA SER TPO PRO ARG NIT 0.401235 0.717647
154 ILE PRO ILE 0.4 0.727273
155 ILE PRO ALA TYR GLY VAL LEU THR ILE 0.4 0.791667
156 ARG SEP PRO VAL PHE SER 0.4 0.810811
157 ASN SER THR LEU GLN 0.4 0.641791
158 ASP VAL GLN THR GLY ARG ARG PRO TYR GLU 0.4 0.849315
Similar Binding Sites (Proteins are less than 50% similar to leader)
Pocket No.: 1; Query (leader) PDB : 1U9L; Ligand: ASN ARG PRO ILE LEU SER LEU; 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: 1u9l.bio2) has 11 residues
No: Leader PDB Ligand Sequence Similarity
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