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 = 3.55 uM
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 308 families.
1 1U9L Kd = 3.55 uM 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 266 families.
1 1U9L Kd = 3.55 uM 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 220 families.
1 1U9L Kd = 3.55 uM ASN ARG PRO ILE LEU SER LEU n/a n/a
Polypharmacology
Similar Ligands (2D)
Ligand no: 1; Ligand: ASN ARG PRO ILE LEU SER LEU; Similar ligands found: 155
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 ACE SER LEU ARG PRO ALA PRO LPD 0.554688 0.898551
4 SER HIS PRO ARG PRO ILE ARG VAL 0.55 0.928571
5 ALA ASN SER ARG ALY PRO THR SER ILE ILE 0.541096 0.928571
6 ALA ASN SER ARG ALA PRO THR SER ILE ILE 0.539568 0.955882
7 ALA LEU PRO HIS ALA ILE LEU ARG LEU 0.537931 0.842857
8 ARG GLN PRO ALA LYS ALA PRO LEU LEU 0.536232 0.855072
9 ALA ASN SER ARG LEU PRO THR SER ILE ILE 0.533835 0.955224
10 ALA MET ALA PRO ARG THR LEU LEU LEU 0.533333 0.835616
11 ARG PRO ARG PRO ASP ASP LEU GLU ILE 0.532847 0.897059
12 ASN PRO ARG ALA MET GLN ALA LEU LEU 0.521739 0.859155
13 PHE ASN ARG PRO VAL 0.519084 0.882353
14 SER ALA PRO ASP THR ARG PRO ALA 0.518519 0.885714
15 ARG PRO GLN VAL PRO LEU ARG PRO MET 0.51773 0.819444
16 GLY LEU LEU GLY SER PRO VAL ARG ALA 0.514706 0.939394
17 VAL MET ALA PRO ARG ALA LEU LEU LEU 0.511111 0.791667
18 ARG LEU PRO ALA LYS ALA PRO LEU LEU 0.510949 0.84058
19 ARG ILE ILE PRO ARG HIS LEU GLN LEU 0.510067 0.871429
20 ALA ASN SER ARG VAL PRO THR SER ILE ILE 0.507353 0.955224
21 VAL VAL ARG PRO GLY SER LEU ASP LEU PRO 0.506757 0.941176
22 ALA ASN SER ARG TRP PRO THR THR ARG LEU 0.506579 0.878378
23 LYS PRO VAL LEU ARG THR ALA 0.50365 0.897059
24 ALA ASN SER ARG PHE PRO THR SER ILE ILE 0.503311 0.942029
25 ASP LEU THR ARG PRO 0.5 0.940298
26 PRO ARG ARG PRO VAL ILE MET ARG ARG 0.496454 0.791667
27 ARG PRO PRO ILE PHE ILE ARG ARG LEU 0.493151 0.842857
28 ALA ASN SER ARG TYR PRO THR SER ILE ILE 0.489933 0.902778
29 LEU ASN PHE PRO ILE SER PRO 0.488722 0.857143
30 VAL PRO LEU ARG PRO MET THR TYR 0.486667 0.805195
31 ASN LEU VAL PRO SER VAL ALA THR VAL 0.485075 0.880597
32 ARG PRO LYS ARG ILE ALA 0.485075 0.865672
33 GLU LYS PRO SER SER SER 0.47541 0.80597
34 SER ALA GLU PRO VAL PRO LEU GLN LEU 0.474453 0.852941
35 ARG GLN ALA SEP ILE GLU LEU PRO SER MET 0.472727 0.844156
36 ARG SER LEU SEP ALA PRO GLY ASN 0.471429 0.863014
37 PRO ARG PRO ILE LEU LEU PRO TRP ARG NH2 0.470588 0.780822
38 ASN LEU VAL PRO THR VAL ALA THR VAL 0.466165 0.850746
39 VAL MET ALA PRO ARG THR LEU PHE LEU 0.464516 0.813333
40 PRO PRO ARG PRO ILE TYR ASN ARG ASN 0.463576 0.849315
41 1IP CYS PHE SER LYS PRO ARG 0.463576 0.873239
42 PRO SER ILE ASP ARG SER THR LYS PRO 0.463576 0.927536
43 GLU ARG THR ILE PRO ILE THR ARG GLU 0.463235 0.897059
44 ASN LEU VAL PRO VAL VAL ALA THR VAL 0.462687 0.850746
45 SER PRO LYS ARG ILE ALA 0.462121 0.895522
46 ALA ASN SER ARG TRP PRO ALY SER ILE ILE 0.461538 0.866667
47 GLY GLU ARG THR ILE PRO ILE THR ARG GLU 0.461538 0.926471
48 SER SER TYR ARG ARG PRO VAL GLY ILE 0.460526 0.876712
49 ALA PHE ARG ILE PRO LEU THR ARG 0.46 0.9
50 ARG MET PHE PRO ASN ALA PRO TYR LEU 0.459627 0.7875
51 ALA ASN SER ARG HIS PRO THR SER ILE ILE 0.459459 0.901408
52 GLN PRO PRO VAL PRO PRO GLN ARG PRO MET 0.458904 0.819444
53 THR PRO ARG ARG SER MLZ SER ALA 0.458647 0.847222
54 ALA ARG MLZ SER ALA PRO ALA THR 0.457746 0.861111
55 LEU ASP PRO ARG 0.456693 0.893939
56 VAL ARG SER ARG ARG ABA LEU ARG LEU 0.455285 0.761194
57 TYR PRO LYS ARG ILE ALA 0.455172 0.794521
58 PHE TYR ALA PRO GLU PRO ILE THR SER LEU 0.455128 0.776316
59 ARG THR PHE SER PRO THR TYR GLY LEU 0.455128 0.864865
60 ARG PRO LYS PRO LEU VAL ASP PRO 0.454545 0.823529
61 PRO LYS ARG PRO THR THR LEU ASN LEU PHE 0.453988 0.887324
62 ARG VAL ALA SER PRO THR SER GLY VAL 0.453901 0.940298
63 GLY LEU LEU GLY SEP PRO VAL ARG ALA 0.452703 0.861111
64 MET THR SER ALA ILE GLY ILE LEU PRO VAL 0.452703 0.830986
65 VAL ARG SER ARG ARG CYS LEU ARG LEU 0.45082 0.735294
66 DTY ILE ARG LEU LPD 0.449275 0.805556
67 5JP PRO LYS ARG ILE ALA 0.448529 0.869565
68 ALA PRO ASP THR ARG PRO ALA PRO 0.448529 0.871429
69 ARG ILE PRO SER TYR ARG TYR ARG TYR 0.448276 0.826667
70 GLN VAL PRO LEU ARG PRO MET THR TYR LYS 0.447059 0.818182
71 ALA ASN SER ARG TRP PRO THR SER ALY ILE 0.444444 0.855263
72 ARG SER ALA SEP GLU PRO SER LEU 0.443709 0.876712
73 GLY ARG PRO ARG THR THR SER PHE ALA GLU 0.443038 0.885714
74 SER ARG ASP HIS SER ARG THR PRO MET 0.440994 0.853333
75 ASN ARG LEU ILE LEU THR GLY 0.439024 0.712121
76 ASN LEU VAL PRO MET VAL ALA VAL VAL 0.438849 0.771429
77 ASN LEU VAL PRO MET VAL ALA ALA VAL 0.438849 0.771429
78 ILE PRO LEU THR GLU GLU ALA GLU LEU 0.437956 0.823529
79 LEU PRO PHE ASP ARG THR THR ILE MET 0.4375 0.864865
80 ASN LEU VAL PRO GLN VAL ALA THR VAL 0.43662 0.850746
81 GLU PRO GLY GLY SER ARG 0.43609 0.880597
82 ASP ARG VAL GLU LEU ASN ALA PRO ARG GLN 0.434483 0.897059
83 ASN ARG LEU LEU LEU THR GLY 0.434426 0.761194
84 ALA ASN SER ARG TRP PRO THR SER FAK ILE 0.434286 0.833333
85 MET CYS PRO ARG MET THR ALA VAL MET 0.434211 0.861111
86 GLY ASP CYS PHE SER LYS PRO ARG 0.432258 0.857143
87 THR THR ALA PRO SER LEU SER GLY LYS 0.430556 0.84058
88 ASN LEU VAL PRO MET VAL ALA THR VAL 0.430556 0.802817
89 PHE PRO ARG PRO TRP LEU HIS GLY LEU 0.430233 0.810811
90 ARG LEU TYR GLN ASN PRO THR THR TYR ILE 0.429448 0.853333
91 DPN PRO DAR ILE NH2 0.428571 0.808824
92 ILE SER PRO ARG THR LEU ASP ALA TRP 0.427746 0.878378
93 3BY PRO LYS ARG ILE ALA 0.426573 0.805556
94 ASN ARG PRO VAL TYR ILE PRO ARG PRO PRO 0.424837 0.808219
95 ILE ARG ALA ALA PRO PRO PRO LEU PHE 0.424837 0.830986
96 ARG THR PRO SEP LEU PRO THR 0.423611 0.813333
97 ARG THR PRO SEP LEU PRO THR 49F 0.423611 0.813333
98 ALA ALA ARG KCR SER ALA PRO ALA 0.422819 0.869565
99 ASN TYR THR PRO GLY PRO GLY ILE ARG PHE 0.422619 0.853333
100 LYS GLY PRO PRO LEU PRO ARG PRO ARG VAL 0.422222 0.823529
101 MET LEU LEU SER VAL PRO LEU LEU LEU GLY 0.422222 0.8
102 SER SER GLY LYS VAL PRO LEU 0.422222 0.850746
103 ALA ASN SER ARG TRP PRO THR SER 2KK ILE 0.422222 0.822785
104 ARG VAL ALA SEP PRO THR SER GLY VAL 0.421053 0.863014
105 THR PRO ARG VAL THR GLY GLY GLY ALA MET 0.421053 0.863014
106 ACE ILE GLU PRO ASJ 0.420635 0.818182
107 LEU PRO PRO GLU GLU ARG LEU ILE 0.41958 0.867647
108 ARG PRO GLY ASN PHE LEU GLN SER ARG LEU 0.419162 0.927536
109 LEU PRO PHE GLU ARG ALA THR ILE MET 0.419162 0.851351
110 SER SER CYS PRO LEU SER LYS 0.41791 0.823529
111 THR PRO GLN ASP LEU ASN THR MET LEU 0.417808 0.791667
112 SER MET PRO GLU LEU SER PRO VAL LEU 0.417266 0.805556
113 PRO PRO LYS ARG ILE ALA 0.416667 0.838235
114 ALA ILE MET PRO ALA ARG PHE TYR PRO LYS 0.416185 0.746835
115 ARG ARG ALA SEP ALA PRO LEU PRO 0.416107 0.8
116 LEU GLN ARG VAL LEU SEP ALA PRO PHE 0.415584 0.813333
117 ALA ASN SER ARG TRP PRO THR SER 2KP ILE 0.415301 0.822785
118 ILE LEU LYS GLU PRO VAL HIS GLY VAL 0.415094 0.785714
119 LYS PRO ILE VAL VAL LEU HIS GLY TYR 0.414634 0.746667
120 ASN ASP TRP LEU LEU PRO SER TYR 0.414634 0.766234
121 LYS ALA PRO ARG ALY GLN LEU ALA THR LYS 0.414013 0.885714
122 SER LEU ILE PRO TPO PRO ASP LYS 0.413333 0.8
123 SER SER GLY LYS VAL PRO LEU SER 0.413043 0.865672
124 HIS HIS ALA SER PRO ARG LYS 0.412903 0.816901
125 DPN PRO ARG 0.412698 0.764706
126 ARG SER HIS SEP SER PRO ALA SER LEU GLN 0.411765 0.842105
127 ARG PHE PRO LEU THR PHE GLY TRP 0.411765 0.826667
128 MET SER LEU PRO GLY ARG TRP LYS PRO LYS 0.411111 0.831169
129 ARG ARG ARG GLU ARG SER PRO THR ARG 0.410959 0.897059
130 GLN ASN TYR PRO ILE VAL GLN 0.410959 0.777778
131 ALA VAL PRO ILE ALA GLN 0.410853 0.787879
132 HIS SER ILE THR TYR LEU LEU PRO VAL 0.409938 0.8
133 THR LYS PRO ARG 0.409836 0.776119
134 PRO GLN ILE ILE ASN ARG PRO GLN ASN 0.409722 0.867647
135 GLU LEU PRO LEU VAL LYS ILE 0.408451 0.791045
136 LYS VAL PRO ARG ASN GLN ASP TRP LEU 0.408046 0.849315
137 VAL PRO PRO PRO ARG PRO PRO PRO PRO GLU 0.407407 0.797101
138 DPN PRO DAR DTH NH2 0.407407 0.826087
139 ACE ARG THR PRO SEP LEU PRO THR PIP 0.406667 0.772152
140 LYS ARG ARG ARG HIS PRO SER GLY 0.406667 0.857143
141 LYS LEU THR PRO LEU CYS VAL THR LEU 0.405594 0.811594
142 ACE GLN GLU ARG GLU VAL PRO CYS 0.404255 0.826087
143 LEU LEU CYS SER TPO PRO ASN GLY LEU 0.40411 0.797297
144 SER PRO ILE VAL PRO SER PHE ASP MET 0.403846 0.797297
145 VAL PRO LEU 0.40367 0.742424
146 ACE ALA ALA ARG LBZ SER ALA PRO ALA 0.402597 0.857143
147 GLU SER ASP PRO ILE VAL ALA GLN TYR 0.402516 0.819444
148 ARG PRO GLY ASN PHE LEU GLN SER ARG PRO 0.402439 0.914286
149 ARG GLN PHE GLY PRO ASP PHE PRO THR ILE 0.402367 0.863014
150 ASN ARG LEU MET LEU THR GLY 0.401515 0.71831
151 GLN ALA SER TPO PRO ARG NIT 0.401235 0.717647
152 ARG SEP PRO VAL PHE SER 0.4 0.810811
153 ILE PRO ALA TYR GLY VAL LEU THR ILE 0.4 0.791667
154 ILE PRO ILE 0.4 0.727273
155 ASN SER THR LEU GLN 0.4 0.641791
Similar Ligands (3D)
Ligand no: 1; Ligand: ASN ARG PRO ILE LEU SER LEU; 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 : 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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