Receptor
PDB id Resolution Class Description Source Keywords
2PEH 2.11 Å NON-ENZYME: TRANSCRIPT_TRANSLATE CRYSTAL STRUCTURE OF THE UHM DOMAIN OF HUMAN SPF45 IN COMPLE SF3B155-ULM5 HOMO SAPIENS RRM UHM PROTEIN BINDING
Ref.: U2AF-HOMOLOGY MOTIF INTERACTIONS ARE REQUIRED FOR ALTERNATIVE SPLICING REGULATION BY SPF45. NAT.STRUCT.MOL.BIOL. V. 14 620 2007
Ligand
Ligand Chain:Residue Validity Ligand Warnings Binding Data NGL Viewer Molecular Weight (Da) Formula SMILES
LYS ARG LYS SER ARG TRP ASP GLU THR PRO C:333;
D:334;
Valid;
Valid;
none;
none;
Kd = 1.1 uM
986.054 n/a O=C(N...
View in 3D viewer
90% Homology Family
Leader
PDB id Resolution Class Description Source Keywords
2PEH 2.11 Å NON-ENZYME: TRANSCRIPT_TRANSLATE CRYSTAL STRUCTURE OF THE UHM DOMAIN OF HUMAN SPF45 IN COMPLE SF3B155-ULM5 HOMO SAPIENS RRM UHM PROTEIN BINDING
Ref.: U2AF-HOMOLOGY MOTIF INTERACTIONS ARE REQUIRED FOR ALTERNATIVE SPLICING REGULATION BY SPF45. NAT.STRUCT.MOL.BIOL. V. 14 620 2007
Members (1)
No: PDB id Binding Data Representative ligand Formula Smiles
The Class containing this family consists of a total of 291 families.
1 2PEH Kd = 1.1 uM LYS ARG LYS SER ARG TRP ASP GLU THR PRO 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 2PEH Kd = 1.1 uM LYS ARG LYS SER ARG TRP ASP GLU THR PRO 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 2PEH Kd = 1.1 uM LYS ARG LYS SER ARG TRP ASP GLU THR PRO n/a n/a
Polypharmacology
Similar Ligands
Ligand no: 1; Ligand: LYS ARG LYS SER ARG TRP ASP GLU THR PRO; Similar ligands found: 119
No: Ligand ECFP6 Tc MDL keys Tc
1 LYS ARG LYS SER ARG TRP ASP GLU THR PRO 1 1
2 ALA ASN SER ARG TRP GLN ASP THR ARG LEU 0.594937 0.824324
3 ARG GLU ARG SER PRO THR ARG 0.552239 0.857143
4 GLU GLY PRO ARG ASN GLN ASP TRP LEU 0.546512 0.90411
5 ALA ASN SER ARG TRP GLN THR SER ILE ILE 0.546012 0.810811
6 LEU GLU LEU ASP LYS TRP ALA SER LEU 0.531646 0.763889
7 ILE SER PRO ARG THR LEU ASP ALA TRP 0.530726 0.932432
8 LYS VAL PRO ARG ASN GLN ASP TRP LEU 0.52809 0.90411
9 GLU LEU ARG SER ARG TYR TRP ALA ILE 0.52071 0.792208
10 GLU ALA ASP LYS TRP GLN SER 0.519481 0.771429
11 GLU GLN ASP LYS TRP ALA SER 0.516129 0.771429
12 GLU LEU ASP NRG TRP ALA SER 0.515337 0.7625
13 ALA ASN SER ARG TRP PRO THR SER ALY ILE 0.513812 0.933333
14 SER ARG ARG TRP ARG ARG TRP ASN ARG 0.513699 0.819444
15 ALA LEU ASP LYS TRP ALA SER 0.509934 0.75
16 ALA THR ALY ALA ALA ARG ALY SER ALA PRO 0.506494 0.861111
17 ALA ASN SER ARG TRP PRO ALY SER ILE ILE 0.505495 0.945946
18 ALA SER ASN GLU ASN TRP GLU THR MET 0.503226 0.688312
19 ALA ASN SER ARG TRP ALY THR SER ILE ILE 0.502924 0.826667
20 ALA ASN SER ARG TRP PRO THR THR ARG LEU 0.50289 0.932432
21 ALA ASN SER ARG TRP PRO THR SER FAK ILE 0.502703 0.884615
22 GLU ASN ASP LYS TRP ALA SER 0.5 0.760563
23 ALA ASN SER ARG TRP PRO THR SER 2KK ILE 0.497355 0.873418
24 SER ARG TYR TRP ALA ILE ARG THR ARG 0.494118 0.789474
25 GLU LEU ASP ORN TRP ALA SER 0.49359 0.736111
26 SER PRO LEU ASP SER LEU TRP TRP ILE 0.490909 0.851351
27 GLU LEU ASP LYS TRP ALA SER 0.490446 0.75
28 ALA ASN SER ARG TRP PRO THR SER 2KP ILE 0.489583 0.873418
29 ARG GLN PHE GLY PRO ASP TRP ILE VAL ALA 0.489474 0.864865
30 PRO SER ARG TRP 0.486486 0.842857
31 ARG GLN TRP GLY PRO ASP PRO ALA ALA VAL 0.481081 0.915493
32 ARG LEU TRP SER 0.47619 0.777778
33 ARG ARG ARG ARG SER TRP TYR 0.475862 0.814286
34 LEU LEU GLU LEU ASP LYS TRP ALA NH2 0.474359 0.694444
35 GLU LEU GLU LYS TRP ALA SER 0.471338 0.736111
36 ALA GLN ASP ILE TYR ARG ALA SER TYR 0.46988 0.710526
37 ARG ARG ARG TRP ARG ARG LEU THR VAL 0.468354 0.808219
38 ARG PHE MET ASP TYR TRP GLU GLY LEU 0.466667 0.7125
39 GLN ALA SER GLN ASP VAL LYS ASN TRP 0.464286 0.777778
40 GLN ALA SER GLN GLU VAL LYS ASN TRP 0.464286 0.777778
41 MET SER LEU PRO GLY ARG TRP LYS PRO LYS 0.463542 0.907895
42 PHE LEU TRP GLY PRO ARG ALA LEU VAL 0.461538 0.863014
43 PRO ALA TRP ASP GLU THR ASN LEU 0.461538 0.756757
44 ALA GLN TRP GLY PRO ASP PRO ALA ALA ALA 0.460227 0.842857
45 ALA LEU ASP LYS TRP ASP 0.46 0.708333
46 ASP ASP TRP ASN TRP GLU VAL GLU ASP 0.46 0.657534
47 GLU LEU ASP LYS TRP ALA ASN 0.459627 0.712329
48 ACE PRO TRP ALA THR CYS ASP SER NH2 0.458333 0.876712
49 GLU LEU ASP HOX TRP ALA SER 0.45679 0.68
50 GLU LEU ASP HIS TRP ALA SER 0.453988 0.726027
51 SER SER THR ARG GLY ILE SER GLN LEU TRP 0.451977 0.824324
52 PRO GLN PRO VAL ASP SER TRP VAL 0.450867 0.887324
53 ASN ASP TRP LEU LEU PRO SER TYR 0.446927 0.818182
54 ARG ARG ARG TRP HIS ARG TRP ARG LEU 0.446541 0.743243
55 PRO ARG PRO ILE LEU LEU PRO TRP ARG NH2 0.445714 0.835616
56 SER LEU SER ARG THR PRO ALA ASP GLY ARG 0.443787 0.887324
57 MET TRP ARG PRO TRP 0.443787 0.776316
58 SER PHE PHE GLU ASP ASN PHE VAL PRO GLU 0.44375 0.821918
59 GLU LEU ASP LYS TRP ALA GLY 0.44375 0.708333
60 PRO LYS LEU GLU PRO TRP LYS HIS PRO 0.441489 0.808219
61 ASP TRP GLU ILE VAL 0.437086 0.616438
62 ASN ASP LYS TYR GLU PRO PHE TRP GLU 0.434555 0.786667
63 ASP ALA GLU PHE ARG HIS ASP 0.434211 0.671429
64 SER SER LEU GLU ASN PHE ARG ALA TYR VAL 0.431818 0.701299
65 GLU PRO GLN ALA PRO TRP MET GLU GLN 0.431034 0.773333
66 GLU PRO GLN ALA PRO TRP MET GLU 0.431034 0.773333
67 ILE ARG TYR PRO LYS THR PHE GLY TRP 0.427136 0.881579
68 ARG ARG LYS TRP ARG ARG TRP HIS LEU 0.42515 0.756757
69 SER TRP PHE PRO 0.424837 0.830986
70 ALA LEU ASP LYS TRP GLN ASN 0.424837 0.694444
71 ILE ASP TRP PHE GLU GLY LYS GLU 0.424419 0.712329
72 ILE ASP TRP PHE ASP GLY LYS GLU 0.424419 0.712329
73 ARG PRO GLY ASN PHE LEU GLN SER ARG PRO 0.423913 0.90411
74 LYS ARG TRP ILE ILE LEU GLY LEU ASN LYS 0.423077 0.797297
75 SER ARG ASP HIS SER ARG THR PRO MET 0.423077 0.857143
76 SER TRP PHE GLN THR ASP LEU 0.422619 0.702703
77 ACE ASN TRP GLU THR PHE 0.421384 0.684932
78 THR LEU PRO TRP ASP LEU TRP THR THR 0.421053 0.824324
79 GLU GLU PHE GLY ARG ALA PHE SER PHE 0.420732 0.732394
80 ASP ALA GLU PHE ARG HIS ASP SER 0.420732 0.760563
81 ARG PHE PRO LEU THR PHE GLY TRP 0.420213 0.905405
82 ASN GLN LEU ALA TRP PHE ASP THR ASP LEU 0.417143 0.662162
83 GLY ARG PRO ARG THR THR SER PHE ALA GLU 0.416667 0.915493
84 VAL ASP SER LYS ASN THR SER SER TRP 0.416667 0.753425
85 ARG ARG ALA SEP ALA PRO LEU PRO 0.416667 0.782051
86 ALA LEU TRP GLY PRO ASP PRO ALA ALA ALA 0.41573 0.819444
87 GLU GLU TYR LEU LYS ALA TRP THR PHE 0.415301 0.710526
88 ARG ARG LYS TRP CIR ARG TRP HIS LEU 0.415205 0.746667
89 LYS GLN TRP ASP ASN TYR GLU PTR ILE TRP 0.414894 0.626506
90 ALA ALA ARG KCR SER ALA PRO ALA 0.414201 0.873239
91 ARG PHE PRO LEU THR PHE GLY TRP CYS PHE 0.414141 0.906667
92 ASP GLN GLY ARG GLY ARG ARG ARG PRO 0.414013 0.814286
93 ARG TYR PRO LEU THR PHE GLY TRP CYS PHE 0.413793 0.87013
94 LYS GLN TRP ASP ASN TYR GLU PHE ILE TRP 0.412429 0.636364
95 VAL VAL ARG PRO GLY SER LEU ASP LEU PRO 0.412429 0.888889
96 ARG TYR PRO LEU THR PHE GLY TRP 0.412371 0.881579
97 ALA GLN PHE SER ALA SER ALA SER ARG 0.411765 0.742857
98 ASP SER TRP LYS ASP GLY CYS TYR 0.411429 0.72
99 ARG TYR PRO LEU THR LEU GLY TRP CYS PHE 0.408867 0.883117
100 LEU PRO PHE GLU ARG ALA THR VAL MET 0.408602 0.818182
101 ASP GLU ASP LYS TRP ASP ASP PHE 0.407643 0.690141
102 ABA SER LEU TRP ASN GLY PRO HIS LEU 0.407609 0.864865
103 PHE PRO ARG PRO TRP LEU HIS GLY LEU 0.407216 0.864865
104 ACE GLU TRP TRP TRP 0.407143 0.619718
105 GLN THR ALA ARG MYK SER THR GLY GLY TRP 0.406417 0.851351
106 PLM GLN THR ALA ARG LYS SER THR GLY GLY TRP 0.406417 0.851351
107 ALA ARG THR GLU LEU TYR ARG SER LEU 0.406061 0.72
108 THR SER ASN LEU GLN GLU GLN ILE GLY TRP 0.404494 0.733333
109 LEU PRO PHE GLU ARG ALA THR ILE MET 0.404255 0.807692
110 THR SER THR THR SER VAL ALA SER SER TRP 0.403846 0.694444
111 MET ASP TRP ASN MET HIS ALA ALA 0.403509 0.671053
112 LYS ARG TRP ILE ILE MET GLY LEU ASN LYS 0.403141 0.75641
113 ARG ILE PRO SER TYR ARG TYR ARG TYR 0.402367 0.855263
114 PHE SER ASP PRO TRP GLY GLY 0.402299 0.859155
115 GLY SER ASP PRO TRP LYS 0.401198 0.871429
116 GLY GLU GLU TRP GLY PRO TRP VAL NH2 0.401198 0.791667
117 ALA ASN SER ARG ALA PRO THR SER ILE ILE 0.401163 0.851351
118 MET HIS PRO ALA GLN THR SER GLN TRP 0.401042 0.831169
119 ALA ARG SER HIS SEP TYR PRO ALA 0.4 0.825
Similar Binding Sites (Proteins are less than 50% similar to leader)
Pocket No.: 1; Query (leader) PDB : 2PEH; Ligand: LYS ARG LYS SER ARG TRP ASP GLU THR PRO; 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: 2peh.bio3) has 16 residues
No: Leader PDB Ligand Sequence Similarity
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