Amino acids
253
Annotations
10
Features
13
PDB binders
21
Druggability
0.668
Overview
Basic information about this protein and its source genome.
- Accession
- KP13_13347
- Gene
- udp ANJ86644.1
- Status
- annotated
- Amino acids
- 253
- Structure source
- AlphaFold + ColabFold
EC
GO
GO:0009166 The chemical reactions and pathways resulting in the breakdown of nucleotides, any nucleoside that is esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the glycose moiety; may be mono-, di- or triphosphate; this definition includes cyclic-nucleotides (nucleoside cyclic phosphates).
GO:0009116 The chemical reactions and pathways involving a nucleoside, a nucleobase linked to either beta-D-ribofuranose (a ribonucleoside) or 2-deoxy-beta-D-ribofuranose, (a deoxyribonucleoside), e.g. adenosine, guanosine, inosine, cytidine, uridine and deoxyadenosine, deoxyguanosine, deoxycytidine and thymidine (= deoxythymidine).
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0004850 Catalysis of the reaction: uridine + phosphate = uracil + alpha-D-ribose 1-phosphate.
GO:0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.
GO:0016763 Catalysis of the transfer of a pentosyl group from one compound (donor) to another (acceptor).
Target profile
Computed evidence for target prioritization.
- Human off-target
- hit
- Human identity (%)
- 30.435
- Human E-value
- 3.22e-09
- Gut microbiome off-target
- hit
- Essential (DEG)
- Y
- DEG identity (%)
- 76.285
- DEG E-value
- 3.72e-147
- Localization
- Cytoplasmic
- ColabFold pLDDT
- 97.17
Selected Druggability evidence
AlphaFold / UniProt modelSelected Druggability is the FPocket score chosen for ranking using the curated structure priority. The 3D viewer may show a different loaded structure, so its visible pockets can differ.
FPocket
0.668
P2Rank
0.471
ColabFold model
Core conservation
Conserved core gene
Gut microbiome
166 / 4744
genomes with a hit
Sequence
Primary amino-acid sequence viewer.
Functional Annotations
Enzyme classification and Gene Ontology terms linked to this protein.
1 EC
9 GO
Enzyme Commission (EC)
1Gene Ontology (GO)
9- GO:0009166 The chemical reactions and pathways resulting in the breakdown of nucleotides, any nucleoside that is esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the glycose moiety; may be mono-, di- or triphosphate; this definition includes cyclic-nucleotides (nucleoside cyclic phosphates).
- GO:0009116 The chemical reactions and pathways involving a nucleoside, a nucleobase linked to either beta-D-ribofuranose (a ribonucleoside) or 2-deoxy-beta-D-ribofuranose, (a deoxyribonucleoside), e.g. adenosine, guanosine, inosine, cytidine, uridine and deoxyadenosine, deoxyguanosine, deoxycytidine and thymidine (= deoxythymidine).
- GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
- GO:0004850 Catalysis of the reaction: uridine + phosphate = uracil + alpha-D-ribose 1-phosphate.
- GO:0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.
- GO:0016763 Catalysis of the transfer of a pentosyl group from one compound (donor) to another (acceptor).
- GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
- GO:0009164 The chemical reactions and pathways resulting in the breakdown of any one of a family of organic molecules consisting of a purine or pyrimidine base covalently bonded to a sugar ribose (a ribonucleoside) or deoxyribose (a deoxyribonucleoside).
- GO:0044206 Any process which produces UMP, uridine monophosphate, from derivatives of it (e.g. cytidine, uridine, cytosine) without de novo synthesis.
Sequence Features
Domain/signature hits from InterPro and related databases.
13 records
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 6 | 253 | NCBIfam | TIGR01718 | uridine phosphorylase |
| 6 | 253 | InterPro | IPR010058 | Uridine phosphorylase |
| 66 | 81 | ProSitePatterns | PS01232 | Purine and other phosphorylases family 1 signature. |
| 66 | 81 | InterPro | IPR018016 | Nucleoside phosphorylase, conserved site |
| 2 | 250 | PANTHER | PTHR43691 | URIDINE PHOSPHORYLASE |
| 7 | 250 | CDD | cd17767 | UP_EcUdp-like |
| 1 | 253 | Gene3D | G3DSA:3.40.50.1580 | Nucleoside phosphorylase domain |
| 1 | 253 | InterPro | IPR035994 | Nucleoside phosphorylase superfamily |
| 1 | 253 | FunFam | G3DSA:3.40.50.1580:FF:000003 | Uridine phosphorylase |
| 6 | 250 | SUPERFAMILY | SSF53167 | Purine and uridine phosphorylases |
| 6 | 250 | InterPro | IPR035994 | Nucleoside phosphorylase superfamily |
| 21 | 248 | Pfam | PF01048 | Phosphorylase superfamily |
| 21 | 248 | InterPro | IPR000845 | Nucleoside phosphorylase domain |
3D Structure
Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; predicted models typically cover the full protein.
Loading 3D structure...
Legend
High
Medium
Low
Structural evidence
0 + 2Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.
| Entry | Method | Resolution | Chain | Coverage | Links | Status |
|---|---|---|---|---|---|---|
|
AlphaFold
AF_A0A0H3GGL0
|
AlphaFold | — | — | full sequence | — | Viewing |
|
ColabFold
KP13_13347
|
ColabFold | — | — | full sequence | — | Loaded |
Pocket details FPocket · P2Rank — toggle visibility and zoom from here, or open full viewer
Pockets (FPOCKET)
Showing top-ranked FPocket candidates by druggability. Druggability is color-coded: high (0.7 or higher), medium (0.4 to 0.69), low (below 0.4).
| FPOCKET | Sticks | Spheres | Surfaces | Druggability | Labels | Zoom | Positions |
|---|---|---|---|---|---|---|---|
| 4 | 0.668 |
Pockets (P2RANK)
Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).
| P2RANK | Sticks | Spheres | Surfaces | Score | Probability | Labels | Zoom | Positions |
|---|---|---|---|---|---|---|---|---|
| 1 | 3.22 | 0.111 | ||||||
| 2 | 1.75 | 0.032 |
Pockets (FPOCKET)
Showing top-ranked FPocket candidates by druggability. Druggability is color-coded: high (0.7 or higher), medium (0.4 to 0.69), low (below 0.4).
| FPOCKET | Sticks | Spheres | Surfaces | Druggability | Labels | Zoom | Positions |
|---|---|---|---|---|---|---|---|
| 2 | 0.575 | ||||||
| 1 | 0.566 |
Pockets (P2RANK)
Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).
| P2RANK | Sticks | Spheres | Surfaces | Score | Probability | Labels | Zoom | Positions |
|---|---|---|---|---|---|---|---|---|
| 1 | 2.46 | 0.067 | ||||||
| 2 | 2.09 | 0.047 |
Ligand evidence
Ligands grouped by evidence source. PDB ligands keep the source crystal visible, and loaded crystals can be opened directly in the structure viewer.
71 records
Highest-confidence structural evidence: ligands co-crystallized with this exact protein. If the source PDB is loaded in TPW, use Open crystal to inspect it in the structure viewer.
No PDB structure with a co-crystallized ligand found for this exact protein.
Structural evidence inferred from similar proteins. The source crystal indicates where the ligand was observed; the UniProt column identifies the homologous protein carrying that ligand.
| Ligand | Source crystal | UniProt (homolog) | MW · LogP · TPSA | Lipinski | PAINS | SMILES |
|---|---|---|---|---|---|---|
| 181 | P12758 | 294.3 Da LogP 0.65 TPSA 84.3 | ✓ Ro5 | ✓ Clean |
c1ccc(cc1)SC2=CN(C(=O)NC2=O)COCCO
|
|
| 182 | P12758 | 341.2 Da LogP -1.84 TPSA 84.3 | ✓ Ro5 | ✓ Clean |
c1ccc(cc1)[Se]C2=CN(C(=O)NC2=O)COCCO
|
|
| 183 | P12758 | 382.4 Da LogP 1.67 TPSA 93.6 | ✓ Ro5 | ✓ Clean |
c1ccc(cc1)COc2cccc(c2)CC3=CN(C(=O)NC3=O)COCCO
|
|
| 4WR | Q9K4U1 | 202.2 Da LogP -2.04 TPSA 106.9 | ✓ Ro5 | ✓ Clean |
C1=C(C(=O)NC(=O)N1C[C@@H](CN)N)F
|
|
| 5UD | P12758 | 262.2 Da LogP -2.71 TPSA 124.8 | ✓ Ro5 | ✓ Clean |
C1=C(C(=O)NC(=O)N1[C@H]2[C@@H]([C@@H]([C@H](O2)…
|
|
| 61N | Q5E046 | 188.2 Da LogP 2.24 TPSA 57.5 | ✓ Ro5 | ✓ Clean |
c1cc2cc(ccc2c(c1)C(=O)O)O
|
|
| 6MU | Q9K4U1 | 126.1 Da LogP 0.20 TPSA 66.2 | ✓ Ro5 | ✓ Clean |
Cc1cc(nc(n1)O)O
|
|
| ANU | P0A1F6 | 226.2 Da LogP -1.75 TPSA 93.8 | ✓ Ro5 | ✓ Clean |
C1=CN2[C@H]3[C@H]([C@@H]([C@H](O3)CO)O)OC2=NC1=O
|
|
| BAU | P12758 | 276.3 Da LogP 0.09 TPSA 84.3 | ✓ Ro5 | ✓ Clean |
c1ccc(cc1)CC2=CN(C(=O)NC2=O)COCCO
|
|
| BBB | P12758 | 398.4 Da LogP 1.38 TPSA 113.8 | ✓ Ro5 | ✓ Clean |
c1ccc(cc1)COc2cccc(c2)CC3=C(N(C(=O)NC3=O)COCCO)O
|
|
| BJE | Q9K4U1 | 226.2 Da LogP -1.75 TPSA 93.8 | ✓ Ro5 | ✓ Clean |
C1=CN2[C@H]3[C@@H]([C@@H]([C@H](O3)CO)O)OC2=NC1…
|
|
| CTN | Q9K4U1 | 243.2 Da LogP -2.56 TPSA 130.8 | ✓ Ro5 | ✓ Clean |
C1=CN(C(=O)N=C1N)[C@H]2[C@@H]([C@@H]([C@H](O2)C…
|
|
| CYT | Q9K4U1 | 111.1 Da LogP -0.65 TPSA 71.8 | ✓ Ro5 | ✓ Clean |
C1=C(NC(=O)N=C1)N
|
|
| DUR | P12758 | 228.2 Da LogP -1.82 TPSA 104.6 | ✓ Ro5 | ✓ Clean |
C1[C@@H]([C@H](O[C@H]1N2C=CC(=O)NC2=O)CO)O
|
|
| IMH | Q2HXR2 | 266.3 Da LogP -2.02 TPSA 134.3 | 1 viol. | ✓ Clean |
c1c(c2c([nH]1)C(=O)NC=N2)[C@H]3[C@@H]([C@@H]([C…
|
|
| M5F | Q9K4U1 | 202.2 Da LogP -2.04 TPSA 106.9 | ✓ Ro5 | ✓ Clean |
C1=C(C(=O)NC(=O)N1C[C@H](CN)N)F
|
|
| TDR | P0A1F6 | 126.1 Da LogP -0.63 TPSA 65.7 | ✓ Ro5 | ✓ Clean |
CC1=CNC(=O)NC1=O
|
|
| THM | P12758 | 242.2 Da LogP -1.51 TPSA 104.6 | ✓ Ro5 | ✓ Clean |
CC1=CN(C(=O)NC1=O)[C@H]2C[C@@H]([C@H](O2)CO)O
|
|
| URA | P0A1F6 | 112.1 Da LogP -0.94 TPSA 65.7 | ✓ Ro5 | ✓ Clean |
C1=CNC(=O)NC1=O
|
|
| URF | P0A1F6 | 130.1 Da LogP -0.80 TPSA 65.7 | ✓ Ro5 | ✓ Clean |
C1=C(C(=O)NC(=O)N1)F
|
|
| URI | P0A1F6 | 244.2 Da LogP -2.85 TPSA 124.8 | ✓ Ro5 | ✓ Clean |
C1=CN(C(=O)NC1=O)[C@H]2[C@@H]([C@@H]([C@H](O2)C…
|
Experimental bioactivity from ChEMBL measured directly on this protein. Score = pchembl (−log Ki/IC₅₀; higher = more potent).
No ChEMBL bioactivity data found for this exact protein.
Bioactivity inferred from similar proteins in ChEMBL. Score = pchembl (−log Ki/IC₅₀; higher = more potent).
No ChEMBL hits found through similar proteins.
Proposed virtual-screening candidates from ZINC. Score = Tanimoto similarity to a known binder (0–1; higher = more similar).
| Ligand | Tanimoto | MW · LogP · TPSA | Lipinski | PAINS | SMILES |
|---|---|---|---|---|---|
| ZINC101742825 | 1.000 | 226.2 Da LogP -1.75 TPSA 93.8 | ✓ Ro5 | ✓ Clean |
O=c1ccn2c(n1)O[C@@H]1[C@H](O)[C@H](CO)O[C@H]12
|
| ZINC11525575 | 1.000 | 244.2 Da LogP -2.85 TPSA 124.8 | ✓ Ro5 | ✓ Clean |
O=c1ccn([C@H]2O[C@H](CO)[C@H](O)[C@H]2O)c(=O)[n…
|
| ZINC11525576 | 1.000 | 244.2 Da LogP -2.85 TPSA 124.8 | ✓ Ro5 | ✓ Clean |
O=c1ccn([C@@H]2O[C@H](CO)[C@H](O)[C@H]2O)c(=O)[…
|
| ZINC12360648 | 1.000 | 226.2 Da LogP -1.75 TPSA 93.8 | ✓ Ro5 | ✓ Clean |
O=c1ccn2c(n1)O[C@@H]1[C@@H]2O[C@H](CO)[C@H]1O
|
| ZINC12360649 | 1.000 | 226.2 Da LogP -1.75 TPSA 93.8 | ✓ Ro5 | ✓ Clean |
O=c1ccn2c(n1)O[C@H]1[C@@H]2O[C@H](CO)[C@H]1O
|
| ZINC12958864 | 1.000 | 226.2 Da LogP -1.75 TPSA 93.8 | ✓ Ro5 | ✓ Clean |
O=c1ccn2c(n1)O[C@H]1[C@H](O)[C@H](CO)O[C@H]12
|
| ZINC12958872 | 1.000 | 226.2 Da LogP -1.75 TPSA 93.8 | ✓ Ro5 | ✓ Clean |
O=c1ccn2c(n1)O[C@@H]1[C@@H]2O[C@@H](CO)[C@H]1O
|
| ZINC1303438 | 1.000 | 226.2 Da LogP -1.75 TPSA 93.8 | ✓ Ro5 | ✓ Clean |
O=c1ccn2c(n1)O[C@H]1[C@@H]2O[C@@H](CO)[C@H]1O
|
| ZINC13492899 | 1.000 | 266.3 Da LogP -2.02 TPSA 134.3 | 1 viol. | ✓ Clean |
O=c1[nH]cnc2c([C@@H]3N[C@H](CO)[C@@H](O)[C@H]3O…
|
| ZINC1446448 | 1.000 | 244.2 Da LogP -2.85 TPSA 124.8 | ✓ Ro5 | ✓ Clean |
O=c1ccn([C@H]2O[C@H](CO)[C@@H](O)[C@H]2O)c(=O)[…
|
| ZINC1842580 | 1.000 | 242.2 Da LogP -1.51 TPSA 104.5 | ✓ Ro5 | ✓ Clean |
Cc1cn([C@@H]2C[C@H](O)[C@H](CO)O2)c(=O)[nH]c1=O
|
| ZINC2021810 | 1.000 | 276.3 Da LogP 0.09 TPSA 84.3 | ✓ Ro5 | ✓ Clean |
O=c1[nH]c(=O)n(COCCO)cc1Cc1ccccc1
|
| ZINC2159 | 1.000 | 242.2 Da LogP -1.51 TPSA 104.5 | ✓ Ro5 | ✓ Clean |
Cc1cn([C@@H]2C[C@@H](O)[C@H](CO)O2)c(=O)[nH]c1=O
|
| ZINC2545102 | 1.000 | 242.2 Da LogP -1.51 TPSA 104.5 | ✓ Ro5 | ✓ Clean |
Cc1cn([C@H]2C[C@@H](O)[C@H](CO)O2)c(=O)[nH]c1=O
|
| ZINC2565479 | 1.000 | 244.2 Da LogP -2.85 TPSA 124.8 | ✓ Ro5 | ✓ Clean |
O=c1ccn([C@@H]2O[C@@H](CO)[C@H](O)[C@@H]2O)c(=O…
|
| ZINC25672 | 1.000 | 242.2 Da LogP -1.51 TPSA 104.5 | ✓ Ro5 | ✓ Clean |
Cc1cn([C@H]2C[C@H](O)[C@@H](CO)O2)c(=O)[nH]c1=O
|
| ZINC2572653 | 1.000 | 242.2 Da LogP -1.51 TPSA 104.5 | ✓ Ro5 | ✓ Clean |
Cc1cn([C@@H]2C[C@@H](O)[C@@H](CO)O2)c(=O)[nH]c1…
|
| ZINC2583633 | 1.000 | 244.2 Da LogP -2.85 TPSA 124.8 | ✓ Ro5 | ✓ Clean |
O=c1ccn([C@@H]2O[C@H](CO)[C@@H](O)[C@H]2O)c(=O)…
|
| ZINC315929 | 1.000 | 226.2 Da LogP -1.75 TPSA 93.8 | ✓ Ro5 | ✓ Clean |
O=c1ccn2c(n1)O[C@H]1[C@H](O)[C@@H](CO)O[C@H]12
|
| ZINC33817734 | 1.000 | 226.2 Da LogP -1.75 TPSA 93.8 | ✓ Ro5 | ✓ Clean |
O=c1ccn2c(n1)O[C@H]1[C@@H](O)[C@H](CO)O[C@@H]12
|
| ZINC33817735 | 1.000 | 226.2 Da LogP -1.75 TPSA 93.8 | ✓ Ro5 | ✓ Clean |
O=c1ccn2c(n1)O[C@@H]1[C@@H](O)[C@H](CO)O[C@@H]12
|
| ZINC3831529 | 1.000 | 242.2 Da LogP -1.51 TPSA 104.5 | ✓ Ro5 | ✓ Clean |
Cc1cn([C@H]2C[C@H](O)[C@H](CO)O2)c(=O)[nH]c1=O
|
| ZINC3834164 | 1.000 | 244.2 Da LogP -2.85 TPSA 124.8 | ✓ Ro5 | ✓ Clean |
O=c1ccn([C@@H]2O[C@H](CO)[C@@H](O)[C@@H]2O)c(=O…
|
| ZINC3870261 | 1.000 | 244.2 Da LogP -2.85 TPSA 124.8 | ✓ Ro5 | ✓ Clean |
O=c1ccn([C@H]2O[C@@H](CO)[C@@H](O)[C@H]2O)c(=O)…
|
| ZINC3870262 | 1.000 | 244.2 Da LogP -2.85 TPSA 124.8 | ✓ Ro5 | ✓ Clean |
O=c1ccn([C@@H]2O[C@@H](CO)[C@@H](O)[C@H]2O)c(=O…
|
| ZINC3870263 | 1.000 | 244.2 Da LogP -2.85 TPSA 124.8 | ✓ Ro5 | ✓ Clean |
O=c1ccn([C@H]2O[C@@H](CO)[C@@H](O)[C@@H]2O)c(=O…
|
| ZINC3870264 | 1.000 | 244.2 Da LogP -2.85 TPSA 124.8 | ✓ Ro5 | ✓ Clean |
O=c1ccn([C@@H]2O[C@@H](CO)[C@@H](O)[C@@H]2O)c(=…
|
| ZINC389497 | 1.000 | 226.2 Da LogP -1.75 TPSA 93.8 | ✓ Ro5 | ✓ Clean |
O=c1ccn2c(n1)O[C@@H]1[C@@H](O)[C@@H](CO)O[C@@H]…
|
| ZINC3956782 | 1.000 | 226.2 Da LogP -1.75 TPSA 93.8 | ✓ Ro5 | ✓ Clean |
O=c1ccn2c(n1)O[C@@H]1[C@H](O)[C@@H](CO)O[C@H]12
|
| ZINC4529544 | 1.000 | 226.2 Da LogP -1.75 TPSA 93.8 | ✓ Ro5 | ✓ Clean |
O=c1ccn2c(n1)O[C@H]1[C@@H](O)[C@@H](CO)O[C@@H]12
|
| ZINC4529545 | 1.000 | 226.2 Da LogP -1.75 TPSA 93.8 | ✓ Ro5 | ✓ Clean |
O=c1ccn2c(n1)O[C@H]1[C@@H](O)[C@@H](CO)O[C@H]12
|
| ZINC4529547 | 1.000 | 226.2 Da LogP -1.75 TPSA 93.8 | ✓ Ro5 | ✓ Clean |
O=c1ccn2c(n1)O[C@@H]1[C@@H](O)[C@@H](CO)O[C@H]12
|
| ZINC5765078 | 1.000 | 242.2 Da LogP -1.51 TPSA 104.5 | ✓ Ro5 | ✓ Clean |
Cc1cn([C@H]2C[C@@H](O)[C@@H](CO)O2)c(=O)[nH]c1=O
|
| ZINC6072455 | 1.000 | 242.2 Da LogP -1.51 TPSA 104.5 | ✓ Ro5 | ✓ Clean |
Cc1cn([C@@H]2C[C@H](O)[C@@H](CO)O2)c(=O)[nH]c1=O
|
| ZINC6091549 | 1.000 | 244.2 Da LogP -2.85 TPSA 124.8 | ✓ Ro5 | ✓ Clean |
O=c1ccn([C@H]2O[C@@H](CO)[C@H](O)[C@H]2O)c(=O)[…
|
| ZINC6524831 | 1.000 | 244.2 Da LogP -2.85 TPSA 124.8 | ✓ Ro5 | ✓ Clean |
O=c1ccn([C@@H]2O[C@@H](CO)[C@H](O)[C@H]2O)c(=O)…
|
| ZINC7998085 | 1.000 | 244.2 Da LogP -2.85 TPSA 124.8 | ✓ Ro5 | ✓ Clean |
O=c1ccn([C@H]2O[C@H](CO)[C@@H](O)[C@@H]2O)c(=O)…
|
| ZINC8613151 | 1.000 | 244.2 Da LogP -2.85 TPSA 124.8 | ✓ Ro5 | ✓ Clean |
O=c1ccn([C@@H]2O[C@H](CO)[C@H](O)[C@@H]2O)c(=O)…
|
| ZINC8613153 | 1.000 | 244.2 Da LogP -2.85 TPSA 124.8 | ✓ Ro5 | ✓ Clean |
O=c1ccn([C@H]2O[C@H](CO)[C@H](O)[C@@H]2O)c(=O)[…
|
| ZINC895165 | 1.000 | 244.2 Da LogP -2.85 TPSA 124.8 | ✓ Ro5 | ✓ Clean |
O=c1ccn([C@H]2O[C@@H](CO)[C@H](O)[C@@H]2O)c(=O)…
|
| ZINC4804742 | 0.854 | 272.3 Da LogP -2.15 TPSA 124.8 | ✓ Ro5 | ✓ Clean |
Cc1cn([C@@H]2C[C@H](O)[C@H](O)[C@H](CO)O2)c(=O)…
|
| ZINC4804743 | 0.854 | 272.3 Da LogP -2.15 TPSA 124.8 | ✓ Ro5 | ✓ Clean |
Cc1cn([C@H]2C[C@H](O)[C@H](O)[C@H](CO)O2)c(=O)[…
|
| ZINC4804744 | 0.854 | 272.3 Da LogP -2.15 TPSA 124.8 | ✓ Ro5 | ✓ Clean |
Cc1cn([C@@H]2C[C@@H](O)[C@H](O)[C@H](CO)O2)c(=O…
|
| ZINC4804745 | 0.854 | 272.3 Da LogP -2.15 TPSA 124.8 | ✓ Ro5 | ✓ Clean |
Cc1cn([C@H]2C[C@@H](O)[C@H](O)[C@H](CO)O2)c(=O)…
|
| ZINC16928956 | 0.810 | 258.3 Da LogP -0.14 TPSA 87.5 | ✓ Ro5 | ✓ Clean |
Cc1cn([C@H]2C[C@@H](O)[C@@H](CO)O2)c(=O)[nH]c1=S
|
| ZINC5085194 | 0.805 | 244.2 Da LogP -0.54 TPSA 84.3 | ✓ Ro5 | ✓ Clean |
Cc1cn([C@@H]2C[C@H](O)[C@H](CF)O2)c(=O)[nH]c1=O
|
| ZINC5085195 | 0.805 | 244.2 Da LogP -0.54 TPSA 84.3 | ✓ Ro5 | ✓ Clean |
Cc1cn([C@H]2C[C@H](O)[C@H](CF)O2)c(=O)[nH]c1=O
|
| ZINC5085196 | 0.805 | 244.2 Da LogP -0.54 TPSA 84.3 | ✓ Ro5 | ✓ Clean |
Cc1cn([C@@H]2C[C@@H](O)[C@H](CF)O2)c(=O)[nH]c1=O
|
| ZINC5085197 | 0.805 | 244.2 Da LogP -0.54 TPSA 84.3 | ✓ Ro5 | ✓ Clean |
Cc1cn([C@H]2C[C@@H](O)[C@H](CF)O2)c(=O)[nH]c1=O
|
| ZINC13546398 | 0.800 | 246.2 Da LogP -1.87 TPSA 104.5 | ✓ Ro5 | ✓ Clean |
O=c1ccn([C@@H]2O[C@H](CO)[C@H](O)[C@H]2F)c(=O)[…
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PDB and ChEMBL records on this protein are shown in full. ChEMBL records from similar proteins are capped at the top 100 per protein (by pchembl) and ZINC at the top 50 (Tanimoto ≥ 0.5). ADME columns are descriptor-based screening flags, not experimental toxicity results.