Promising target candidate with multiple supporting evidence streams.
Automated synthesis of the evidence currently loaded. Review the underlying records before prioritizing this protein.
Main supporting evidence
Risks to review
Terms and data sources used on this page
PDB: experimentally determined structures from the Protein Data Bank. These are the strongest structural evidence, but may cover only part of the protein.
AlphaFold DB model: a precomputed predicted structure downloaded from AlphaFold Database/UniProt, not an experiment performed here.
ColabFold model: a predicted structure generated for this workspace; interpret it with coverage and confidence.
pLDDT: confidence score for predicted structures. High values support local geometry; low values mean the region should not drive pocket interpretation.
FPocket / P2Rank: software tools that predict possible ligand-binding pockets on a 3D structure. They are useful screening signals, not experimental validation.
Druggability: a pocket-based estimate of whether a small molecule could bind productively. It does not mean a drug already exists.
PDB ligand: a compound observed in an experimental structure. Direct same-protein records are stronger than homolog-transferred records.
ChEMBL: a public database of measured compound bioactivity. Direct entries are stronger than entries transferred from similar proteins.
ZINC: a purchasable-compound database. Here it marks proposed candidates from chemical similarity, not measured binders.
LigQ / LigQ_2: an internal Target pipeline step that gathers PDB, ChEMBL, and ZINC ligand evidence for each protein.
Off-target: sequence similarity to proteins we prefer not to hit, such as human proteins or beneficial gut microbiome proteins.
DEG: Database of Essential Genes. A match suggests the protein resembles genes known to be essential in other organisms.
Roary / CoreCruncher: pan-genome tools used to decide whether a gene is core across analyzed strains or accessory/strain-specific.
EC / GO: functional annotations: EC describes enzyme reactions; GO describes biological process, molecular function, or cellular component.
KEGG pathway: a curated metabolic route label used here to group reactions imported from the metabolic model.
Chokepoint: a metabolic reaction that is the only producer or consumer of a metabolite in the imported model.
Prioritization evidence
Selectivity, essentiality, structural confidence, conservation, and predicted binding-site evidence.
Off-target risk
- Human off-target
- No hit
- Gut microbiome similarity
- 3.4% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.
Essentiality
- Essential (DEG)
- Y
- DEG identity (%)
- 70.0 Higher values support similarity to known essential genes.
- DEG E-value
- 1.24e-175 Smaller values mean stronger essential-gene similarity.
Localization
- Localization
- Cytoplasmic
Structure confidence
- ColabFold pLDDT
- 93.15 0-100 confidence; >70 supports local structural interpretation.
Binding-site evidence
AlphaFold DB / UniProt modelThe selected pocket score is the FPocket value used for ranking after applying the curated structure priority. It estimates small-molecule pocket quality; it is not experimental binding evidence. The 3D viewer may show a different loaded structure, so visible pockets can differ.
Cross-references
External database identifiers for this protein, its structures, ligands, and metabolic reactions.
Sequence
Sequence
Primary amino-acid sequence viewer.
MMSVMFDPETAIYPFPAKPQPLTVDEKQFYREKIKRLLRERDAVMVAHYYTDPEIQQLAEETGGCIADSLEMARFGARHSASTLLVAGVRFMGETAKILSPEKTILMPTLNAECSLDLGCPIEEFNAFCDAHPDRTVVVYANTSAAVKARADWVVTSSIAVELIDHLDSLGQKILWAPDRHLGRYVQRQTGADVLCWQGACIVHDEFKTQALMRMKALHPEAAVLVHPESPQAIVEMADAVGSTSQLIAAAKSLPQRQLIVATDRGIFYKMQQAVPEKTLLEAPTAGEGATCRSCAHCPWMAMNGLKAIAEGLEQGGAAHEIHIDEALRTGALIPLNRMLDFAATLRG
Functional annotations
Enzyme classification and Gene Ontology terms linked to this protein.
Enzyme Commission (EC)
1Gene Ontology (GO)
7- GO:0008987 Catalysis of the reaction: iminoaspartate + dihydroxy-acetone-phosphate = quinolinate + 2 H2O + phosphate.
- GO:0009435 The chemical reactions and pathways resulting in the formation of nicotinamide adenine dinucleotide (NAD+), a coenzyme that interconverts with its reduced form, NADH, in many redox and catabolic reactions. NAD+ is derived from various sources including vitamin B3.
- GO:0051539 Binding to a 4 iron, 4 sulfur (4Fe-4S) cluster; this cluster consists of four iron atoms, with the inorganic sulfur atoms found between the irons and acting as bridging ligands.
- GO:0016765 Catalysis of the transfer of an alkyl or aryl (but not methyl) 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:0046872 Binding to a metal ion.
- GO:0034628 The chemical reactions and pathways resulting in the formation of nicotinamide adenine dinucleotide (NAD+), beginning with the catabolism of L-aspartate into the precursor quinolinate. NAD+ is a coenzyme that interconverts with its reduced form, NADH, in many redox and catabolic reactions.
Sequence domains and features
Domain and signature matches imported from InterPro and related databases.
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 28 | 342 | NCBIfam | TIGR00550 | quinolinate synthase |
| 28 | 342 | InterPro | IPR003473 | Quinolinate synthetase A |
| 201 | 296 | Gene3D | G3DSA:3.40.50.10800 | - |
| 201 | 296 | InterPro | IPR036094 | Quinolinate synthetase A superfamily |
| 33 | 323 | Gene3D | G3DSA:3.40.50.10800 | - |
| 33 | 323 | InterPro | IPR036094 | Quinolinate synthetase A superfamily |
| 286 | 345 | PANTHER | PTHR30573 | QUINOLINATE SYNTHETASE A |
| 286 | 345 | InterPro | IPR003473 | Quinolinate synthetase A |
| 116 | 216 | FunFam | G3DSA:3.40.50.10800:FF:000003 | Quinolinate synthase A |
| 116 | 340 | Gene3D | G3DSA:3.40.50.10800 | - |
| 116 | 340 | InterPro | IPR036094 | Quinolinate synthetase A superfamily |
| 30 | 342 | SUPERFAMILY | SSF142754 | NadA-like |
| 30 | 342 | InterPro | IPR036094 | Quinolinate synthetase A superfamily |
| 2 | 348 | Hamap | MF_00567 | Quinolinate synthase [nadA]. |
| 2 | 348 | InterPro | IPR023513 | Quinolinate synthase A, type 1 |
| 32 | 341 | Pfam | PF02445 | Quinolinate synthetase A protein |
| 32 | 341 | InterPro | IPR003473 | Quinolinate synthetase A |
3D structure
Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; AlphaFold DB and ColabFold models typically cover the full protein but remain computational predictions.
How colors and pocket overlays are used
Pocket details Inspect a specific pocket, or open the full viewer
- Method
- -
- Score
- -
- Visible layer
- -
- Residues
- -
- Pocket properties
- -
Selecting a pocket opens its details and centers the viewer without clearing other active layers. Use Focus this pocket when you want to hide the rest; use Surface for the wider residue environment.
Binding pockets · FPocket
Druggability: high ≥ 0.7 · medium 0.4–0.69 · low < 0.4
Binding pockets · P2Rank
Probability: high ≥ 0.5 · medium 0.2–0.49 · low < 0.2
Residue sets
Binding pockets · FPocket
Druggability: high ≥ 0.7 · medium 0.4–0.69 · low < 0.4
Binding pockets · P2Rank
Probability: high ≥ 0.5 · medium 0.2–0.49 · low < 0.2
All structural evidence
Structural evidence
0 + 2Experimental PDB entries plus predicted AlphaFold DB or ColabFold models. Click Switch to display a different loaded structure in the viewer.
| Entry | Method | Resolution | Chain | Coverage | Links | Status |
|---|---|---|---|---|---|---|
|
AlphaFold DB
AF_A0A0H3GU73
|
AlphaFold DB | — | — | full sequence | — | Viewing |
|
ColabFold
KP13_03261
|
ColabFold | — | — | full sequence | — | Loaded |
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.
Structural ligand evidence is available for this target.
Highest-confidence structural evidence: ligands co-crystallized with this exact protein. If the source PDB is loaded in Target, 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 |
|---|---|---|---|---|---|---|
| 13P RCSB PDB | O57767 | 170.1 Da LogP -1.34 TPSA 104.1 | ✓ Ro5 | ✓ Clean |
C(C(=O)COP(=O)(O)O)O
|
|
| 5UK RCSB PDB | Q9X1X7 | 203.1 Da LogP -1.26 TPSA 135.8 | ✓ Ro5 | ✓ Clean |
[H]/N=C(\[C@H](CC(=O)CO)C(=O)O)/C(=O)O
|
|
| 5XR RCSB PDB | O57767 | 221.2 Da LogP -2.27 TPSA 144.2 | ✓ Ro5 | ✓ Clean |
C(C=O)[C@@H](N[C@@](CC(=O)O)(C(=O)O)O)O
|
|
| 5XW RCSB PDB | O57767 | 203.2 Da LogP -1.11 TPSA 124.3 | ✓ Ro5 | ✓ Clean |
C(C=O)C(/N=C(/CC(=O)O)\C(=O)O)O
|
|
| CIZ RCSB PDB | O57767 | 130.1 Da LogP 0.10 TPSA 74.6 | ✓ Ro5 | ✓ Clean |
C/C(=C/C(=O)O)/C(=O)O
|
|
| DYA RCSB PDB | O57767 | 131.1 Da LogP -1.00 TPSA 100.6 | ✓ Ro5 | ✓ Clean |
C(=C(/C(=O)O)\N)\C(=O)O
|
|
| FLC RCSB PDB | Q9X1X7 | 189.1 Da LogP -5.25 TPSA 140.6 | ✓ Ro5 | ✓ Clean |
C(C(=O)[O-])C(CC(=O)[O-])(C(=O)[O-])O
|
|
| GZ8 RCSB PDB | Q9X1X7 | 198.2 Da LogP 0.64 TPSA 74.6 | ✓ Ro5 | Alert |
C1=CC(=S)C=C(C1C(=O)O)C(=O)O
|
|
| H2S RCSB PDB | Q9X1X7 | 34.1 Da LogP 0.11 TPSA 0.0 | ✓ Ro5 | ✓ Clean |
S
|
|
| ITN RCSB PDB | O57767 | 130.1 Da LogP 0.10 TPSA 74.6 | ✓ Ro5 | ✓ Clean |
C=C(CC(=O)O)C(=O)O
|
|
| LMR RCSB PDB | O57767 | 134.1 Da LogP -1.09 TPSA 94.8 | ✓ Ro5 | ✓ Clean |
C([C@@H](C(=O)O)O)C(=O)O
|
|
| MAE RCSB PDB | O57767 | 116.1 Da LogP -0.29 TPSA 74.6 | ✓ Ro5 | ✓ Clean |
C(=C/C(=O)O)/C(=O)O
|
|
| MLT RCSB PDB | O57767 | 134.1 Da LogP -1.09 TPSA 94.8 | ✓ Ro5 | ✓ Clean |
C([C@H](C(=O)O)O)C(=O)O
|
|
| NH4 RCSB PDB | O57767 | 18.0 Da LogP 0.38 TPSA 36.5 | ✓ Ro5 | ✓ Clean |
[NH4+]
|
|
| NHE RCSB PDB | Q9X1X7 | 207.3 Da LogP 0.80 TPSA 66.4 | ✓ Ro5 | ✓ Clean |
C1CCC(CC1)NCCS(=O)(=O)O
|
|
| NTM RCSB PDB | Q9X1X7 | 167.1 Da LogP 0.48 TPSA 87.5 | ✓ Ro5 | ✓ Clean |
c1cc(c(nc1)C(=O)O)C(=O)O
|
|
| PGH RCSB PDB | Q9X1X7 | 171.0 Da LogP -1.40 TPSA 116.1 | ✓ Ro5 | ✓ Clean |
C(C(=O)NO)OP(=O)(O)O
|
|
| PHT RCSB PDB | Q9X1X7 | 166.1 Da LogP 1.08 TPSA 74.6 | ✓ Ro5 | ✓ Clean |
c1ccc(c(c1)C(=O)O)C(=O)O
|
|
| QAS RCSB PDB | Q9X1X7 | 199.2 Da LogP 0.77 TPSA 87.5 | ✓ Ro5 | ✓ Clean |
c1cc(nc(c1C(=O)O)C(=O)O)S
|
|
| QAT RCSB PDB | Q9X1X7 | 199.2 Da LogP 0.25 TPSA 87.0 | ✓ Ro5 | Alert |
C1C(=S)C=NC(=C1C(=O)O)C(=O)O
|
|
| XQB RCSB PDB | Q9X1X7 | 203.1 Da LogP -1.26 TPSA 135.8 | ✓ Ro5 | ✓ Clean |
[H]/N=C(/[C@H](C[C@@H](C=O)O)C(=O)O)\C(=O)O
|
|
| YQA RCSB PDB | Q9X1X7 | 185.1 Da LogP -0.75 TPSA 107.2 | ✓ Ro5 | ✓ Clean |
C1[C@H](C=NC(=C1C(=O)O)C(=O)O)O
|
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 |
|---|---|---|---|---|---|
| ZINC1710230 ZINC | 1.000 | 207.3 Da LogP 0.80 TPSA 66.4 | ✓ Ro5 | ✓ Clean |
O=S(=O)(O)CCNC1CCCCC1
|
| ZINC2004372 ZINC | 0.786 | 221.3 Da LogP 1.19 TPSA 66.4 | ✓ Ro5 | ✓ Clean |
O=S(=O)(O)CCCNC1CCCCC1
|
| ZINC38364153 ZINC | 0.786 | 235.3 Da LogP 1.58 TPSA 66.4 | ✓ Ro5 | ✓ Clean |
O=S(=O)(O)CCCCNC1CCCCC1
|
| ZINC135598 ZINC | 0.690 | 227.2 Da LogP 2.01 TPSA 67.3 | ✓ Ro5 | ✓ Clean |
O=C(c1ccccc1)c1cccnc1C(=O)O
|
| ZINC343335 ZINC | 0.690 | 227.2 Da LogP 2.01 TPSA 67.3 | ✓ Ro5 | ✓ Clean |
O=C(O)c1cccnc1C(=O)c1ccccc1
|
| ZINC1296728 ZINC | 0.654 | 244.2 Da LogP 1.54 TPSA 100.4 | ✓ Ro5 | ✓ Clean |
O=C(O)c1ncccc1-c1cccnc1C(=O)O
|
| ZINC47217 ZINC | 0.654 | 244.2 Da LogP 1.54 TPSA 100.4 | ✓ Ro5 | ✓ Clean |
O=C(O)c1cccnc1-c1ncccc1C(=O)O
|
| ZINC151254 ZINC | 0.607 | 202.0 Da LogP 1.54 TPSA 50.2 | ✓ Ro5 | ✓ Clean |
O=C(O)c1cccnc1Br
|
| ZINC2456171 ZINC | 0.607 | 202.0 Da LogP 1.54 TPSA 50.2 | ✓ Ro5 | ✓ Clean |
O=C(O)c1ncccc1Br
|
| ZINC39243629 ZINC | 0.607 | 249.0 Da LogP 1.38 TPSA 50.2 | ✓ Ro5 | ✓ Clean |
O=C(O)c1cccnc1I
|
| ZINC5944065 ZINC | 0.607 | 249.0 Da LogP 1.38 TPSA 50.2 | ✓ Ro5 | ✓ Clean |
O=C(O)c1ncccc1I
|
| ZINC20272728 ZINC | 0.606 | 209.2 Da LogP 1.34 TPSA 76.5 | ✓ Ro5 | ✓ Clean |
CC(C)OC(=O)c1ncccc1C(=O)O
|
| ZINC59916715 ZINC | 0.606 | 223.2 Da LogP 1.74 TPSA 76.5 | ✓ Ro5 | ✓ Clean |
CC(C)(C)OC(=O)c1cccnc1C(=O)O
|
| ZINC72233329 ZINC | 0.606 | 209.2 Da LogP 1.34 TPSA 76.5 | ✓ Ro5 | ✓ Clean |
CC(C)OC(=O)c1cccnc1C(=O)O
|
| ZINC2158679 ZINC | 0.588 | 243.2 Da LogP 1.43 TPSA 92.2 | ✓ Ro5 | ✓ Clean |
O=C(Nc1ccccn1)c1cccnc1C(=O)O
|
| ZINC1857793323 ZINC | 0.586 | 320.3 Da LogP 3.21 TPSA 100.4 | ✓ Ro5 | ✓ Clean |
O=C(O)c1cccnc1-c1ccc(-c2ncccc2C(=O)O)cc1
|
| ZINC142147 ZINC | 0.583 | 219.2 Da LogP 1.62 TPSA 57.6 | ✓ Ro5 | ✓ Clean |
O=C(O)c1ccccc1C(=O)N1CCCC1
|
| ZINC2182270 ZINC | 0.583 | 224.2 Da LogP 0.16 TPSA 88.5 | ✓ Ro5 | ✓ Clean |
COCCNC(=O)c1cccnc1C(=O)O
|
| ZINC2575594 ZINC | 0.583 | 270.3 Da LogP 1.75 TPSA 79.3 | ✓ Ro5 | ✓ Clean |
O=C(NCCc1ccccc1)c1cccnc1C(=O)O
|
| ZINC394746 ZINC | 0.583 | 242.2 Da LogP 2.32 TPSA 74.6 | ✓ Ro5 | ✓ Clean |
O=C(O)c1ccccc1C(=O)c1ccc(O)cc1
|
| ZINC1732721 ZINC | 0.571 | 222.2 Da LogP 1.31 TPSA 79.3 | ✓ Ro5 | ✓ Clean |
CCCCNC(=O)c1ncccc1C(=O)O
|
| ZINC40803118 ZINC | 0.571 | 270.3 Da LogP 1.75 TPSA 79.3 | ✓ Ro5 | ✓ Clean |
O=C(O)c1cccnc1C(=O)NCCc1ccccc1
|
| ZINC4649243 ZINC | 0.571 | 286.2 Da LogP 1.73 TPSA 116.6 | ✓ Ro5 | ✓ Clean |
O=C(O)c1ccc(NC(=O)c2cccnc2C(=O)O)cc1
|
| ZINC9694250 ZINC | 0.571 | 286.2 Da LogP 1.73 TPSA 116.6 | ✓ Ro5 | ✓ Clean |
O=C(O)c1ccc(NC(=O)c2ncccc2C(=O)O)cc1
|
| ZINC1602105 ZINC | 0.565 | 242.2 Da LogP 2.75 TPSA 74.6 | ✓ Ro5 | ✓ Clean |
O=C(O)c1ccc(-c2ccccc2)cc1C(=O)O
|
| ZINC41229465 ZINC | 0.563 | 217.2 Da LogP 2.59 TPSA 50.2 | ✓ Ro5 | ✓ Clean |
O=C(O)c1ncccc1-c1ccccc1F
|
| ZINC12137488 ZINC | 0.560 | 247.3 Da LogP 2.40 TPSA 57.6 | ✓ Ro5 | ✓ Clean |
O=C(O)c1ccccc1C(=O)N1CCCCCC1
|
| ZINC143407 ZINC | 0.560 | 221.3 Da LogP 1.91 TPSA 66.4 | ✓ Ro5 | ✓ Clean |
CC(C)(C)NC(=O)c1ccccc1C(=O)O
|
| ZINC167015 ZINC | 0.560 | 205.3 Da LogP 2.38 TPSA 40.5 | ✓ Ro5 | ✓ Clean |
O=C(O)c1ccccc1N1CCCCC1
|
| ZINC1707321 ZINC | 0.560 | 223.2 Da LogP 0.20 TPSA 103.7 | ✓ Ro5 | ✓ Clean |
O=C(O)CNC(=O)c1ccccc1C(=O)O
|
| ZINC185924 ZINC | 0.560 | 249.3 Da LogP 2.64 TPSA 57.6 | ✓ Ro5 | ✓ Clean |
CC(C)N(C(=O)c1ccccc1C(=O)O)C(C)C
|
| ZINC19367005 ZINC | 0.560 | 224.4 Da LogP 2.83 TPSA 24.1 | ✓ Ro5 | ✓ Clean |
C1CCC(NCCNC2CCCCC2)CC1
|
| ZINC2584518 ZINC | 0.560 | 222.2 Da LogP 2.34 TPSA 63.6 | ✓ Ro5 | ✓ Clean |
CC(C)(C)OC(=O)c1ccccc1C(=O)O
|
| ZINC267002 ZINC | 0.560 | 215.3 Da LogP 2.79 TPSA 42.2 | ✓ Ro5 | Alert |
Cc1ccc(C)n1-c1ccccc1C(=O)O
|
| ZINC28115 ZINC | 0.560 | 233.3 Da LogP 2.01 TPSA 57.6 | ✓ Ro5 | ✓ Clean |
O=C(O)c1ccccc1C(=O)N1CCCCC1
|
| ZINC34519769 ZINC | 0.560 | 241.2 Da LogP 2.20 TPSA 80.4 | ✓ Ro5 | ✓ Clean |
Nc1ccc(C(=O)c2ccccc2C(=O)O)cc1
|
| ZINC3847474 ZINC | 0.560 | 240.3 Da LogP 2.92 TPSA 54.4 | ✓ Ro5 | ✓ Clean |
Cc1ccc(C(=O)c2ccccc2C(=O)O)cc1
|
| ZINC4729531 ZINC | 0.560 | 217.2 Da LogP 0.81 TPSA 74.7 | ✓ Ro5 | ✓ Clean |
O=C(O)c1ccccc1N1C(=O)C=CC1=O
|
| ZINC56439 ZINC | 0.560 | 244.2 Da LogP 2.75 TPSA 54.4 | ✓ Ro5 | ✓ Clean |
O=C(O)c1ccccc1C(=O)c1ccc(F)cc1
|
| ZINC5760826 ZINC | 0.560 | 208.2 Da LogP 1.95 TPSA 63.6 | ✓ Ro5 | ✓ Clean |
CC(C)OC(=O)c1ccccc1C(=O)O
|
| ZINC60221109 ZINC | 0.560 | 224.2 Da LogP 0.63 TPSA 100.9 | ✓ Ro5 | ✓ Clean |
O=C(O)COC(=O)c1ccccc1C(=O)O
|
| ZINC26468763 ZINC | 0.559 | 243.3 Da LogP -1.35 TPSA 100.5 | ✓ Ro5 | ✓ Clean |
O=S(=O)(O)CCN[C@@H]1CCS(=O)(=O)C1
|
| ZINC26468770 ZINC | 0.559 | 243.3 Da LogP -1.35 TPSA 100.5 | ✓ Ro5 | ✓ Clean |
O=S(=O)(O)CCN[C@H]1CCS(=O)(=O)C1
|
| ZINC1563686 ZINC | 0.556 | 257.2 Da LogP 2.02 TPSA 76.5 | ✓ Ro5 | ✓ Clean |
COc1ccc(C(=O)c2cccnc2C(=O)O)cc1
|
| ZINC5188799 ZINC | 0.556 | 280.5 Da LogP 4.39 TPSA 24.1 | ✓ Ro5 | ✓ Clean |
C(CCCNC1CCCCC1)CCNC1CCCCC1
|
| ZINC6701074 ZINC | 0.556 | 243.2 Da LogP 1.43 TPSA 92.2 | ✓ Ro5 | ✓ Clean |
O=C(Nc1cccnc1)c1cccnc1C(=O)O
|
| ZINC82485552 ZINC | 0.556 | 220.2 Da LogP 0.92 TPSA 79.3 | ✓ Ro5 | ✓ Clean |
O=C(O)c1cccnc1C(=O)NCC1CC1
|
| ZINC95938319 ZINC | 0.550 | 252.2 Da LogP 0.85 TPSA 162.8 | 1 viol. | ✓ Clean |
N=C(O)c1cc(C(=N)O)c(C(=O)O)cc1C(=O)O
|
| ZINC6471224 ZINC | 0.548 | 203.2 Da LogP 0.03 TPSA 104.6 | ✓ Ro5 | ✓ Clean |
O=C(O)c1cccnc1S(=O)(=O)O
|
| ZINC65347090 ZINC | 0.548 | 215.2 Da LogP 2.15 TPSA 70.4 | ✓ Ro5 | ✓ Clean |
O=C(O)c1ncccc1-c1ccccc1O
|
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.