Protein target profile
KP13_00203
putative 8-amino-7-oxononanoate synthase/2-amino-3-ketobutyrate coenzyme A ligase
Target candidate with partial support; inspect missing evidence before prioritizing.
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
- Hit
- Human identity (%)
- 55.385 Lower values reduce human off-target concern.
- Human E-value
- 1.78e-149
- Gut microbiome similarity
- 15.0% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.
Essentiality
- Essential (DEG)
- N
- DEG identity (%)
- 0.0 Higher values support similarity to known essential genes.
Localization
- Localization
- Cytoplasmic
Structure confidence
- ColabFold pLDDT
- 98.23 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
Chemistry
Sequence
Primary amino-acid sequence viewer.
MRGDFYKQLTSNLETARAEGLFKEERIITSAQQADITVGDSHVINFCANNYLGLANHPELIAAAKSGMDSHGFGMASVRFICGTQDTHKQLEKKLADFLGMEDAILYSSCFDANGGLFETLLGPEDAIISDALNHASIIDGVRLCKAKRFRYANNDMQELEARLKEAREAGARHVLIATDGVFSMDGVIANLQGVCDLADKYDALVMVDDSHAVGFVGENGRGSHEYCDVMGRVDIITGTLGKALGGASGGYTAARKEVVEWLRQRSRPYLFSNSLAPAIVAASIKVLEMVEEGADLRDRLWANARLFREKMTAAGFTLAGADHAIIPVMLGEAVVAQNFARELQKEGIYVTGFFYPVVPKGQARIRTQMSAAHTPEQIERAVEAFTRIGKQLGVIA
Functional annotations
Enzyme classification and Gene Ontology terms linked to this protein.
Enzyme Commission (EC)
1Gene Ontology (GO)
9- GO:0030170 Binding to pyridoxal 5' phosphate, 3-hydroxy-5-(hydroxymethyl)-2-methyl4-pyridine carboxaldehyde 5' phosphate, the biologically active form of vitamin B6.
- GO:0009058 A cellular process consisting of the biochemical pathways by which a living organism synthesizes chemical substances. This typically represents the energy-requiring part of metabolism in which simpler substances are transformed into more complex ones.
- GO:0016740 Catalysis of the transfer of a group, e.g. a methyl group, glycosyl group, acyl group, phosphorus-containing, or other groups, from one compound (generally regarded as the donor) to another compound (generally regarded as the acceptor). Transferase is the systematic name for any enzyme of EC class 2.
- 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:0006567 The chemical reactions and pathways resulting in the breakdown of L-threonine.
- GO:0008890 Catalysis of the reaction: acetyl-CoA + glycine = L-2-amino-3-oxobutanoate + CoA.
- GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
- GO:0016874 Catalysis of the joining of two molecules, or two groups within a single molecule, using the energy from the hydrolysis of ATP, a similar triphosphate, or a pH gradient.
- GO:0019518 OBSOLETE. The chemical reactions and pathways resulting in the breakdown of L-threonine (the L-enantiomer of 2-amino-3-hydroxybutyric acid) to form 2-amino-3-oxobutanoate, which is subsequently converted to glycine.
Sequence domains and features
Domain and signature matches imported from InterPro and related databases.
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 294 | 386 | FunFam | G3DSA:3.90.1150.10:FF:000004 | 2-amino-3-ketobutyrate coenzyme A ligase |
| 240 | 249 | ProSitePatterns | PS00599 | Aminotransferases class-II pyridoxal-phosphate attachment site. |
| 240 | 249 | InterPro | IPR001917 | Aminotransferase, class-II, pyridoxal-phosphate binding site |
| 2 | 394 | Hamap | MF_00985 | 2-amino-3-ketobutyrate coenzyme A ligase [kbl]. |
| 2 | 394 | InterPro | IPR011282 | 2-amino-3-ketobutyrate coenzyme A ligase |
| 57 | 295 | FunFam | G3DSA:3.40.640.10:FF:000006 | 5-aminolevulinate synthase, mitochondrial |
| 14 | 388 | PANTHER | PTHR13693 | CLASS II AMINOTRANSFERASE/8-AMINO-7-OXONONANOATE SYNTHASE |
| 39 | 387 | Gene3D | G3DSA:3.90.1150.10 | Aspartate Aminotransferase, domain 1 |
| 39 | 387 | InterPro | IPR015422 | Pyridoxal phosphate-dependent transferase, small domain |
| 57 | 295 | Gene3D | G3DSA:3.40.640.10 | - |
| 57 | 295 | InterPro | IPR015421 | Pyridoxal phosphate-dependent transferase, major domain |
| 42 | 386 | Pfam | PF00155 | Aminotransferase class I and II |
| 42 | 386 | InterPro | IPR004839 | Aminotransferase, class I/classII |
| 5 | 396 | NCBIfam | TIGR01822 | glycine C-acetyltransferase |
| 5 | 396 | InterPro | IPR011282 | 2-amino-3-ketobutyrate coenzyme A ligase |
| 4 | 395 | SUPERFAMILY | SSF53383 | PLP-dependent transferases |
| 4 | 395 | InterPro | IPR015424 | Pyridoxal phosphate-dependent transferase |
| 41 | 390 | CDD | cd06454 | KBL_like |
| 150 | 170 | Coils | Coil | Coil |
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 · P2Rank
Probability: high ≥ 0.5 · medium 0.2–0.49 · low < 0.2
Residue sets
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_A0A0H3H4H3
|
AlphaFold DB | — | — | full sequence | — | Viewing |
|
ColabFold
KP13_00203
|
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 and bioactivity evidence are both 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 |
|---|---|---|---|---|---|---|
| 2BK RCSB PDB | Q0K313 | 350.3 Da LogP -0.37 TPSA 169.4 | 1 viol. | ✓ Clean |
Cc1c(c(c(cn1)COP(=O)(O)O)CN[C@@H]([C@H](C)O)C(=…
|
|
| AKB RCSB PDB | P0AB77 | 117.1 Da LogP -1.01 TPSA 80.4 | ✓ Ro5 | ✓ Clean |
CC(=O)[C@@H](C(=O)O)N
|
|
| F9X RCSB PDB | Q0K313 | 364.3 Da LogP 0.02 TPSA 169.4 | 1 viol. | ✓ Clean |
CC[C@H]([C@@H](C(=O)O)NCc1c(cnc(c1O)C)COP(=O)(O…
|
|
| HR5 RCSB PDB | P22557 | 207.3 Da LogP 1.26 TPSA 46.9 | ✓ Ro5 | ✓ Clean |
Cc1c(cnn1C)C(=O)NCC2CCC2
|
|
| J4Q RCSB PDB | P22557 | 243.3 Da LogP 0.79 TPSA 64.8 | ✓ Ro5 | ✓ Clean |
CS(=O)(=O)c1nccn1Cc2cscn2
|
|
| JHP RCSB PDB | P22557 | 227.7 Da LogP 1.75 TPSA 46.9 | ✓ Ro5 | ✓ Clean |
Cn1cc(c(n1)C(=O)NC2CCCC2)Cl
|
|
| JO1 RCSB PDB | P22557 | 221.3 Da LogP 1.41 TPSA 46.9 | ✓ Ro5 | ✓ Clean |
Cn1c(ccn1)C(=O)NCc2cccs2
|
|
| K0V RCSB PDB | P22557 | 242.3 Da LogP 1.38 TPSA 58.6 | ✓ Ro5 | ✓ Clean |
CC(C)(C)NC(=O)N1CCC(CC1)C(=O)OC
|
|
| LUY RCSB PDB | P22557 | 237.3 Da LogP 3.22 TPSA 40.7 | ✓ Ro5 | ✓ Clean |
c1ccc(cc1)CCNc2[nH]c3ccccc3n2
|
|
| NSJ RCSB PDB | P22557 | 209.3 Da LogP 1.94 TPSA 23.5 | ✓ Ro5 | ✓ Clean |
c1cc(cc(c1)O)CN2CCSCC2
|
|
| NSV RCSB PDB | P22557 | 197.3 Da LogP 0.86 TPSA 28.2 | ✓ Ro5 | ✓ Clean |
Cc1ncc(s1)CN2CCNCC2
|
|
| NT7 RCSB PDB | P22557 | 248.3 Da LogP 1.57 TPSA 41.6 | ✓ Ro5 | ✓ Clean |
Cc1cccc(c1C)NC(=O)CN2CCOCC2
|
|
| NTG RCSB PDB | P22557 | 203.2 Da LogP 1.18 TPSA 49.2 | ✓ Ro5 | ✓ Clean |
c1cc(ncc1N2CCCOCC2)C#N
|
|
| NTV RCSB PDB | P22557 | 239.7 Da LogP 2.77 TPSA 38.3 | ✓ Ro5 | ✓ Clean |
Cc1c(cccc1Cl)NC(=O)[C@@H]2CCCO2
|
|
| NU4 RCSB PDB | P22557 | 202.2 Da LogP 2.24 TPSA 55.1 | ✓ Ro5 | ✓ Clean |
Cc1c(cco1)C(=O)Nc2ccncc2
|
|
| NUA RCSB PDB | P22557 | 193.2 Da LogP 1.64 TPSA 46.9 | ✓ Ro5 | ✓ Clean |
CCn1cc(cn1)NC(=O)C2CCC2
|
|
| NUG RCSB PDB | P22557 | 199.3 Da LogP 1.12 TPSA 23.5 | ✓ Ro5 | ✓ Clean |
C1CN(CCC1O)CC2=CCSC2
|
|
| NUJ RCSB PDB | P22557 | 207.3 Da LogP 1.05 TPSA 49.2 | ✓ Ro5 | ✓ Clean |
Cc1cc(nc(n1)C)N(C)C2CC(C2)O
|
|
| NUM RCSB PDB | P22557 | 242.3 Da LogP 1.76 TPSA 62.2 | ✓ Ro5 | ✓ Clean |
c1ccnc(c1)C(=O)NCCc2ccc(cc2)O
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|
| NUY RCSB PDB | P22557 | 238.4 Da LogP 1.91 TPSA 23.6 | ✓ Ro5 | ✓ Clean |
CC(C)N1CCN(CC1)C(=O)c2cccs2
|
|
| NV7 RCSB PDB | P22557 | 244.3 Da LogP 0.36 TPSA 53.8 | ✓ Ro5 | ✓ Clean |
CS(=O)(=O)N1CCN(CC1)Cc2ccco2
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|
| NVD RCSB PDB | P22557 | 217.3 Da LogP 1.09 TPSA 46.0 | ✓ Ro5 | Alert |
CN(C)c1ccc(cc1)CNn2cnnc2
|
|
| NVJ RCSB PDB | P22557 | 179.2 Da LogP 1.93 TPSA 38.3 | ✓ Ro5 | ✓ Clean |
CCOC(=O)NCc1ccccc1
|
|
| NVM RCSB PDB | P22557 | 222.3 Da LogP 2.53 TPSA 33.2 | ✓ Ro5 | ✓ Clean |
C[C@H]1CCN(C=CC1)C(=O)c2cscn2
|
|
| NVY RCSB PDB | P22557 | 222.3 Da LogP 2.72 TPSA 15.3 | ✓ Ro5 | ✓ Clean |
CCN1CCC(CC1)Nc2ccccc2F
|
|
| NW4 RCSB PDB | P22557 | 225.3 Da LogP 2.21 TPSA 29.5 | ✓ Ro5 | ✓ Clean |
C1CCC(CC1)CCC(=O)N2CCOCC2
|
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| NW7 RCSB PDB | P22557 | 235.2 Da LogP 2.09 TPSA 81.2 | ✓ Ro5 | ✓ Clean |
CCc1c(c(on1)C)C(=O)Nc2cc(on2)C
|
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| PE3 RCSB PDB | P09950 | 634.8 Da LogP -0.81 TPSA 160.5 | 2 viol. | ✓ Clean |
C(COCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO)O
|
|
| PLG RCSB PDB | Q0K313 | 306.2 Da LogP -0.12 TPSA 149.2 | ✓ Ro5 | ✓ Clean |
Cc1c(c(c(cn1)COP(=O)(O)O)CNCC(=O)O)O
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| PLS RCSB PDB | Q93UV0 | 336.2 Da LogP -0.76 TPSA 169.4 | 1 viol. | ✓ Clean |
Cc1c(c(c(cn1)COP(=O)(O)O)CN[C@@H](CO)C(=O)O)O
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| PMP RCSB PDB | Q93UV0 | 248.2 Da LogP 0.16 TPSA 125.9 | ✓ Ro5 | ✓ Clean |
Cc1c(c(c(cn1)COP(=O)(O)O)CN)O
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| SCA RCSB PDB | P18079 | 867.6 Da LogP -1.47 TPSA 400.9 | 3 viol. | ✓ Clean |
CC(C)(CO[P@@](=O)(O)O[P@](=O)(O)OC[C@@H]1[C@H](…
|
|
| SIN RCSB PDB | P18079 | 118.1 Da LogP -0.06 TPSA 74.6 | ✓ Ro5 | ✓ Clean |
C(CC(=O)O)C(=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).
| Ligand | UniProt (homolog) | pchembl | MW · LogP · TPSA | Lipinski | PAINS | SMILES |
|---|---|---|---|---|---|---|
| CHEMBL207222 ChEMBL | Q93UV0 | — | 149.2 Da LogP 0.11 TPSA 63.3 | ✓ Ro5 | ✓ Clean |
CC(C)(S)[C@H](N)C(=O)O
|
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 |
|---|---|---|---|---|---|
| ZINC1016488 ZINC | 1.000 | 242.3 Da LogP 1.76 TPSA 62.2 | ✓ Ro5 | ✓ Clean |
O=C(NCCc1ccc(O)cc1)c1ccccn1
|
| ZINC1019104 ZINC | 1.000 | 221.3 Da LogP 1.41 TPSA 46.9 | ✓ Ro5 | ✓ Clean |
Cn1nccc1C(=O)NCc1cccs1
|
| ZINC12501520 ZINC | 1.000 | 458.5 Da LogP -0.88 TPSA 123.5 | 1 viol. | ✓ Clean |
OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO
|
| ZINC1516906 ZINC | 1.000 | 202.2 Da LogP 2.24 TPSA 55.1 | ✓ Ro5 | ✓ Clean |
Cc1occc1C(=O)Nc1ccncc1
|
| ZINC1532708 ZINC | 1.000 | 248.2 Da LogP 0.16 TPSA 125.9 | ✓ Ro5 | ✓ Clean |
Cc1ncc(COP(=O)(O)O)c(CN)c1O
|
| ZINC19235648 ZINC | 1.000 | 248.3 Da LogP 1.57 TPSA 41.6 | ✓ Ro5 | ✓ Clean |
Cc1cccc(NC(=O)CN2CCOCC2)c1C
|
| ZINC19787430 ZINC | 1.000 | 244.3 Da LogP 0.36 TPSA 53.8 | ✓ Ro5 | ✓ Clean |
CS(=O)(=O)N1CCN(Cc2ccco2)CC1
|
| ZINC237165 ZINC | 1.000 | 209.3 Da LogP 1.94 TPSA 23.5 | ✓ Ro5 | ✓ Clean |
Oc1cccc(CN2CCSCC2)c1
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| ZINC26143362 ZINC | 1.000 | 207.3 Da LogP 1.26 TPSA 46.9 | ✓ Ro5 | ✓ Clean |
Cc1c(C(=O)NCC2CCC2)cnn1C
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| ZINC373530 ZINC | 1.000 | 235.2 Da LogP 2.09 TPSA 81.2 | ✓ Ro5 | ✓ Clean |
CCc1noc(C)c1C(=O)Nc1cc(C)on1
|
| ZINC3874716 ZINC | 1.000 | 414.5 Da LogP -0.90 TPSA 114.3 | ✓ Ro5 | ✓ Clean |
OCCOCCOCCOCCOCCOCCOCCOCCOCCO
|
| ZINC4283769 ZINC | 1.000 | 238.3 Da LogP -0.96 TPSA 77.4 | ✓ Ro5 | ✓ Clean |
OCCOCCOCCOCCOCCO
|
| ZINC4521548 ZINC | 1.000 | 282.3 Da LogP -0.95 TPSA 86.6 | ✓ Ro5 | ✓ Clean |
OCCOCCOCCOCCOCCOCCO
|
| ZINC460647 ZINC | 1.000 | 225.3 Da LogP 2.21 TPSA 29.5 | ✓ Ro5 | ✓ Clean |
O=C(CCC1CCCCC1)N1CCOCC1
|
| ZINC467615 ZINC | 1.000 | 227.7 Da LogP 1.75 TPSA 46.9 | ✓ Ro5 | ✓ Clean |
Cn1cc(Cl)c(C(=O)NC2CCCC2)n1
|
| ZINC468583 ZINC | 1.000 | 217.3 Da LogP 1.09 TPSA 46.0 | ✓ Ro5 | Alert |
CN(C)c1ccc(CNn2cnnc2)cc1
|
| ZINC513006 ZINC | 1.000 | 237.3 Da LogP 3.22 TPSA 40.7 | ✓ Ro5 | ✓ Clean |
c1ccc(CCNc2nc3ccccc3[nH]2)cc1
|
| ZINC5178829 ZINC | 1.000 | 326.4 Da LogP -0.93 TPSA 95.8 | ✓ Ro5 | ✓ Clean |
OCCOCCOCCOCCOCCOCCOCCO
|
| ZINC5178830 ZINC | 1.000 | 370.4 Da LogP -0.91 TPSA 105.1 | ✓ Ro5 | ✓ Clean |
OCCOCCOCCOCCOCCOCCOCCOCCO
|
| ZINC55250732 ZINC | 1.000 | 238.4 Da LogP 1.91 TPSA 23.6 | ✓ Ro5 | ✓ Clean |
CC(C)N1CCN(C(=O)c2cccs2)CC1
|
| ZINC766484 ZINC | 1.000 | 222.3 Da LogP 2.72 TPSA 15.3 | ✓ Ro5 | ✓ Clean |
CCN1CCC(Nc2ccccc2F)CC1
|
| ZINC800871 ZINC | 1.000 | 242.3 Da LogP 1.38 TPSA 58.6 | ✓ Ro5 | ✓ Clean |
COC(=O)C1CCN(C(=O)NC(C)(C)C)CC1
|
| ZINC804571 ZINC | 1.000 | 239.7 Da LogP 2.77 TPSA 38.3 | ✓ Ro5 | ✓ Clean |
Cc1c(Cl)cccc1NC(=O)[C@H]1CCCO1
|
| ZINC804572 ZINC | 1.000 | 239.7 Da LogP 2.77 TPSA 38.3 | ✓ Ro5 | ✓ Clean |
Cc1c(Cl)cccc1NC(=O)[C@@H]1CCCO1
|
| ZINC96447797 ZINC | 1.000 | 243.3 Da LogP 0.79 TPSA 64.8 | ✓ Ro5 | ✓ Clean |
CS(=O)(=O)c1nccn1Cc1cscn1
|
| ZINC97115406 ZINC | 1.000 | 207.3 Da LogP 1.05 TPSA 49.2 | ✓ Ro5 | ✓ Clean |
Cc1cc(N(C)C2CC(O)C2)nc(C)n1
|
| ZINC97227385 ZINC | 1.000 | 203.2 Da LogP 1.18 TPSA 49.2 | ✓ Ro5 | ✓ Clean |
N#Cc1ccc(N2CCCOCC2)cn1
|
| ZINC2487640 ZINC | 0.971 | 241.7 Da LogP 2.14 TPSA 46.9 | ✓ Ro5 | ✓ Clean |
Cn1cc(Cl)c(C(=O)NC2CCCCC2)n1
|
| ZINC468315 ZINC | 0.971 | 255.7 Da LogP 2.53 TPSA 46.9 | ✓ Ro5 | ✓ Clean |
Cn1cc(Cl)c(C(=O)NC2CCCCCC2)n1
|
| ZINC5382476 ZINC | 0.966 | 211.3 Da LogP 1.82 TPSA 29.5 | ✓ Ro5 | ✓ Clean |
O=C(CCC1CCCC1)N1CCOCC1
|
| ZINC58393643 ZINC | 0.944 | 207.3 Da LogP 2.03 TPSA 46.9 | ✓ Ro5 | ✓ Clean |
CCn1cc(NC(=O)C2CCCC2)cn1
|
| ZINC65535452 ZINC | 0.919 | 221.3 Da LogP 2.42 TPSA 46.9 | ✓ Ro5 | ✓ Clean |
CCn1cc(NC(=O)C2CCCCC2)cn1
|
| ZINC2748482 ZINC | 0.821 | 280.3 Da LogP 2.18 TPSA 76.7 | ✓ Ro5 | ✓ Clean |
CCOC(=O)NCc1ccc(CNC(=O)OCC)cc1
|
| ZINC311613615 ZINC | 0.814 | 265.4 Da LogP 1.26 TPSA 67.2 | ✓ Ro5 | ✓ Clean |
Cc1c(C(=O)NC[C@H]2CCC[C@@H](CO)C2)cnn1C
|
| ZINC20180646 ZINC | 0.806 | 268.3 Da LogP 0.98 TPSA 60.9 | ✓ Ro5 | ✓ Clean |
C[C@H](C(=O)O)N1CCN(C(=O)c2cccs2)CC1
|
| ZINC20180647 ZINC | 0.806 | 268.3 Da LogP 0.98 TPSA 60.9 | ✓ Ro5 | ✓ Clean |
C[C@@H](C(=O)O)N1CCN(C(=O)c2cccs2)CC1
|
| ZINC3334151 ZINC | 0.806 | 226.3 Da LogP 2.05 TPSA 42.0 | ✓ Ro5 | ✓ Clean |
O=C(NCCc1ccccc1)c1ccccn1
|
| ZINC19973461 ZINC | 0.800 | 234.3 Da LogP 1.27 TPSA 41.6 | ✓ Ro5 | ✓ Clean |
Cc1ccccc1NC(=O)CN1CCOCC1
|
| ZINC8084935 ZINC | 0.789 | 260.7 Da LogP 2.71 TPSA 42.0 | ✓ Ro5 | ✓ Clean |
O=C(NCCc1ccc(Cl)cc1)c1ccccn1
|
| ZINC42079857 ZINC | 0.788 | 236.3 Da LogP 1.05 TPSA 67.4 | ✓ Ro5 | ✓ Clean |
CCOC(=O)NCC(=O)NCc1ccccc1
|
| ZINC220477 ZINC | 0.784 | 236.3 Da LogP 3.11 TPSA 15.3 | ✓ Ro5 | ✓ Clean |
CCCN1CCC(Nc2ccccc2F)CC1
|
| ZINC475979 ZINC | 0.781 | 324.3 Da LogP 3.99 TPSA 84.5 | ✓ Ro5 | ✓ Clean |
Cc1occc1C(=O)Nc1ccc(NC(=O)c2ccoc2C)cc1
|
| ZINC35781317 ZINC | 0.780 | 222.3 Da LogP 0.84 TPSA 59.0 | ✓ Ro5 | ✓ Clean |
CCn1cc(NC(=O)C2CCNCC2)cn1
|
| ZINC20190338 ZINC | 0.778 | 258.3 Da LogP 0.75 TPSA 53.8 | ✓ Ro5 | ✓ Clean |
CCS(=O)(=O)N1CCN(Cc2ccco2)CC1
|
| ZINC6704044 ZINC | 0.775 | 232.3 Da LogP 2.34 TPSA 32.3 | ✓ Ro5 | ✓ Clean |
Cc1cccc(NC(=O)CN2CCCC2)c1C
|
| ZINC198808 ZINC | 0.774 | 306.4 Da LogP 2.41 TPSA 40.6 | ✓ Ro5 | ✓ Clean |
O=C(c1cccs1)N1CCN(C(=O)c2cccs2)CC1
|
| ZINC213884 ZINC | 0.774 | 280.3 Da LogP 2.18 TPSA 76.7 | ✓ Ro5 | ✓ Clean |
CCOC(=O)NCc1cccc(CNC(=O)OCC)c1
|
| ZINC1532705 ZINC | 0.769 | 249.2 Da LogP 0.20 TPSA 120.1 | ✓ Ro5 | ✓ Clean |
Cc1ncc(COP(=O)(O)O)c(CO)c1O
|
| ZINC269633 ZINC | 0.769 | 292.3 Da LogP 3.83 TPSA 55.1 | ✓ Ro5 | ✓ Clean |
Cc1occc1C(=O)Nc1ccc(Cc2ccncc2)cc1
|
| ZINC8264974 ZINC | 0.769 | 244.3 Da LogP 2.19 TPSA 42.0 | ✓ Ro5 | ✓ Clean |
O=C(NCCc1ccc(F)cc1)c1ccccn1
|
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.