Amino acids
521
Annotations
11
Features
44
PDB binders
4
Druggability
0.684
Overview
Basic information about this protein and its source genome.
- Accession
- PA0140
- Gene
- PA0140 ahpF
- Status
- annotated
- Amino acids
- 521
- Structure source
- AlphaFold
EC
GO
GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
GO:0032991 A stable assembly of two or more macromolecules, i.e. proteins, nucleic acids, carbohydrates or lipids, in which at least one component is a protein and the constituent parts function together.
GO:0050660 Binding to FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2.
GO:0051287 Binding to nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NAD+, or the reduced form, NADH.
GO:0102039 Catalysis of the reaction: a hydroperoxide + H+ + NADH = an alcohol + H2O + NAD+.
GO:0004791 Catalysis of the reaction: thioredoxin-dithiol + NADP+ = thioredoxin-disulfide + H+ + NADPH.
Target profile
Computed evidence for target prioritization.
- Human off-target
- hit
- Human identity (%)
- 25.538
- Human E-value
- 9.27e-07
- Gut microbiome off-target
- hit
- Essential (DEG)
- N
- Localization
- CytoplasmicMembrane
Selected Druggability evidence
Selected 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
0.684
Sequence
Primary amino-acid sequence viewer.
MLDANLKTQLKAYLEKVSQPFEIVASLDDSDKSRELLGLLQDIVGLTDKITLKTDGSDARKPSFSLNRPGADIGLRFAGIPMGHEFTSLVLALLQVGGHPSKLDADVIEQVKGIEGTFEFETYFSLSCQNCPDVVQALNLMAVLNPNIRHVAIDGALFQDEVEARQIMSVPSIYLNGEVFGQGRMGVEEILAKIDTGAAARDAEKLTARDAFDVLVVGGGPAGAAAAIYAARKGIRTGVAAERFGGQVLDTMAIENFISVQETEGPKLARALEEHVRHYEVDIMNLQRASKLVPAKNAGELHEVRFESGGSLKAKTLILATGARWREMGVPGEQEYKAKGVCFCPHCDGPLFKGKRVAVIGGGNSGVEAAIDLAGIVAHVTLLEFDSKLRADAVLQRKLYSLPNVEVITSALTSEVKGDGQKVTGLVYKDRNSEEFKSIELEGIFVQIGLLPNTEWLKGSVELSPRGEIIVDARGETSLPGIFAAGDVTTVPYKQIVIAVGEGAKASLSAFDHLIRTSAPE
Functional Annotations
Enzyme classification and Gene Ontology terms linked to this protein.
1 EC
10 GO
Enzyme Commission (EC)
1Gene Ontology (GO)
10- GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
- GO:0032991 A stable assembly of two or more macromolecules, i.e. proteins, nucleic acids, carbohydrates or lipids, in which at least one component is a protein and the constituent parts function together.
- GO:0050660 Binding to FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2.
- GO:0051287 Binding to nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NAD+, or the reduced form, NADH.
- GO:0102039 Catalysis of the reaction: a hydroperoxide + H+ + NADH = an alcohol + H2O + NAD+.
- GO:0004791 Catalysis of the reaction: thioredoxin-dithiol + NADP+ = thioredoxin-disulfide + H+ + NADPH.
- GO:0045454 Any process that maintains the redox environment of a cell or compartment within a cell.
- GO:0000302 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a reactive oxygen species stimulus. Reactive oxygen species include singlet oxygen, superoxide, and oxygen free radicals.
- GO:0016491 Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.
- GO:0008785 Catalysis of the reaction: octane hydroperoxide + NADH + H+ = H2O + NAD+ + 1-octanol.
Sequence Features
Domain/signature hits from InterPro and related databases.
44 records
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 356 | 374 | PRINTS | PR00368 | FAD-dependent pyridine nucleotide reductase signature |
| 441 | 457 | PRINTS | PR00368 | FAD-dependent pyridine nucleotide reductase signature |
| 314 | 332 | PRINTS | PR00368 | FAD-dependent pyridine nucleotide reductase signature |
| 467 | 489 | PRINTS | PR00368 | FAD-dependent pyridine nucleotide reductase signature |
| 214 | 233 | PRINTS | PR00368 | FAD-dependent pyridine nucleotide reductase signature |
| 211 | 515 | PANTHER | PTHR48105 | THIOREDOXIN REDUCTASE 1-RELATED-RELATED |
| 269 | 289 | Coils | Coil | Coil |
| 344 | 364 | ProSitePatterns | PS00573 | Pyridine nucleotide-disulphide oxidoreductases class-II active site. |
| 344 | 364 | InterPro | IPR008255 | Pyridine nucleotide-disulphide oxidoreductase, class-II, active site |
| 103 | 196 | SUPERFAMILY | SSF52833 | Thioredoxin-like |
| 103 | 196 | InterPro | IPR036249 | Thioredoxin-like superfamily |
| 105 | 193 | CDD | cd03026 | AhpF_NTD_C |
| 105 | 193 | InterPro | IPR044141 | AhpF, N-terminal domain, C-terminal TRX-fold subdomain |
| 108 | 207 | ProSiteProfiles | PS51354 | Glutaredoxin domain profile. |
| 326 | 449 | Gene3D | G3DSA:3.50.50.60 | - |
| 326 | 449 | InterPro | IPR036188 | FAD/NAD(P)-binding domain superfamily |
| 202 | 513 | SUPERFAMILY | SSF51905 | FAD/NAD(P)-binding domain |
| 202 | 513 | InterPro | IPR036188 | FAD/NAD(P)-binding domain superfamily |
| 1 | 199 | Gene3D | G3DSA:3.40.30.80 | - |
| 1 | 199 | FunFam | G3DSA:3.40.30.80:FF:000001 | Alkyl hydroperoxide reductase subunit F |
| 326 | 449 | FunFam | G3DSA:3.50.50.60:FF:000007 | Alkyl hydroperoxide reductase, F subunit |
| 1 | 520 | PIRSF | PIRSF000238 | AhpF |
| 1 | 520 | InterPro | IPR012081 | Alkyl hydroperoxide reductase subunit F |
| 265 | 275 | PRINTS | PR00469 | Pyridine nucleotide disulphide reductase class-II signature |
| 245 | 260 | PRINTS | PR00469 | Pyridine nucleotide disulphide reductase class-II signature |
| 213 | 235 | PRINTS | PR00469 | Pyridine nucleotide disulphide reductase class-II signature |
| 315 | 323 | PRINTS | PR00469 | Pyridine nucleotide disulphide reductase class-II signature |
| 352 | 376 | PRINTS | PR00469 | Pyridine nucleotide disulphide reductase class-II signature |
| 443 | 464 | PRINTS | PR00469 | Pyridine nucleotide disulphide reductase class-II signature |
| 337 | 349 | PRINTS | PR00469 | Pyridine nucleotide disulphide reductase class-II signature |
| 404 | 420 | PRINTS | PR00469 | Pyridine nucleotide disulphide reductase class-II signature |
| 477 | 495 | PRINTS | PR00469 | Pyridine nucleotide disulphide reductase class-II signature |
| 124 | 192 | Pfam | PF13192 | Thioredoxin domain |
| 124 | 192 | InterPro | IPR012336 | Thioredoxin-like fold |
| 1 | 100 | SUPERFAMILY | SSF52833 | Thioredoxin-like |
| 1 | 100 | InterPro | IPR036249 | Thioredoxin-like superfamily |
| 214 | 510 | Gene3D | G3DSA:3.50.50.60 | - |
| 214 | 510 | InterPro | IPR036188 | FAD/NAD(P)-binding domain superfamily |
| 1 | 516 | NCBIfam | TIGR03140 | alkyl hydroperoxide reductase subunit F |
| 1 | 516 | InterPro | IPR012081 | Alkyl hydroperoxide reductase subunit F |
| 212 | 503 | Pfam | PF07992 | Pyridine nucleotide-disulphide oxidoreductase |
| 212 | 503 | InterPro | IPR023753 | FAD/NAD(P)-binding domain |
| 1 | 94 | CDD | cd02974 | AhpF_NTD_N |
| 1 | 94 | InterPro | IPR044142 | AhpF, N-terminal domain, N-terminal TRX-fold subdomain |
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...
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Structural evidence
0 + 1Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.
| Entry | Method | Resolution | Chain | Coverage | Links | Status |
|---|---|---|---|---|---|---|
|
AlphaFold
PA0140
|
AlphaFold | — | — | full sequence | — | Viewing |
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 |
|---|---|---|---|---|---|---|---|
| 1 | 0.254 |
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.
70 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 |
|---|---|---|---|---|---|---|
| 3AA | P0A9P4 | 716.4 Da LogP -2.42 TPSA 347.7 | 3 viol. | ✓ Clean |
c1cc(c[n+](c1)[C@H]2[C@@H]([C@@H]([C@H](O2)CO[P…
|
|
| FDA | Q8YID2 | 787.6 Da LogP -1.75 TPSA 363.3 | 3 viol. | ✓ Clean |
Cc1cc2c(cc1C)N(C3=C(N2)C(=O)NC(=O)N3)C[C@@H]([C…
|
|
| MLI | A0A229Y1X4 | 102.0 Da LogP -3.12 TPSA 80.3 | ✓ Ro5 | ✓ Clean |
C(C(=O)[O-])C(=O)[O-]
|
|
| MLT | A0A229Y1X4 | 134.1 Da LogP -1.09 TPSA 94.8 | ✓ Ro5 | ✓ Clean |
C([C@H](C(=O)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 |
|---|---|---|---|---|---|---|
| CHEMBL2035464 | P0A9P4 | 8.00 | 478.3 Da LogP 2.69 TPSA 44.0 | ✓ Ro5 | ✓ Clean |
O=c1c2ccccc2[se]n1CCCCCCn1[se]c2ccccc2c1=O
|
| CHEMBL2035461 | P0A9P4 | 7.40 | 436.2 Da LogP 1.52 TPSA 44.0 | ✓ Ro5 | ✓ Clean |
O=c1c2ccccc2[se]n1CCCn1[se]c2ccccc2c1=O
|
| CHEMBL2035460 | P0A9P4 | 7.30 | 422.2 Da LogP 1.13 TPSA 44.0 | ✓ Ro5 | ✓ Clean |
O=c1c2ccccc2[se]n1CCn1[se]c2ccccc2c1=O
|
| CHEMBL3655713 | P0A9P4 | 6.60 | 322.7 Da LogP 3.01 TPSA 22.0 | ✓ Ro5 | ✓ Clean |
Cc1cc(Cl)ccc1-n1[se]c2ccccc2c1=O
|
| CHEMBL3655720 | P0A9P4 | 6.60 | 320.2 Da LogP 1.35 TPSA 78.0 | ✓ Ro5 | ✓ Clean |
O=c1c2ccccc2[se]n1-c1ncccc1[N+](=O)[O-]
|
| CHEMBL51085 | P0A9P4 | 6.52 | 274.2 Da LogP 2.05 TPSA 22.0 | ✓ Ro5 | ✓ Clean |
O=c1c2ccccc2[se]n1-c1ccccc1
|
| CHEMBL3926452 | C4LW95 | 6.41 | 361.4 Da LogP 4.48 TPSA 58.7 | ✓ Ro5 | ✓ Clean |
O=C1/C(=C/c2ccccn2)S/C(=N\c2ccccc2)N1Cc1ccco1
|
| CHEMBL5395264 | P0A9P4 | 6.30 | 476.3 Da LogP 3.86 TPSA 35.6 | ✓ Ro5 | ✓ Clean |
Cc1nn(CC[Se][Se]CCn2nc(C)c3ccccc32)c2ccccc12
|
| CHEMBL3655712 | P0A9P4 | 6.26 | 308.6 Da LogP 2.70 TPSA 22.0 | ✓ Ro5 | ✓ Clean |
O=c1c2ccccc2[se]n1-c1ccc(Cl)cc1
|
| CHEMBL3913125 | C4LW95 | 6.17 | 420.5 Da LogP 5.10 TPSA 64.3 | 1 viol. | ✓ Clean |
COc1ccc(/C=C2\S/C(=N\c3ccccc3)N(Cc3ccco3)C2=O)c…
|
| CHEMBL3968421 | C4LW95 | 6.16 | 420.5 Da LogP 5.10 TPSA 64.3 | 1 viol. | ✓ Clean |
COc1ccc(OC)c(/C=C2\S/C(=N\c3ccccc3)N(Cc3ccco3)C…
|
| CHEMBL5397149 | P0A9P4 | 6.16 | 538.3 Da LogP 3.06 TPSA 121.9 | 1 viol. | ✓ Clean |
O=[N+]([O-])c1ccc2c(cnn2CC[Se][Se]CCn2ncc3cc([N…
|
| CHEMBL5416840 | P0A9P4 | 6.16 | 473.2 Da LogP 3.48 TPSA 35.6 | ✓ Ro5 | ✓ Clean |
Cc1nn(CC[Se][Se]CCn2nc(C)c(Cl)c2C)c(C)c1Cl
|
| CHEMBL5440854 | P0A9P4 | 6.16 | 506.3 Da LogP 1.74 TPSA 74.8 | 1 viol. | ✓ Clean |
O=C1c2ccccc2C(=O)N1CC[Se][Se]CCN1C(=O)c2ccccc2C…
|
| CHEMBL3976958 | C4LW95 | 6.14 | 376.4 Da LogP 4.79 TPSA 66.0 | ✓ Ro5 | ✓ Clean |
O=C1/C(=C/c2ccc(O)cc2)S/C(=N\c2ccccc2)N1Cc1ccco1
|
| CHEMBL3655716 | P0A9P4 | 6.00 | 198.1 Da LogP 0.59 TPSA 32.9 | ✓ Ro5 | ✓ Clean |
O=c1[nH][se]c2ccccc12
|
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 |
|---|---|---|---|---|---|
| ZINC18246980 | 1.000 | 376.4 Da LogP 4.79 TPSA 66.0 | ✓ Ro5 | ✓ Clean |
O=C1/C(=C\c2ccc(O)cc2)S/C(=N/c2ccccc2)N1Cc1ccco1
|
| ZINC2293355652 | 1.000 | 376.4 Da LogP 4.79 TPSA 66.0 | ✓ Ro5 | ✓ Clean |
O=C1C(=Cc2ccc(O)cc2)SC(=Nc2ccccc2)N1Cc1ccco1
|
| ZINC15013521 | 0.852 | 406.5 Da LogP 4.80 TPSA 75.3 | ✓ Ro5 | ✓ Clean |
COc1cc(/C=C2/S/C(=N/c3ccccc3)N(Cc3ccco3)C2=O)cc…
|
| ZINC9261465 | 0.818 | 478.5 Da LogP 4.64 TPSA 90.6 | ✓ Ro5 | ✓ Clean |
COC(=O)COc1ccc(/C=C2/S/C(=N\c3ccccc3)N(Cc3ccco3…
|
| ZINC4660313 | 0.780 | 368.5 Da LogP 4.33 TPSA 51.1 | ✓ Ro5 | ✓ Clean |
CCN1C(=O)/C(=C\c2cc(OC)ccc2OC)S/C1=N\c1ccccc1
|
| ZINC100314562 | 0.769 | 434.5 Da LogP 4.82 TPSA 73.5 | ✓ Ro5 | ✓ Clean |
COc1cc2c(cc1/C=C1/S/C(=N\c3ccccc3)N(Cc3ccco3)C1…
|
| ZINC17719664 | 0.769 | 434.5 Da LogP 4.82 TPSA 73.5 | ✓ Ro5 | ✓ Clean |
COc1cc2c(cc1/C=C1/S/C(=N/c3ccccc3)N(Cc3ccco3)C1…
|
| ZINC245309458 | 0.769 | 434.5 Da LogP 4.82 TPSA 73.5 | ✓ Ro5 | ✓ Clean |
COc1cc2c(cc1/C=C1/SC(=Nc3ccccc3)N(Cc3ccco3)C1=O…
|
| ZINC13546520 | 0.759 | 405.4 Da LogP 4.99 TPSA 88.9 | ✓ Ro5 | ✓ Clean |
O=C1/C(=C/c2ccc([N+](=O)[O-])cc2)S/C(=N\c2ccccc…
|
| ZINC4664355 | 0.759 | 368.5 Da LogP 4.33 TPSA 51.1 | ✓ Ro5 | ✓ Clean |
CCN1C(=O)/C(=C\c2ccc(OC)c(OC)c2)S/C1=N/c1ccccc1
|
| ZINC13880821 | 0.750 | 418.5 Da LogP 4.87 TPSA 72.1 | ✓ Ro5 | ✓ Clean |
COC(=O)c1ccc(/C=C2\S/C(=N\c3ccccc3)N(Cc3ccco3)C…
|
| ZINC49582222 | 0.750 | 207.2 Da LogP 0.94 TPSA 81.2 | ✓ Ro5 | ✓ Clean |
O=[N+]([O-])c1ccc2c(cnn2CCO)c1
|
| ZINC4526109 | 0.741 | 350.4 Da LogP 4.68 TPSA 59.0 | ✓ Ro5 | ✓ Clean |
O=C1/C(=C/c2ccco2)S/C(=N\c2ccccc2)N1Cc1ccco1
|
| ZINC1014076 | 0.738 | 382.5 Da LogP 4.72 TPSA 51.1 | ✓ Ro5 | ✓ Clean |
CCCN1C(=O)/C(=C/c2cc(OC)ccc2OC)S/C1=N\c1ccccc1
|
| ZINC4664262 | 0.738 | 382.5 Da LogP 4.72 TPSA 51.1 | ✓ Ro5 | ✓ Clean |
CCCN1C(=O)/C(=C\c2cc(OC)ccc2OC)S/C1=N/c1ccccc1
|
| ZINC18246975 | 0.733 | 445.5 Da LogP 4.92 TPSA 58.3 | ✓ Ro5 | Alert |
O=C1/C(=C\c2ccc(N3CCOCC3)cc2)S/C(=N/c2ccccc2)N1…
|
| ZINC8816280 | 0.729 | 477.5 Da LogP 4.35 TPSA 107.4 | ✓ Ro5 | ✓ Clean |
CCOc1cc(/C=C2\S/C(=N\c3ccccc3)N(Cc3ccco3)C2=O)c…
|
| ZINC2777124 | 0.714 | 398.5 Da LogP 3.95 TPSA 60.4 | ✓ Ro5 | ✓ Clean |
COCCN1C(=O)/C(=C/c2cc(OC)ccc2OC)S/C1=N\c1ccccc1
|
| ZINC5660821 | 0.714 | 398.5 Da LogP 3.95 TPSA 60.4 | ✓ Ro5 | ✓ Clean |
COCCN1C(=O)/C(=C\c2cc(OC)ccc2OC)S/C1=N\c1ccccc1
|
| ZINC1184606 | 0.710 | 361.4 Da LogP 3.70 TPSA 51.9 | ✓ Ro5 | Alert |
COc1ccc(OC)c(/C=C2/SC(=S)N(Cc3ccco3)C2=O)c1
|
| ZINC13534752 | 0.710 | 361.4 Da LogP 3.70 TPSA 51.9 | ✓ Ro5 | Alert |
COc1ccc(OC)c(/C=C2\SC(=S)N(Cc3ccco3)C2=O)c1
|
| ZINC175473 | 0.708 | 320.3 Da LogP 1.58 TPSA 74.8 | ✓ Ro5 | ✓ Clean |
O=C1c2ccccc2C(=O)N1CCN1C(=O)c2ccccc2C1=O
|
| ZINC13739257 | 0.705 | 361.4 Da LogP 3.70 TPSA 51.9 | ✓ Ro5 | Alert |
COc1ccc(/C=C2\SC(=S)N(Cc3ccco3)C2=O)cc1OC
|
| ZINC1532902 | 0.700 | 206.2 Da LogP -0.86 TPSA 132.1 | ✓ Ro5 | ✓ Clean |
O=C(O)CC[C@@](O)(CC(=O)O)C(=O)O
|
| ZINC2018106 | 0.700 | 206.2 Da LogP -0.86 TPSA 132.1 | ✓ Ro5 | ✓ Clean |
O=C(O)CC[C@](O)(CC(=O)O)C(=O)O
|
| ZINC1065235 | 0.696 | 302.4 Da LogP 3.08 TPSA 46.3 | ✓ Ro5 | Alert |
O=C1/C(=C\c2ccccn2)SC(=S)N1Cc1ccco1
|
| ZINC1065238 | 0.696 | 302.4 Da LogP 3.08 TPSA 46.3 | ✓ Ro5 | Alert |
O=C1/C(=C/c2ccccn2)SC(=S)N1Cc1ccco1
|
| ZINC2141838 | 0.694 | 398.5 Da LogP 3.95 TPSA 60.4 | ✓ Ro5 | ✓ Clean |
COCCN1C(=O)/C(=C/c2ccc(OC)c(OC)c2)S/C1=N\c1cccc…
|
| ZINC5879640 | 0.694 | 398.5 Da LogP 3.95 TPSA 60.4 | ✓ Ro5 | ✓ Clean |
COCCN1C(=O)/C(=C\c2ccc(OC)c(OC)c2)S/C1=N\c1cccc…
|
| ZINC1187854 | 0.673 | 317.4 Da LogP 3.39 TPSA 53.7 | ✓ Ro5 | Alert |
O=C1/C(=C/c2ccc(O)cc2)SC(=S)N1Cc1ccco1
|
| ZINC12436467 | 0.673 | 317.4 Da LogP 3.39 TPSA 53.7 | ✓ Ro5 | Alert |
O=C1/C(=C\c2ccc(O)cc2)SC(=S)N1Cc1ccco1
|
| ZINC4660314 | 0.672 | 354.4 Da LogP 3.94 TPSA 51.1 | ✓ Ro5 | ✓ Clean |
COc1ccc(OC)c(/C=C2/S/C(=N\c3ccccc3)N(C)C2=O)c1
|
| ZINC96592063 | 0.672 | 354.4 Da LogP 3.94 TPSA 51.1 | ✓ Ro5 | ✓ Clean |
COc1ccc(OC)c(/C=C2/S/C(=N/c3ccccc3)N(C)C2=O)c1
|
| ZINC4491584 | 0.667 | 383.5 Da LogP 3.78 TPSA 54.4 | ✓ Ro5 | ✓ Clean |
COc1ccc(OC)c(/C=C2/S/C(=N\c3ccccc3)N(N(C)C)C2=O…
|
| ZINC4664352 | 0.667 | 368.5 Da LogP 4.33 TPSA 51.1 | ✓ Ro5 | ✓ Clean |
CCN1C(=O)/C(=C\c2ccc(OC)cc2OC)S/C1=N/c1ccccc1
|
| ZINC71773889 | 0.667 | 206.1 Da LogP -1.77 TPSA 132.1 | ✓ Ro5 | ✓ Clean |
O=C(C[C@H](O)C(=O)O)C[C@H](O)C(=O)O
|
| ZINC71773890 | 0.667 | 206.1 Da LogP -1.77 TPSA 132.1 | ✓ Ro5 | ✓ Clean |
O=C(C[C@H](O)C(=O)O)C[C@@H](O)C(=O)O
|
| ZINC71773891 | 0.667 | 206.1 Da LogP -1.77 TPSA 132.1 | ✓ Ro5 | ✓ Clean |
O=C(C[C@@H](O)C(=O)O)C[C@@H](O)C(=O)O
|
| ZINC101695107 | 0.662 | 412.5 Da LogP 4.34 TPSA 60.4 | ✓ Ro5 | ✓ Clean |
CCOCCN1C(=O)/C(=C/c2ccc(OC)c(OC)c2)S/C1=N/c1ccc…
|
| ZINC4466315 | 0.661 | 336.4 Da LogP 4.18 TPSA 52.9 | ✓ Ro5 | ✓ Clean |
C=CCN1C(=O)/C(=C\c2ccc(O)cc2)S/C1=N/c1ccccc1
|
| ZINC4672070 | 0.656 | 382.5 Da LogP 4.64 TPSA 51.1 | ✓ Ro5 | ✓ Clean |
CCN1C(=O)/C(=C\c2cc(OC)ccc2OC)S/C1=N\c1ccc(C)cc1
|
| ZINC1719027 | 0.654 | 348.4 Da LogP 2.36 TPSA 74.8 | ✓ Ro5 | ✓ Clean |
O=C1c2ccccc2C(=O)N1CCCCN1C(=O)c2ccccc2C1=O
|
| ZINC398642 | 0.654 | 334.3 Da LogP 1.97 TPSA 74.8 | ✓ Ro5 | ✓ Clean |
O=C1c2ccccc2C(=O)N1CCCN1C(=O)c2ccccc2C1=O
|
| ZINC3593496 | 0.652 | 206.2 Da LogP -1.16 TPSA 121.1 | ✓ Ro5 | ✓ Clean |
COC(=O)C[C@@](O)(CC(=O)O)C(=O)O
|
| ZINC3593497 | 0.652 | 206.2 Da LogP -1.16 TPSA 121.1 | ✓ Ro5 | ✓ Clean |
COC(=O)C[C@](O)(CC(=O)O)C(=O)O
|
| ZINC4660312 | 0.651 | 352.5 Da LogP 4.63 TPSA 41.9 | ✓ Ro5 | ✓ Clean |
CCN1C(=O)/C(=C\c2ccc(C)c(OC)c2)S/C1=N\c1ccccc1
|
| ZINC96610654 | 0.651 | 352.5 Da LogP 4.63 TPSA 41.9 | ✓ Ro5 | ✓ Clean |
CCN1C(=O)/C(=C\c2ccc(C)c(OC)c2)S/C1=N/c1ccccc1
|
| ZINC4682460 | 0.650 | 342.4 Da LogP 3.10 TPSA 72.1 | ✓ Ro5 | ✓ Clean |
COC(=O)/C=C1/S/C(=N\c2ccccc2)N(Cc2ccco2)C1=O
|
| ZINC9957365 | 0.647 | 474.5 Da LogP 4.96 TPSA 88.4 | ✓ Ro5 | ✓ Clean |
COc1cc(/C=C2\S/C(=N\c3ccccc3)N(Cc3ccccc3)C2=O)c…
|
| ZINC8698499 | 0.636 | 253.3 Da LogP 2.99 TPSA 61.0 | ✓ Ro5 | ✓ Clean |
O=[N+]([O-])c1ccc2c(cnn2Cc2ccccc2)c1
|
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.