KpKP13 Protein target profile
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase
Accession: KP13_01800
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 (%)
- 93.842 Higher values support similarity to known essential genes.
- DEG E-value
- 0.0 Smaller values mean stronger essential-gene similarity.
Structure confidence
- ColabFold pLDDT
- 97.37 0-100 confidence; >70 supports local structural interpretation.
Binding-site evidence
AlphaFold DB / UniProt modelP2Rank's binding-site probability is the primary druggability signal shown across the app; FPocket's druggability score is shown alongside it for comparison. Both estimate small-molecule pocket quality after applying the curated structure priority — neither is experimental binding evidence. The 3D viewer may show a different loaded structure, so visible pockets can differ.
Sequence
Primary amino-acid sequence viewer.
MPSIRLADLAQQLDAELHGDGDIVITGVASMQSAKTGQITFMVNPKYREHLAACQASAVVMTQDDLPFAHSAALVVRNPYLTYARMAQILDTTPQPAQDIAPSAVIDPSAKLGSNVAIGANAVIESGVVLGDNVVIGAGCFVGKNTKIGAGSRLWANVTVYHEIEIGENCLIQSSTVIGADGFGYANDRGNWVKIPQLGRVIIGDRVEIGACTTIDRGALDDTVIGNGVIIDNQCQIAHNVVIGDNTAVAGGVIMAGSLKIGRYCMIGGASVINGHMEICDKVTVTGMGMVMRPISEPGVYSSGIPLQPNKAWRKTAALVMNIDEMSKRLKAIERKVNQQD
Functional annotations
Enzyme classification and Gene Ontology terms linked to this protein.
Subcellular localization
- Localization
- Cytoplasmic
Enzyme Commission (EC)
1Gene Ontology (GO)
6- GO:0009245 The chemical reactions and pathways resulting in the formation of lipid A, the glycolipid group of bacterial lipopolysaccharides, consisting of four to six fatty acyl chains linked to two glucosamine residues. Further modifications of the backbone are common.
- GO:0016410 Catalysis of the transfer of an acyl group to a nitrogen atom on the acceptor molecule.
- 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:0016747 Catalysis of the transfer of an acyl group, other than amino-acyl, from one compound (donor) to another (acceptor).
- GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
- GO:0103118 Catalysis of the reaction: a UDP-3-O-[(3R)-3-hydroxyacyl]-alpha-D-glucosamine + a (3R)-hydroxyacyl-[ACP] = a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-glucosamine + holo-[ACP] + H+.
Sequence domains and features
Domain and signature matches imported from InterPro and related databases.
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 1 | 99 | Gene3D | G3DSA:3.40.1390.10 | - |
| 33 | 316 | SUPERFAMILY | SSF51161 | Trimeric LpxA-like enzymes |
| 33 | 316 | InterPro | IPR011004 | Trimeric LpxA-like superfamily |
| 323 | 341 | Coils | Coil | Coil |
| 100 | 309 | Gene3D | G3DSA:2.160.10.10 | Hexapeptide repeat proteins |
| 9 | 326 | Hamap | MF_00523 | UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase [lpxD]. |
| 9 | 326 | InterPro | IPR007691 | UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase LpxD |
| 310 | 341 | Gene3D | G3DSA:1.20.5.170 | - |
| 145 | 179 | Pfam | PF00132 | Bacterial transferase hexapeptide (six repeats) |
| 145 | 179 | InterPro | IPR001451 | Hexapeptide repeat |
| 109 | 144 | Pfam | PF00132 | Bacterial transferase hexapeptide (six repeats) |
| 109 | 144 | InterPro | IPR001451 | Hexapeptide repeat |
| 222 | 255 | Pfam | PF00132 | Bacterial transferase hexapeptide (six repeats) |
| 222 | 255 | InterPro | IPR001451 | Hexapeptide repeat |
| 130 | 158 | ProSitePatterns | PS00101 | Hexapeptide-repeat containing-transferases signature. |
| 130 | 158 | InterPro | IPR018357 | Hexapeptide transferase, conserved site |
| 8 | 329 | NCBIfam | TIGR01853 | UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase |
| 8 | 329 | InterPro | IPR007691 | UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase LpxD |
| 4 | 338 | PANTHER | PTHR43378 | UDP-3-O-ACYLGLUCOSAMINE N-ACYLTRANSFERASE |
| 4 | 338 | InterPro | IPR007691 | UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase LpxD |
| 100 | 309 | FunFam | G3DSA:2.160.10.10:FF:000005 | UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase |
| 109 | 314 | CDD | cd03352 | LbH_LpxD |
| 109 | 314 | InterPro | IPR007691 | UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase LpxD |
| 310 | 341 | FunFam | G3DSA:1.20.5.170:FF:000032 | UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase |
| 22 | 88 | Pfam | PF04613 | UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase, LpxD |
| 22 | 88 | InterPro | IPR020573 | UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase, non-repeat region |
| 225 | 253 | ProSitePatterns | PS00101 | Hexapeptide-repeat containing-transferases signature. |
| 225 | 253 | InterPro | IPR018357 | Hexapeptide transferase, conserved site |
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
Druggability (P2Rank): high ≥ 0.5 · medium 0.2–0.49 · low < 0.2
Binding pockets · FPocket
Druggability (FPocket): high ≥ 0.7 · medium 0.4–0.69 · low < 0.4
Residue sets
Binding pockets · P2Rank
Druggability (P2Rank): high ≥ 0.5 · medium 0.2–0.49 · low < 0.2
Binding pockets · FPocket
Druggability (FPocket): high ≥ 0.7 · medium 0.4–0.69 · low < 0.4
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_A0A0H3GS43
|
AlphaFold DB | — | — | full sequence | — | Viewing |
|
ColabFold
KP13_01800
|
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 |
|---|---|---|---|---|---|---|
| 1F7 RCSB PDB | P21645 | 584.7 Da LogP 3.04 TPSA 182.5 | 2 viol. | ✓ Clean |
CCCCCCCCCCC[C@H](CC(=O)SCCNC(=O)CCNC(=O)[C@H](C…
|
|
| FTT RCSB PDB | P21645 | 244.4 Da LogP 3.74 TPSA 57.5 | ✓ Ro5 | ✓ Clean |
CCCCCCCCCCC[C@H](CC(=O)O)O
|
|
| O3V RCSB PDB | P21645 | 389.5 Da LogP 5.01 TPSA 68.0 | 1 viol. | ✓ Clean |
CC1(Cc2c(c(c3c(n2)nn(c3O)c4ccccc4)c5cccs5)C(=O)…
|
|
| O3Y RCSB PDB | P21645 | 417.9 Da LogP 5.60 TPSA 68.0 | 1 viol. | ✓ Clean |
CC1(Cc2c(c(c3c(n2)nn(c3O)c4ccccc4)c5ccccc5Cl)C(…
|
|
| O4D RCSB PDB | P21645 | 396.5 Da LogP 1.68 TPSA 77.2 | ✓ Ro5 | ✓ Clean |
Cc1cc(nc2c1c(nn2CC(=O)NCCCN3CCOCC3)n4cccc4)C
|
|
| O4G RCSB PDB | P21645 | 364.4 Da LogP 3.56 TPSA 89.8 | ✓ Ro5 | ✓ Clean |
c1cc(cc(c1)NC(=O)c2ccco2)NC(=O)c3ccc4c(c3)OCCO4
|
|
| O4P RCSB PDB | P21645 | 406.5 Da LogP 4.86 TPSA 54.6 | ✓ Ro5 | ✓ Clean |
CN([C@@H](c1cccs1)c2c[nH]c3c2cccc3)C(=O)COc4ccc…
|
|
| O4S RCSB PDB | P21645 | 474.6 Da LogP 3.51 TPSA 73.0 | ✓ Ro5 | ✓ Clean |
CCc1ccc(cc1)CNC(=O)CN2c3cc(ccc3N4CCCC[C@@H]4C2=…
|
|
| O4V RCSB PDB | P21645 | 358.4 Da LogP 2.39 TPSA 100.1 | ✓ Ro5 | ✓ Clean |
CCOc1ccccc1n2c(c(nn2)S(=O)(=O)c3ccc(cc3)C)N
|
|
| PE5 RCSB PDB | Q5LH16 | 398.5 Da LogP 0.13 TPSA 94.1 | ✓ Ro5 | ✓ Clean |
CCOCCOCCOCCOCCOCCOCCOCCOCCO
|
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| PG0 RCSB PDB | Q5LH16 | 120.1 Da LogP -0.36 TPSA 38.7 | ✓ Ro5 | ✓ Clean |
COCCOCCO
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|
| PNS RCSB PDB | P21645 | 358.4 Da LogP -0.96 TPSA 145.2 | 1 viol. | ✓ Clean |
CC(C)(COP(=O)(O)O)[C@H](C(=O)NCCC(=O)NCCS)O
|
|
| PO3 RCSB PDB | B4F258 | 79.0 Da LogP -1.64 TPSA 63.2 | ✓ Ro5 | ✓ Clean |
[O-][P-](=O)[O-]
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|
| Q5M RCSB PDB | Q9HXY6 | 228.2 Da LogP 2.89 TPSA 54.4 | ✓ Ro5 | ✓ Clean |
c1ccc2c(c1)cccc2C(=O)CCC(=O)O
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|
| S2N RCSB PDB | Q8EZA6 | 570.7 Da LogP 2.91 TPSA 171.5 | 1 viol. | ✓ Clean |
CCCCCCCCC[C@H](CC(=O)SCCNC(=O)CCNC(=O)[C@@H](C(…
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| U22 RCSB PDB | Q8EZA6 | 804.7 Da LogP -1.63 TPSA 335.0 | 3 viol. | ✓ Clean |
CCCCCCCCC[C@H](CC(=O)N[C@@H]1[C@H]([C@H](O[C@@H…
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| UD1 RCSB PDB | Q5LH16 | 607.4 Da LogP -4.65 TPSA 305.9 | 3 viol. | ✓ Clean |
CC(=O)N[C@@H]1[C@H]([C@@H]([C@H](O[C@@H]1O[P@@]…
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| VFZ RCSB PDB | A0A069Q726 | 405.9 Da LogP 2.31 TPSA 118.1 | ✓ Ro5 | ✓ Clean |
c1ccc(c(c1)SCC(=O)N(Cc2nnc(o2)N)CC3=CNC(=O)C=C3…
|
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 |
|---|---|---|---|---|---|
| ZINC100305273 ZINC | 1.000 | 286.5 Da LogP 4.91 TPSA 57.5 | ✓ Ro5 | ✓ Clean |
CCCCCCCCCCCCCC[C@H](O)CC(=O)O
|
| ZINC100305277 ZINC | 1.000 | 286.5 Da LogP 4.91 TPSA 57.5 | ✓ Ro5 | ✓ Clean |
CCCCCCCCCCCCCC[C@@H](O)CC(=O)O
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| ZINC100500540 ZINC | 1.000 | 230.3 Da LogP 3.35 TPSA 57.5 | ✓ Ro5 | ✓ Clean |
CCCCCCCCCC[C@@H](O)CC(=O)O
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| ZINC100500548 ZINC | 1.000 | 258.4 Da LogP 4.13 TPSA 57.5 | ✓ Ro5 | ✓ Clean |
CCCCCCCCCCCC[C@H](O)CC(=O)O
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| ZINC100500553 ZINC | 1.000 | 258.4 Da LogP 4.13 TPSA 57.5 | ✓ Ro5 | ✓ Clean |
CCCCCCCCCCCC[C@@H](O)CC(=O)O
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| ZINC1580161 ZINC | 1.000 | 208.3 Da LogP -0.33 TPSA 57.2 | ✓ Ro5 | ✓ Clean |
COCCOCCOCCOCCO
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| ZINC15835555 ZINC | 1.000 | 406.5 Da LogP 4.86 TPSA 54.6 | ✓ Ro5 | ✓ Clean |
COc1ccccc1OCC(=O)N(C)[C@@H](c1cccs1)c1c[nH]c2cc…
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| ZINC15835557 ZINC | 1.000 | 406.5 Da LogP 4.86 TPSA 54.6 | ✓ Ro5 | ✓ Clean |
COc1ccccc1OCC(=O)N(C)[C@H](c1cccs1)c1c[nH]c2ccc…
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| ZINC16051927 ZINC | 1.000 | 216.3 Da LogP 2.96 TPSA 57.5 | ✓ Ro5 | ✓ Clean |
CCCCCCCCC[C@@H](O)CC(=O)O
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| ZINC16052118 ZINC | 1.000 | 340.4 Da LogP -0.28 TPSA 84.8 | ✓ Ro5 | ✓ Clean |
COCCOCCOCCOCCOCCOCCOCCO
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| ZINC16052257 ZINC | 1.000 | 384.5 Da LogP -0.26 TPSA 94.1 | ✓ Ro5 | ✓ Clean |
COCCOCCOCCOCCOCCOCCOCCOCCO
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| ZINC2039068 ZINC | 1.000 | 244.4 Da LogP 3.74 TPSA 57.5 | ✓ Ro5 | ✓ Clean |
CCCCCCCCCCC[C@H](O)CC(=O)O
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| ZINC2039069 ZINC | 1.000 | 244.4 Da LogP 3.74 TPSA 57.5 | ✓ Ro5 | ✓ Clean |
CCCCCCCCCCC[C@@H](O)CC(=O)O
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| ZINC236510 ZINC | 1.000 | 228.2 Da LogP 2.89 TPSA 54.4 | ✓ Ro5 | ✓ Clean |
O=C(O)CCC(=O)c1cccc2ccccc12
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| ZINC2504625 ZINC | 1.000 | 216.3 Da LogP 2.96 TPSA 57.5 | ✓ Ro5 | ✓ Clean |
CCCCCCCCC[C@H](O)CC(=O)O
|
| ZINC2558055 ZINC | 1.000 | 202.3 Da LogP 2.57 TPSA 57.5 | ✓ Ro5 | ✓ Clean |
CCCCCCCC[C@H](O)CC(=O)O
|
| ZINC2558056 ZINC | 1.000 | 230.3 Da LogP 3.35 TPSA 57.5 | ✓ Ro5 | ✓ Clean |
CCCCCCCCCC[C@H](O)CC(=O)O
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| ZINC32838984 ZINC | 1.000 | 272.4 Da LogP 4.52 TPSA 57.5 | ✓ Ro5 | ✓ Clean |
CCCCCCCCCCCCC[C@@H](O)CC(=O)O
|
| ZINC32838986 ZINC | 1.000 | 272.4 Da LogP 4.52 TPSA 57.5 | ✓ Ro5 | ✓ Clean |
CCCCCCCCCCCCC[C@H](O)CC(=O)O
|
| ZINC34317654 ZINC | 1.000 | 472.6 Da LogP -0.23 TPSA 112.5 | 1 viol. | ✓ Clean |
COCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO
|
| ZINC44076059 ZINC | 1.000 | 428.5 Da LogP -0.24 TPSA 103.3 | ✓ Ro5 | ✓ Clean |
COCCOCCOCCOCCOCCOCCOCCOCCOCCO
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| ZINC5210101 ZINC | 1.000 | 252.3 Da LogP -0.31 TPSA 66.4 | ✓ Ro5 | ✓ Clean |
COCCOCCOCCOCCOCCO
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| ZINC5650743 ZINC | 1.000 | 222.3 Da LogP 0.07 TPSA 57.2 | ✓ Ro5 | ✓ Clean |
CCOCCOCCOCCOCCO
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| ZINC5997860 ZINC | 1.000 | 296.4 Da LogP -0.29 TPSA 75.6 | ✓ Ro5 | ✓ Clean |
COCCOCCOCCOCCOCCOCCO
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| ZINC6403917 ZINC | 1.000 | 354.4 Da LogP 0.11 TPSA 84.8 | ✓ Ro5 | ✓ Clean |
CCOCCOCCOCCOCCOCCOCCOCCO
|
| ZINC6817538 ZINC | 1.000 | 358.4 Da LogP 2.39 TPSA 100.1 | ✓ Ro5 | ✓ Clean |
CCOc1ccccc1-n1nnc(S(=O)(=O)c2ccc(C)cc2)c1N
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| ZINC754049 ZINC | 1.000 | 364.4 Da LogP 3.56 TPSA 89.8 | ✓ Ro5 | ✓ Clean |
O=C(Nc1cccc(NC(=O)c2ccco2)c1)c1ccc2c(c1)OCCO2
|
| ZINC85915165 ZINC | 1.000 | 202.3 Da LogP 2.57 TPSA 57.5 | ✓ Ro5 | ✓ Clean |
CCCCCCCC[C@@H](O)CC(=O)O
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| ZINC2858547 ZINC | 0.864 | 350.3 Da LogP 3.51 TPSA 89.8 | ✓ Ro5 | ✓ Clean |
O=C(Nc1cccc(NC(=O)c2ccco2)c1)c1ccc2c(c1)OCO2
|
| ZINC861606 ZINC | 0.860 | 364.4 Da LogP 3.56 TPSA 89.8 | ✓ Ro5 | ✓ Clean |
O=C(Nc1ccc(NC(=O)c2ccco2)cc1)c1ccc2c(c1)OCCO2
|
| ZINC8907957 ZINC | 0.844 | 364.4 Da LogP 3.56 TPSA 89.8 | ✓ Ro5 | ✓ Clean |
O=C(Nc1ccc2c(c1)OCCO2)c1cccc(NC(=O)c2ccco2)c1
|
| ZINC2378696 ZINC | 0.828 | 242.3 Da LogP 3.28 TPSA 54.4 | ✓ Ro5 | ✓ Clean |
O=C(O)CCCC(=O)c1cccc2ccccc12
|
| ZINC2378697 ZINC | 0.800 | 256.3 Da LogP 3.67 TPSA 54.4 | ✓ Ro5 | ✓ Clean |
O=C(O)CCCCC(=O)c1cccc2ccccc12
|
| ZINC8060160 ZINC | 0.800 | 364.4 Da LogP 3.56 TPSA 89.8 | ✓ Ro5 | ✓ Clean |
O=C(Nc1ccc2c(c1)OCCO2)c1ccc(NC(=O)c2ccco2)cc1
|
| ZINC15835570 ZINC | 0.789 | 406.5 Da LogP 4.86 TPSA 54.6 | ✓ Ro5 | ✓ Clean |
COc1ccc(OCC(=O)N(C)[C@@H](c2cccs2)c2c[nH]c3cccc…
|
| ZINC15835572 ZINC | 0.789 | 406.5 Da LogP 4.86 TPSA 54.6 | ✓ Ro5 | ✓ Clean |
COc1ccc(OCC(=O)N(C)[C@H](c2cccs2)c2c[nH]c3ccccc…
|
| ZINC15835539 ZINC | 0.786 | 376.5 Da LogP 4.86 TPSA 45.3 | ✓ Ro5 | ✓ Clean |
CN(C(=O)COc1ccccc1)[C@@H](c1cccs1)c1c[nH]c2cccc…
|
| ZINC15835541 ZINC | 0.786 | 376.5 Da LogP 4.86 TPSA 45.3 | ✓ Ro5 | ✓ Clean |
CN(C(=O)COc1ccccc1)[C@H](c1cccs1)c1c[nH]c2ccccc…
|
| ZINC15835551 ZINC | 0.783 | 421.5 Da LogP 4.76 TPSA 88.5 | ✓ Ro5 | ✓ Clean |
CN(C(=O)COc1ccccc1[N+](=O)[O-])[C@@H](c1cccs1)c…
|
| ZINC15835553 ZINC | 0.783 | 421.5 Da LogP 4.76 TPSA 88.5 | ✓ Ro5 | ✓ Clean |
CN(C(=O)COc1ccccc1[N+](=O)[O-])[C@H](c1cccs1)c1…
|
| ZINC31159540 ZINC | 0.778 | 204.3 Da LogP 1.15 TPSA 77.8 | ✓ Ro5 | ✓ Clean |
CCCCC[C@@H](O)C[C@@H](O)CC(=O)O
|
| ZINC31159544 ZINC | 0.778 | 204.3 Da LogP 1.15 TPSA 77.8 | ✓ Ro5 | ✓ Clean |
CCCCC[C@H](O)C[C@@H](O)CC(=O)O
|
| ZINC31159548 ZINC | 0.778 | 204.3 Da LogP 1.15 TPSA 77.8 | ✓ Ro5 | ✓ Clean |
CCCCC[C@@H](O)C[C@H](O)CC(=O)O
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| ZINC31159552 ZINC | 0.778 | 204.3 Da LogP 1.15 TPSA 77.8 | ✓ Ro5 | ✓ Clean |
CCCCC[C@H](O)C[C@H](O)CC(=O)O
|
| ZINC15835543 ZINC | 0.776 | 394.5 Da LogP 5.00 TPSA 45.3 | ✓ Ro5 | ✓ Clean |
CN(C(=O)COc1ccc(F)cc1)[C@@H](c1cccs1)c1c[nH]c2c…
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| ZINC15835545 ZINC | 0.776 | 394.5 Da LogP 5.00 TPSA 45.3 | ✓ Ro5 | ✓ Clean |
CN(C(=O)COc1ccc(F)cc1)[C@H](c1cccs1)c1c[nH]c2cc…
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| ZINC2243634 ZINC | 0.774 | 284.4 Da LogP 4.45 TPSA 54.4 | ✓ Ro5 | ✓ Clean |
O=C(O)CCCCCCC(=O)c1cccc2ccccc12
|
| ZINC2378699 ZINC | 0.774 | 270.3 Da LogP 4.06 TPSA 54.4 | ✓ Ro5 | ✓ Clean |
O=C(O)CCCCCC(=O)c1cccc2ccccc12
|
| ZINC8610730 ZINC | 0.769 | 460.6 Da LogP 3.25 TPSA 73.0 | ✓ Ro5 | ✓ Clean |
Cc1cccc(CNC(=O)CN2C(=O)[C@@H]3CCCCN3c3ccc(C(=O)…
|
| ZINC147022 ZINC | 0.767 | 245.2 Da LogP 2.30 TPSA 60.7 | ✓ Ro5 | ✓ Clean |
O=C(Nc1ccc2c(c1)OCCO2)c1ccco1
|
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.
Cross-references
External database identifiers for this protein, its structures, ligands, and metabolic reactions.