Protein profile
KP13_01121
UDP-N-acetylglucosamine 1-carboxyvinyltransferase
Genome: KpKP13
Amino acids
419
Annotations
10
Features
17
PDB binders
18
Druggability
0.245
Overview
Basic information about this protein and its source genome.
- Accession
- KP13_01121
- Gene
- AHE42485.1 murA
- Status
- annotated
- Amino acids
- 419
- Structure source
- AlphaFold + ColabFold
EC
GO
GO:0008760 Catalysis of the reaction: phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine.
GO:0019277 The chemical reactions and pathways resulting in the formation of UDP-N-acetylgalactosamine, a substance composed of N-acetylgalactosamine, a common structural unit of oligosaccharides, in glycosidic linkage with uridine diphosphate.
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:0016765 Catalysis of the transfer of an alkyl or aryl (but not methyl) group from one compound (donor) to another (acceptor).
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0051301 The process resulting in division and partitioning of components of a cell to form more cells; may or may not be accompanied by the physical separation of a cell into distinct, individually membrane-bounded daughter cells.
Target profile
Computed evidence for target prioritization.
- Human off-target
- No hit
- Human identity (%)
- 0.0
- Gut microbiome off-target
- hit
- Essential (DEG)
- Y
- DEG identity (%)
- 92.124
- DEG E-value
- 0.0
- Localization
- Cytoplasmic
- ColabFold pLDDT
- 96.35
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
0.245
P2Rank
0.952
ColabFold model
Core conservation
Conserved core gene
Gut microbiome
609 / 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:0008760 Catalysis of the reaction: phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine.
- GO:0019277 The chemical reactions and pathways resulting in the formation of UDP-N-acetylgalactosamine, a substance composed of N-acetylgalactosamine, a common structural unit of oligosaccharides, in glycosidic linkage with uridine diphosphate.
- 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:0016765 Catalysis of the transfer of an alkyl or aryl (but not methyl) group from one compound (donor) to another (acceptor).
- GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
- GO:0051301 The process resulting in division and partitioning of components of a cell to form more cells; may or may not be accompanied by the physical separation of a cell into distinct, individually membrane-bounded daughter cells.
- GO:0071555 A process that results in the assembly, arrangement of constituent parts, or disassembly of the cell wall, the rigid or semi-rigid envelope lying outside the cell membrane of plant, fungal and most prokaryotic cells, maintaining their shape and protecting them from osmotic lysis.
- GO:0009252 The chemical reactions and pathways resulting in the formation of peptidoglycans, any of a class of glycoconjugates found in bacterial cell walls and consisting of long glycan strands of alternating residues of beta-(1,4) linked N-acetylglucosamine and N-acetylmuramic acid, cross-linked by short peptides.
- GO:0008360 Any process that modulates the surface configuration of a cell.
Sequence Features
Domain/signature hits from InterPro and related databases.
17 records
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 2 | 417 | PANTHER | PTHR43783 | UDP-N-ACETYLGLUCOSAMINE 1-CARBOXYVINYLTRANSFERASE |
| 1 | 418 | SUPERFAMILY | SSF55205 | EPT/RTPC-like |
| 1 | 418 | InterPro | IPR013792 | RNA 3'-terminal phosphate cyclase/enolpyruvate transferase, alpha/beta |
| 5 | 414 | Gene3D | G3DSA:3.65.10.10 | Enolpyruvate transferase domain |
| 5 | 414 | InterPro | IPR036968 | Enolpyruvate transferase domain superfamily |
| 6 | 406 | Pfam | PF00275 | EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase) |
| 6 | 406 | InterPro | IPR001986 | Enolpyruvate transferase domain |
| 1 | 416 | Hamap | MF_00111 | UDP-N-acetylglucosamine 1-carboxyvinyltransferase [murA]. |
| 1 | 416 | InterPro | IPR005750 | UDP-N-acetylglucosamine 1-carboxyvinyltransferase |
| 399 | 419 | Coils | Coil | Coil |
| 214 | 414 | FunFam | G3DSA:3.65.10.10:FF:000002 | UDP-N-acetylglucosamine 1-carboxyvinyltransferase |
| 12 | 409 | CDD | cd01555 | UdpNAET |
| 12 | 409 | InterPro | IPR005750 | UDP-N-acetylglucosamine 1-carboxyvinyltransferase |
| 1 | 415 | NCBIfam | TIGR01072 | UDP-N-acetylglucosamine 1-carboxyvinyltransferase |
| 1 | 415 | InterPro | IPR005750 | UDP-N-acetylglucosamine 1-carboxyvinyltransferase |
| 21 | 228 | Gene3D | G3DSA:3.65.10.10 | Enolpyruvate transferase domain |
| 21 | 228 | InterPro | IPR036968 | Enolpyruvate transferase domain superfamily |
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_A0A0H3GYZ6
|
AlphaFold | — | — | full sequence | — | Viewing |
|
ColabFold
KP13_01121
|
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 |
|---|---|---|---|---|---|---|---|
| 22 | 0.245 |
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 | 25.7 | 0.908 | ||||||
| 2 | 1.08 | 0.007 |
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 | 25.54 | 0.907 |
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.
74 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 |
|---|---|---|---|---|---|---|
| 0V5 | Q88P88 | 170.1 Da LogP -0.43 TPSA 104.1 | ✓ Ro5 | ✓ Clean |
C[C@H](C(=O)O)OP(=O)(O)O
|
|
| 2AN | P33038 | 299.4 Da LogP 3.83 TPSA 66.4 | ✓ Ro5 | ✓ Clean |
c1ccc(cc1)Nc2cccc3c2c(ccc3)S(=O)(=O)O
|
|
| EPU | P33038 | 677.4 Da LogP -4.03 TPSA 332.2 | 3 viol. | ✓ Clean |
CC(=O)N[C@@H]1[C@H]([C@@H]([C@H](O[C@@H]1O[P@@]…
|
|
| EPZ | P33038 | 679.4 Da LogP -4.15 TPSA 332.2 | 3 viol. | ✓ Clean |
C[C@H](C(=O)O)O[C@@H]1[C@H]([C@H](O[C@@H]([C@H]…
|
|
| FFQ | P33038 | 140.1 Da LogP -0.11 TPSA 77.8 | ✓ Ro5 | ✓ Clean |
CC[C@H](O)P(=O)(O)O
|
|
| GG6 | P45025 | 156.1 Da LogP -1.14 TPSA 98.0 | ✓ Ro5 | ✓ Clean |
C[C@@H]([C@@H](O)P(=O)(O)O)O
|
|
| HAI | P33038 | 100.2 Da LogP 0.56 TPSA 27.6 | ✓ Ro5 | ✓ Clean |
C1CCC(CC1)[NH3+]
|
|
| MOE | P33038 | 75.1 Da LogP -1.01 TPSA 32.3 | ✓ Ro5 | ✓ Clean |
COCC[O-]
|
|
| PG0 | P33038 | 120.1 Da LogP -0.36 TPSA 38.7 | ✓ Ro5 | ✓ Clean |
COCCOCCO
|
|
| PO3 | P0A749 | 79.0 Da LogP -1.64 TPSA 63.2 | ✓ Ro5 | ✓ Clean |
[O-][P-](=O)[O-]
|
|
| TAV | P33038 | 662.7 Da LogP 4.56 TPSA 184.4 | 1 viol. | ✓ Clean |
CN([C@@H](CC(=O)O)C(=O)O)C(=O)c1cc(ccc1NS(=O)(=…
|
|
| TET | P0A749 | 793.4 Da LogP -4.77 TPSA 398.9 | 3 viol. | ✓ Clean |
CC(=O)N[C@@H]1[C@H]([C@@H]([C@H](O[C@@H]1O[P@@]…
|
|
| TR9 | P33038 | 156.1 Da LogP -0.28 TPSA 74.6 | ✓ Ro5 | ✓ Clean |
CC1=C(C(=O)C[C@@H](C1=O)O)O
|
|
| UD1 | P33038 | 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@@]…
|
|
| UD2 | P33038 | 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@@](…
|
|
| UDA | P33038 | 775.4 Da LogP -4.72 TPSA 398.9 | 3 viol. | ✓ Clean |
CC(=O)N[C@@H]1[C@H]([C@@H]([C@H](O[C@@H]1O[P@@]…
|
|
| UPG | P33038 | 566.3 Da LogP -4.79 TPSA 297.0 | 3 viol. | ✓ Clean |
C1=CN(C(=O)NC1=O)[C@H]2[C@@H]([C@@H]([C@H](O2)C…
|
|
| UPN | P33038 | 677.4 Da LogP -4.03 TPSA 332.2 | 3 viol. | ✓ Clean |
CC(=O)N[C@@H]1[C@H]([C@H]([C@H](O[C@@H]1O[P@](=…
|
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 |
|---|---|---|---|---|---|---|
| FCN | P0A749 | 7.00 | 138.1 Da LogP -0.09 TPSA 70.1 | ✓ Ro5 | ✓ Clean |
C[C@H]1[C@H](O1)P(=O)(O)O
|
| CHEMBL1200331 | P0A749 | — | 259.2 Da LogP -2.43 TPSA 156.8 | 1 viol. | ✓ Clean |
C[C@@H]1O[C@@H]1P(=O)(O)O.NC(CO)(CO)CO
|
| CHEMBL2335230 | P0A749 | — | 296.9 Da LogP 3.01 TPSA 56.3 | ✓ Ro5 | ✓ Clean |
O=[N+]([O-])/C(Br)=C/c1ccc(Br)o1
|
| CHEMBL5219390 | P0A749 | — | 509.0 Da LogP 6.45 TPSA 92.9 | 2 viol. | ✓ Clean |
CC(C)(C)OC(=O)C1=C(O)C(=O)N(c2nc3ccccc3s2)C1c1c…
|
| CHEMBL5417308 | P0A749 | — | 229.8 Da LogP 2.70 TPSA 29.1 | ✓ Ro5 | ✓ Clean |
O=C(CCl)NC1CCCC2CCCCC21
|
| FOM | P0A749 | — | 183.1 Da LogP -0.60 TPSA 98.1 | ✓ Ro5 | ✓ Clean |
C(CN(C=O)O)CP(=O)(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 |
|---|---|---|---|---|---|
| ZINC1532216 | 1.000 | 299.4 Da LogP 3.83 TPSA 66.4 | ✓ Ro5 | ✓ Clean |
O=S(=O)(O)c1cccc2cccc(Nc3ccccc3)c12
|
| ZINC1580161 | 1.000 | 208.3 Da LogP -0.33 TPSA 57.2 | ✓ Ro5 | ✓ Clean |
COCCOCCOCCOCCO
|
| ZINC16052118 | 1.000 | 340.4 Da LogP -0.28 TPSA 84.8 | ✓ Ro5 | ✓ Clean |
COCCOCCOCCOCCOCCOCCOCCO
|
| ZINC16052257 | 1.000 | 384.5 Da LogP -0.26 TPSA 94.1 | ✓ Ro5 | ✓ Clean |
COCCOCCOCCOCCOCCOCCOCCOCCO
|
| ZINC34317654 | 1.000 | 472.6 Da LogP -0.23 TPSA 112.5 | 1 viol. | ✓ Clean |
COCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO
|
| ZINC44076059 | 1.000 | 428.5 Da LogP -0.24 TPSA 103.3 | ✓ Ro5 | ✓ Clean |
COCCOCCOCCOCCOCCOCCOCCOCCOCCO
|
| ZINC5210101 | 1.000 | 252.3 Da LogP -0.31 TPSA 66.4 | ✓ Ro5 | ✓ Clean |
COCCOCCOCCOCCOCCO
|
| ZINC5997860 | 1.000 | 296.4 Da LogP -0.29 TPSA 75.6 | ✓ Ro5 | ✓ Clean |
COCCOCCOCCOCCOCCOCCO
|
| ZINC7571 | 1.000 | 296.9 Da LogP 3.01 TPSA 56.3 | ✓ Ro5 | ✓ Clean |
O=[N+]([O-])/C(Br)=C/c1ccc(Br)o1
|
| ZINC1712810 | 0.757 | 313.4 Da LogP 4.14 TPSA 66.4 | ✓ Ro5 | ✓ Clean |
Cc1ccc(Nc2cccc3cccc(S(=O)(=O)O)c23)cc1
|
| ZINC575419714 | 0.727 | 312.4 Da LogP 0.42 TPSA 66.4 | ✓ Ro5 | ✓ Clean |
COCCOCCOCCSCCOCCOCCO
|
| ZINC115163232 | 0.700 | 222.3 Da LogP 0.07 TPSA 57.2 | ✓ Ro5 | ✓ Clean |
COCCOCCOCCOCCCO
|
| ZINC258837490 | 0.700 | 354.4 Da LogP 0.11 TPSA 84.8 | ✓ Ro5 | ✓ Clean |
COCCOCCOCCOCCOCCOCCOCCCO
|
| ZINC5162495 | 0.697 | 249.3 Da LogP 2.68 TPSA 66.4 | ✓ Ro5 | ✓ Clean |
O=S(=O)(O)c1ccccc1Nc1ccccc1
|
| ZINC12501520 | 0.688 | 458.5 Da LogP -0.88 TPSA 123.5 | 1 viol. | ✓ Clean |
OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO
|
| ZINC1692489 | 0.688 | 222.3 Da LogP 0.33 TPSA 46.2 | ✓ Ro5 | ✓ Clean |
COCCOCCOCCOCCOC
|
| ZINC3874716 | 0.688 | 414.5 Da LogP -0.90 TPSA 114.3 | ✓ Ro5 | ✓ Clean |
OCCOCCOCCOCCOCCOCCOCCOCCOCCO
|
| ZINC4283769 | 0.688 | 238.3 Da LogP -0.96 TPSA 77.4 | ✓ Ro5 | ✓ Clean |
OCCOCCOCCOCCOCCO
|
| ZINC4521548 | 0.688 | 282.3 Da LogP -0.95 TPSA 86.6 | ✓ Ro5 | ✓ Clean |
OCCOCCOCCOCCOCCOCCO
|
| ZINC4530388 | 0.688 | 266.3 Da LogP 0.35 TPSA 55.4 | ✓ Ro5 | ✓ Clean |
COCCOCCOCCOCCOCCOC
|
| ZINC5178829 | 0.688 | 326.4 Da LogP -0.93 TPSA 95.8 | ✓ Ro5 | ✓ Clean |
OCCOCCOCCOCCOCCOCCOCCO
|
| ZINC5178830 | 0.688 | 370.4 Da LogP -0.91 TPSA 105.1 | ✓ Ro5 | ✓ Clean |
OCCOCCOCCOCCOCCOCCOCCOCCO
|
| ZINC5701172 | 0.688 | 310.4 Da LogP 0.36 TPSA 64.6 | ✓ Ro5 | ✓ Clean |
COCCOCCOCCOCCOCCOCCOC
|
| ZINC5997861 | 0.688 | 398.5 Da LogP 0.40 TPSA 83.1 | ✓ Ro5 | ✓ Clean |
COCCOCCOCCOCCOCCOCCOCCOCCOC
|
| ZINC2053549711 | 0.676 | 232.0 Da LogP 2.68 TPSA 56.3 | ✓ Ro5 | ✓ Clean |
CC(=Cc1ccc(Br)o1)[N+](=O)[O-]
|
| ZINC34984414 | 0.676 | 232.0 Da LogP 2.68 TPSA 56.3 | ✓ Ro5 | ✓ Clean |
C/C(=C\c1ccc(Br)o1)[N+](=O)[O-]
|
| ZINC575432150 | 0.667 | 344.4 Da LogP -0.89 TPSA 100.5 | ✓ Ro5 | ✓ Clean |
COCCOCCOCCS(=O)(=O)CCOCCOCCO
|
| ZINC1857524240 | 0.652 | 207.3 Da LogP -0.75 TPSA 60.0 | ✓ Ro5 | ✓ Clean |
COCCNCCOCCOCCO
|
| ZINC71772395 | 0.605 | 265.3 Da LogP 2.04 TPSA 83.5 | ✓ Ro5 | ✓ Clean |
CC(=O)Nc1cccc2cccc(S(=O)(=O)O)c12
|
| ZINC5650743 | 0.600 | 222.3 Da LogP 0.07 TPSA 57.2 | ✓ Ro5 | ✓ Clean |
CCOCCOCCOCCOCCO
|
| ZINC6403917 | 0.600 | 354.4 Da LogP 0.11 TPSA 84.8 | ✓ Ro5 | ✓ Clean |
CCOCCOCCOCCOCCOCCOCCOCCO
|
| ZINC116981890 | 0.594 | 288.3 Da LogP 1.33 TPSA 108.7 | ✓ Ro5 | ✓ Clean |
O=S(=O)(O)c1cccc2cccc(S(=O)(=O)O)c12
|
| ZINC116078641 | 0.583 | 222.2 Da LogP -0.80 TPSA 74.2 | ✓ Ro5 | ✓ Clean |
COC(=O)COCCOCCOCCO
|
| ZINC1857790631 | 0.583 | 280.3 Da LogP -0.39 TPSA 83.5 | ✓ Ro5 | ✓ Clean |
COC(=O)CCOCCOCCOCCOCCO
|
| ZINC196151418 | 0.583 | 266.3 Da LogP -0.78 TPSA 83.5 | ✓ Ro5 | ✓ Clean |
COC(=O)COCCOCCOCCOCCO
|
| ZINC202958272 | 0.583 | 236.3 Da LogP -0.41 TPSA 74.2 | ✓ Ro5 | ✓ Clean |
COC(=O)CCOCCOCCOCCO
|
| ZINC34111591 | 0.583 | 207.3 Da LogP -1.06 TPSA 62.2 | ✓ Ro5 | ✓ Clean |
COCCOCCN(CCO)CCO
|
| ZINC642881862 | 0.583 | 324.4 Da LogP -0.38 TPSA 92.7 | ✓ Ro5 | ✓ Clean |
COC(=O)CCOCCOCCOCCOCCOCCO
|
| ZINC2169453 | 0.575 | 266.3 Da LogP 1.46 TPSA 92.4 | ✓ Ro5 | ✓ Clean |
NCCNc1cccc2cccc(S(=O)(=O)O)c12
|
| ZINC5575424 | 0.565 | 200.0 Da LogP -1.37 TPSA 141.4 | ✓ Ro5 | ✓ Clean |
O=C(O)C(OP(=O)(O)O)C(=O)O
|
| ZINC22590709 | 0.561 | 312.4 Da LogP 3.54 TPSA 72.2 | ✓ Ro5 | ✓ Clean |
Cc1ccc(Nc2cccc3cccc(S(N)(=O)=O)c23)cc1
|
| ZINC1586638 | 0.559 | 223.4 Da LogP 3.26 TPSA 29.1 | ✓ Ro5 | ✓ Clean |
CC(=O)N[C@H]1CCCC[C@H]1C1CCCCC1
|
| ZINC1586639 | 0.559 | 223.4 Da LogP 3.26 TPSA 29.1 | ✓ Ro5 | ✓ Clean |
CC(=O)N[C@@H]1CCCC[C@H]1C1CCCCC1
|
| ZINC1586640 | 0.559 | 223.4 Da LogP 3.26 TPSA 29.1 | ✓ Ro5 | ✓ Clean |
CC(=O)N[C@H]1CCCC[C@@H]1C1CCCCC1
|
| ZINC1586641 | 0.559 | 223.4 Da LogP 3.26 TPSA 29.1 | ✓ Ro5 | ✓ Clean |
CC(=O)N[C@@H]1CCCC[C@@H]1C1CCCCC1
|
| ZINC139635624 | 0.556 | 207.3 Da LogP 2.65 TPSA 29.1 | ✓ Ro5 | ✓ Clean |
C=CC(=O)N[C@@H]1CCC[C@H]2CCCC[C@@H]21
|
| ZINC139635897 | 0.556 | 207.3 Da LogP 2.65 TPSA 29.1 | ✓ Ro5 | ✓ Clean |
C=CC(=O)N[C@@H]1CCC[C@@H]2CCCC[C@@H]21
|
| ZINC141055552 | 0.556 | 207.3 Da LogP 2.65 TPSA 29.1 | ✓ Ro5 | ✓ Clean |
C=CC(=O)N[C@@H]1CCC[C@@H]2CCCC[C@H]21
|
| ZINC141055927 | 0.556 | 207.3 Da LogP 2.65 TPSA 29.1 | ✓ Ro5 | ✓ Clean |
C=CC(=O)N[C@@H]1CCC[C@H]2CCCC[C@H]21
|
| ZINC12959005 | 0.551 | 484.1 Da LogP -2.50 TPSA 264.4 | 2 viol. | ✓ Clean |
O=c1ccn([C@@H]2O[C@H](CO[P@](=O)(O)O[P@](=O)(O)…
|
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.