Amino acids
1320
Annotations
13
Features
42
PDB binders
17
Druggability
0.956
Overview
Basic information about this protein and its source genome.
- Accession
- KP13_03922
- Gene
- AHE45332.1 putA
- Status
- annotated
- Amino acids
- 1320
- Structure source
- ColabFold
GO
GO:0006355 Any process that modulates the frequency, rate or extent of cellular DNA-templated transcription.
GO:0006561 OBSOLETE. The chemical reactions and pathways resulting in the formation of proline (pyrrolidine-2-carboxylic acid), a chiral, cyclic, nonessential alpha-amino acid found in peptide linkage in proteins.
GO:0010133 OBSOLETE. The chemical reactions and pathways resulting in the breakdown of L-proline into L-glutamate.
GO:0003700 A transcription regulator activity that modulates transcription of gene sets via selective and non-covalent binding to a specific double-stranded genomic DNA sequence (sometimes referred to as a motif) within a cis-regulatory region. Regulatory regions include promoters (proximal and distal) and enhancers. Genes are transcriptional units, and include bacterial operons.
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:0016620 Catalysis of an oxidation-reduction (redox) reaction in which an aldehyde or ketone (oxo) group acts as a hydrogen or electron donor and reduces NAD or NADP.
Target profile
Computed evidence for target prioritization.
- Human off-target
- hit
- Human identity (%)
- 34.653
- Human E-value
- 2.44e-25
- Gut microbiome off-target
- hit
- Essential (DEG)
- N
- DEG identity (%)
- 0.0
- Localization
- Cytoplasmic
- ColabFold pLDDT
- 90.72
Selected Druggability evidence
ColabFold / curated 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
0.956
P2Rank
0.967
ColabFold model
Core conservation
Accessory gene
Gut microbiome
147 / 4744
genomes with a hit
Sequence
Primary amino-acid sequence viewer.
Functional Annotations
Enzyme classification and Gene Ontology terms linked to this protein.
13 GO
Gene Ontology (GO)
13- GO:0006355 Any process that modulates the frequency, rate or extent of cellular DNA-templated transcription.
- GO:0006561 OBSOLETE. The chemical reactions and pathways resulting in the formation of proline (pyrrolidine-2-carboxylic acid), a chiral, cyclic, nonessential alpha-amino acid found in peptide linkage in proteins.
- GO:0010133 OBSOLETE. The chemical reactions and pathways resulting in the breakdown of L-proline into L-glutamate.
- GO:0003700 A transcription regulator activity that modulates transcription of gene sets via selective and non-covalent binding to a specific double-stranded genomic DNA sequence (sometimes referred to as a motif) within a cis-regulatory region. Regulatory regions include promoters (proximal and distal) and enhancers. Genes are transcriptional units, and include bacterial operons.
- 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:0016620 Catalysis of an oxidation-reduction (redox) reaction in which an aldehyde or ketone (oxo) group acts as a hydrogen or electron donor and reduces NAD or NADP.
- GO:0003842 L-glutamate 5-semialdehyde + NAD+ + H2O = L-glutamate + NADH + 2 H+.
- GO:0004657 Catalysis of the reaction: L-proline + a quinone = (S)-1-pyrroline-5-carboxylate + a quinol + H+.
- GO:0009898 The leaflet of the plasma membrane that faces the cytoplasm, including any protein embedded in, attached to, or peripherally associated with it.
- GO:0043168 Binding to an anion, a charged atom or group of atoms with a net negative charge.
- GO:0001217 A DNA-binding transcription factor activity that represses or decreases the transcription of specific gene sets.
- GO:1901363 Binding to heterocyclic compound.
- GO:0000976 Binding to a specific sequence of DNA that is part of a regulatory region that controls transcription of that section of the DNA. The transcribed region might be described as a gene, cistron, or operon.
Sequence Features
Domain/signature hits from InterPro and related databases.
42 records
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 885 | 1082 | Gene3D | G3DSA:3.40.309.10 | Aldehyde Dehydrogenase; Chain A, domain 2 |
| 885 | 1082 | InterPro | IPR016163 | Aldehyde dehydrogenase, C-terminal |
| 88 | 261 | SUPERFAMILY | SSF81935 | N-terminal domain of bifunctional PutA protein |
| 88 | 261 | InterPro | IPR024089 | Proline dehydrogenase PutA, domain I/II |
| 87 | 138 | Gene3D | G3DSA:1.20.5.550 | Single Helix bin |
| 87 | 138 | InterPro | IPR024090 | Proline dehydrogenase PutA, domain I |
| 262 | 618 | SUPERFAMILY | SSF51730 | FAD-linked oxidoreductase |
| 262 | 618 | InterPro | IPR029041 | FAD-linked oxidoreductase-like |
| 11 | 52 | Gene3D | G3DSA:1.10.1220.10 | - |
| 11 | 52 | InterPro | IPR013321 | Arc-type ribbon-helix-helix |
| 162 | 187 | Gene3D | G3DSA:1.20.5.460 | Single helix bin |
| 269 | 569 | Pfam | PF01619 | Proline dehydrogenase |
| 269 | 569 | InterPro | IPR002872 | Proline dehydrogenase domain |
| 652 | 891 | FunFam | G3DSA:3.40.605.10:FF:000017 | Bifunctional protein PutA |
| 4 | 46 | CDD | cd22233 | RHH_CopAso-like |
| 659 | 1106 | Pfam | PF00171 | Aldehyde dehydrogenase family |
| 659 | 1106 | InterPro | IPR015590 | Aldehyde dehydrogenase domain |
| 74 | 1320 | PIRSF | PIRSF000197 | Bifunct_PutA |
| 74 | 1320 | InterPro | IPR025703 | Bifunctional protein PutA |
| 237 | 1318 | PANTHER | PTHR42862 | DELTA-1-PYRROLINE-5-CARBOXYLATE DEHYDROGENASE 1, ISOFORM A-RELATED |
| 885 | 1082 | FunFam | G3DSA:3.40.309.10:FF:000005 | 1-pyrroline-5-carboxylate dehydrogenase 1 |
| 87 | 138 | FunFam | G3DSA:1.20.5.550:FF:000001 | Bifunctional protein PutA |
| 610 | 1113 | NCBIfam | TIGR01238 | L-glutamate gamma-semialdehyde dehydrogenase |
| 610 | 1113 | InterPro | IPR005933 | Bifunctional protein PutA, C-terminal domain |
| 148 | 259 | Pfam | PF14850 | DNA-binding domain of Proline dehydrogenase |
| 148 | 259 | InterPro | IPR024082 | Proline dehydrogenase PutA, domain II |
| 3 | 45 | SUPERFAMILY | SSF47598 | Ribbon-helix-helix |
| 3 | 45 | InterPro | IPR010985 | Ribbon-helix-helix |
| 643 | 1119 | CDD | cd07125 | ALDH_PutA-P5CDH |
| 162 | 187 | FunFam | G3DSA:1.20.5.460:FF:000001 | Bifunctional protein PutA |
| 882 | 889 | ProSitePatterns | PS00687 | Aldehyde dehydrogenases glutamic acid active site. |
| 882 | 889 | InterPro | IPR029510 | Aldehyde dehydrogenase, glutamic acid active site |
| 219 | 610 | Gene3D | G3DSA:3.20.20.220 | - |
| 653 | 1113 | Gene3D | G3DSA:3.40.605.10 | Aldehyde Dehydrogenase; Chain A, domain 1 |
| 653 | 1113 | InterPro | IPR016162 | Aldehyde dehydrogenase, N-terminal |
| 89 | 136 | Pfam | PF18327 | Proline utilization A proline dehydrogenase N-terminal domain |
| 89 | 136 | InterPro | IPR041349 | Proline utilization A proline dehydrogenase N-terminal domain |
| 656 | 1112 | SUPERFAMILY | SSF53720 | ALDH-like |
| 656 | 1112 | InterPro | IPR016161 | Aldehyde/histidinol dehydrogenase |
| 910 | 921 | ProSitePatterns | PS00070 | Aldehyde dehydrogenases cysteine active site. |
| 910 | 921 | InterPro | IPR016160 | Aldehyde dehydrogenase, cysteine active site |
| 218 | 610 | FunFam | G3DSA:3.20.20.220:FF:000004 | Bifunctional protein PutA |
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 |
|---|---|---|---|---|---|---|
|
ColabFold
KP13_03922
|
ColabFold | — | — | 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 |
|---|---|---|---|---|---|---|---|
| 20 | 0.956 | ||||||
| 44 | 0.68 | ||||||
| 96 | 0.314 | ||||||
| 2 | 0.227 |
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 | 29.92 | 0.933 | ||||||
| 2 | 22.8 | 0.883 | ||||||
| 3 | 22.55 | 0.882 | ||||||
| 4 | 7.62 | 0.402 | ||||||
| 5 | 4.45 | 0.189 |
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.
67 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 |
|---|---|---|---|---|---|---|
| 2L3 | Q746X3 | 254.3 Da LogP 1.10 TPSA 88.5 | ✓ Ro5 | Alert |
C[C@]1(CC(=O)c2ccccc2C1=O)S(=O)(=O)O
|
|
| 2OP | P09546 | 90.1 Da LogP -0.55 TPSA 57.5 | ✓ Ro5 | ✓ Clean |
C[C@@H](C(=O)O)O
|
|
| C15 | Q746X3 | 336.6 Da LogP 4.26 TPSA 54.4 | ✓ Ro5 | ✓ Clean |
CCCCCCCCCCCC[N+](C)(C)CCCS(=O)(=O)O
|
|
| DPR | Q5SI02 | 115.1 Da LogP -0.18 TPSA 49.3 | ✓ Ro5 | ✓ Clean |
C1C[C@@H](NC1)C(=O)O
|
|
| FDA | P09546 | 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…
|
|
| HYP | P09546 | 131.1 Da LogP -1.21 TPSA 69.6 | ✓ Ro5 | ✓ Clean |
C1[C@H](CN[C@@H]1C(=O)O)O
|
|
| P5F | Q6MNK1 | — | — | — |
CC1=CC2=[N](C3=C(C(=O)NC(=O)N3)[N](=C2C=C1C)C=C…
|
|
| SO2 | P09546 | 64.1 Da LogP -0.67 TPSA 34.1 | ✓ Ro5 | ✓ Clean |
O=S=O
|
|
| TFB | P09546 | 116.1 Da LogP 0.25 TPSA 46.5 | ✓ Ro5 | ✓ Clean |
C1C[C@H](OC1)C(=O)O
|
|
| UJD | F7X6I3 | 150.2 Da LogP 0.88 TPSA 37.3 | ✓ Ro5 | ✓ Clean |
C1CSC(S1)C(=O)O
|
|
| UJM | F7X6I3 | 132.2 Da LogP 0.97 TPSA 37.3 | ✓ Ro5 | ✓ Clean |
C1C[C@H](SC1)C(=O)O
|
|
| UJP | F7X6I3 | 132.2 Da LogP 0.97 TPSA 37.3 | ✓ Ro5 | ✓ Clean |
C1C[C@@H](SC1)C(=O)O
|
|
| UY7 | F7X6I3 | 131.1 Da LogP -1.21 TPSA 69.6 | ✓ Ro5 | ✓ Clean |
C1[C@@H](CN[C@H]1C(=O)O)O
|
|
| UYA | F7X6I3 | 131.1 Da LogP -1.21 TPSA 69.6 | ✓ Ro5 | ✓ Clean |
C1[C@H](CN[C@H]1C(=O)O)O
|
|
| ZPJ | P09546 | 86.1 Da LogP 0.48 TPSA 37.3 | ✓ Ro5 | ✓ Clean |
C1CC1C(=O)O
|
|
| ZPM | P09546 | 100.1 Da LogP 0.87 TPSA 37.3 | ✓ Ro5 | ✓ Clean |
C1CC(C1)C(=O)O
|
|
| ZPS | P09546 | 144.1 Da LogP 0.33 TPSA 74.6 | ✓ Ro5 | ✓ Clean |
C1CC(C1)(C(=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).
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 |
|---|---|---|---|---|---|
| ZINC14880434 | 1.000 | 336.6 Da LogP 4.26 TPSA 54.4 | ✓ Ro5 | ✓ Clean |
CCCCCCCCCCCC[N+](C)(C)CCCS(=O)(=O)O
|
| ZINC1999508 | 1.000 | 254.3 Da LogP 1.10 TPSA 88.5 | ✓ Ro5 | Alert |
C[C@@]1(S(=O)(=O)O)CC(=O)c2ccccc2C1=O
|
| ZINC1999509 | 1.000 | 254.3 Da LogP 1.10 TPSA 88.5 | ✓ Ro5 | Alert |
C[C@]1(S(=O)(=O)O)CC(=O)c2ccccc2C1=O
|
| ZINC2384686 | 1.000 | 280.5 Da LogP 2.70 TPSA 54.4 | ✓ Ro5 | ✓ Clean |
CCCCCCCC[N+](C)(C)CCCS(=O)(=O)O
|
| ZINC5029952 | 1.000 | 200.2 Da LogP 1.74 TPSA 74.6 | ✓ Ro5 | ✓ Clean |
O=C(O)C1CCCC(C(=O)O)CCC1
|
| ZINC58541260 | 1.000 | 308.5 Da LogP 3.48 TPSA 54.4 | ✓ Ro5 | ✓ Clean |
CCCCCCCCCC[N+](C)(C)CCCS(=O)(=O)O
|
| ZINC4521338 | 0.813 | 212.3 Da LogP 3.99 TPSA 37.3 | ✓ Ro5 | ✓ Clean |
O=C(O)C1CCCCCCCCCCC1
|
| ZINC2325704365 | 0.800 | 254.3 Da LogP 2.77 TPSA 74.6 | ✓ Ro5 | ✓ Clean |
O=C(O)[C@H]1CC[C@H]([C@H]2CC[C@H](C(=O)O)CC2)CC1
|
| 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
|
| ZINC2379127 | 0.655 | 212.3 Da LogP -0.67 TPSA 74.6 | ✓ Ro5 | ✓ Clean |
C[N+](C)(CCO)CCCS(=O)(=O)O
|
| ZINC100019805 | 0.654 | 292.5 Da LogP 4.97 TPSA 54.4 | ✓ Ro5 | ✓ Clean |
CCCCCCCCCCCCCCCS(=O)(=O)O
|
| ZINC1625794 | 0.654 | 264.4 Da LogP 4.19 TPSA 54.4 | ✓ Ro5 | ✓ Clean |
CCCCCCCCCCCCCS(=O)(=O)O
|
| ZINC1651926 | 0.654 | 250.4 Da LogP 3.80 TPSA 54.4 | ✓ Ro5 | ✓ Clean |
CCCCCCCCCCCCS(=O)(=O)O
|
| ZINC1843748 | 0.654 | 222.3 Da LogP 3.01 TPSA 54.4 | ✓ Ro5 | ✓ Clean |
CCCCCCCCCCS(=O)(=O)O
|
| ZINC2515939 | 0.654 | 236.4 Da LogP 3.41 TPSA 54.4 | ✓ Ro5 | ✓ Clean |
CCCCCCCCCCCS(=O)(=O)O
|
| ZINC42921009 | 0.654 | 278.5 Da LogP 4.58 TPSA 54.4 | ✓ Ro5 | ✓ Clean |
CCCCCCCCCCCCCCS(=O)(=O)O
|
| ZINC80135680 | 0.654 | 208.3 Da LogP 2.62 TPSA 54.4 | ✓ Ro5 | ✓ Clean |
CCCCCCCCCS(=O)(=O)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
|
| ZINC101661450 | 0.649 | 407.6 Da LogP 3.77 TPSA 83.5 | ✓ Ro5 | ✓ Clean |
CCCCCCCCCCCC(=O)NCCC[N+](C)(C)CCCS(=O)(=O)O
|
| ZINC97943292 | 0.649 | 435.7 Da LogP 4.55 TPSA 83.5 | ✓ Ro5 | ✓ Clean |
CCCCCCCCCCCCCC(=O)NCCC[N+](C)(C)CCCS(=O)(=O)O
|
| ZINC14686440 | 0.625 | 436.4 Da LogP -2.64 TPSA 247.9 | 1 viol. | ✓ Clean |
O=C(O)C[C@](O)(CC(=O)NCCCCNC(=O)C[C@@](O)(CC(=O…
|
| ZINC14686442 | 0.625 | 436.4 Da LogP -2.64 TPSA 247.9 | 1 viol. | ✓ Clean |
O=C(O)C[C@@](O)(CC(=O)NCCCCNC(=O)C[C@](O)(CC(=O…
|
| ZINC14686444 | 0.625 | 436.4 Da LogP -2.64 TPSA 247.9 | 1 viol. | ✓ Clean |
O=C(O)C[C@@](O)(CC(=O)NCCCCNC(=O)C[C@@](O)(CC(=…
|
| ZINC117798402 | 0.611 | 216.2 Da LogP 0.27 TPSA 111.9 | ✓ Ro5 | ✓ Clean |
O=C(O)[C@H]1CC[C@@H](C(=O)O)[C@@H](C(=O)O)C1
|
| ZINC44069472 | 0.611 | 216.2 Da LogP 0.27 TPSA 111.9 | ✓ Ro5 | ✓ Clean |
O=C(O)[C@H]1CC[C@@H](C(=O)O)C[C@H]1C(=O)O
|
| ZINC60121565 | 0.611 | 240.3 Da LogP 2.52 TPSA 74.6 | ✓ Ro5 | ✓ Clean |
O=C(O)C1CCC2(CC1)CCC(C(=O)O)CC2
|
| ZINC153514 | 0.609 | 211.3 Da LogP 1.11 TPSA 57.6 | ✓ Ro5 | ✓ Clean |
O=C(O)C1CCN(C(=O)C2CCC2)CC1
|
| ZINC757066037 | 0.609 | 200.2 Da LogP 1.44 TPSA 63.6 | ✓ Ro5 | ✓ Clean |
COC(=O)[C@@H]1CCC[C@@H](C(=O)O)CC1
|
| ZINC757066044 | 0.609 | 200.2 Da LogP 1.44 TPSA 63.6 | ✓ Ro5 | ✓ Clean |
COC(=O)[C@@H]1CCC[C@H](C(=O)O)CC1
|
| ZINC757066048 | 0.609 | 200.2 Da LogP 1.44 TPSA 63.6 | ✓ Ro5 | ✓ Clean |
COC(=O)[C@H]1CCC[C@@H](C(=O)O)CC1
|
| ZINC757066049 | 0.609 | 200.2 Da LogP 1.44 TPSA 63.6 | ✓ Ro5 | ✓ Clean |
COC(=O)[C@H]1CCC[C@H](C(=O)O)CC1
|
| ZINC103598261 | 0.600 | 297.4 Da LogP 2.36 TPSA 86.6 | ✓ Ro5 | ✓ Clean |
O=C(O)[C@H]1CC[C@@H](CNC[C@H]2CC[C@@H](C(=O)O)C…
|
| ZINC14806503 | 0.600 | 216.2 Da LogP 0.27 TPSA 111.9 | ✓ Ro5 | ✓ Clean |
O=C(O)C1CC(C(=O)O)CC(C(=O)O)C1
|
| ZINC245204662 | 0.600 | 216.2 Da LogP 0.27 TPSA 111.9 | ✓ Ro5 | ✓ Clean |
O=C(O)[C@H]1C[C@@H](C(=O)O)C[C@@H](C(=O)O)C1
|
| ZINC100050172 | 0.588 | 352.6 Da LogP 3.23 TPSA 74.6 | ✓ Ro5 | ✓ Clean |
CCCCCCCCCCCC[N+](C)(C)C[C@H](O)CS(=O)(=O)O
|
| ZINC100050174 | 0.588 | 352.6 Da LogP 3.23 TPSA 74.6 | ✓ Ro5 | ✓ Clean |
CCCCCCCCCCCC[N+](C)(C)C[C@@H](O)CS(=O)(=O)O
|
| ZINC13398039 | 0.577 | 234.2 Da LogP -0.38 TPSA 121.1 | ✓ Ro5 | ✓ Clean |
CC(C)OC(=O)C[C@](O)(CC(=O)O)C(=O)O
|
| ZINC2528012 | 0.577 | 234.2 Da LogP -0.38 TPSA 121.1 | ✓ Ro5 | ✓ Clean |
CC(C)OC(=O)C[C@@](O)(CC(=O)O)C(=O)O
|
| ZINC108246896 | 0.571 | 206.3 Da LogP 0.67 TPSA 71.4 | ✓ Ro5 | ✓ Clean |
CS(=O)(=O)C1CCC(C(=O)O)CC1
|
| ZINC261596316 | 0.571 | 225.3 Da LogP 1.50 TPSA 57.6 | ✓ Ro5 | ✓ Clean |
O=C(O)[C@H]1CC[C@H](C(=O)N2CCCC2)CC1
|
| ZINC307226840 | 0.571 | 207.3 Da LogP -0.08 TPSA 97.5 | ✓ Ro5 | ✓ Clean |
NS(=O)(=O)C1CCC(C(=O)O)CC1
|
| ZINC31729329 | 0.571 | 240.3 Da LogP 2.67 TPSA 74.6 | ✓ Ro5 | ✓ Clean |
O=C(O)C1(C(=O)O)CCC2(CCCCC2)CC1
|
| ZINC37472008 | 0.571 | 211.3 Da LogP 1.16 TPSA 66.4 | ✓ Ro5 | ✓ Clean |
O=C(O)C1CCC(NC(=O)C2CC2)CC1
|
| ZINC6741121 | 0.571 | 211.3 Da LogP 1.96 TPSA 29.5 | ✓ Ro5 | ✓ Clean |
O=C([C@@H]1CCCO1)N1CCCCCCC1
|
| ZINC6741122 | 0.571 | 211.3 Da LogP 1.96 TPSA 29.5 | ✓ Ro5 | ✓ Clean |
O=C([C@H]1CCCO1)N1CCCCCCC1
|
| ZINC108323602 | 0.563 | 255.3 Da LogP 1.32 TPSA 75.6 | ✓ Ro5 | ✓ Clean |
O=C(O)[C@H]1CCCCC[C@H]1NC(=O)[C@H]1CCCO1
|
| ZINC157702634 | 0.563 | 255.3 Da LogP 1.32 TPSA 75.6 | ✓ Ro5 | ✓ Clean |
O=C(N[C@@H]1CCCCC[C@H]1C(=O)O)[C@H]1CCCO1
|
| ZINC94744170 | 0.563 | 255.3 Da LogP 1.32 TPSA 75.6 | ✓ Ro5 | ✓ Clean |
O=C(N[C@@H]1CCCCC[C@@H]1C(=O)O)[C@@H]1CCCO1
|
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.