Protein target profile

VK055_1436

putA bifunctional enzyme and transcriptional regulator PutA transcriptional repressor, Proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase

Genome: KpATCC43816 Gene: AIK80057.1 3D evidence: ColabFold model Metabolism 1 reaction UniProt A0A9Q9Q9F8

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Length 1320

Pocket druggability 0.964

Metabolic reactions 1

Chokepoint No

Direct ligand evidence 0 67 total records

Functional annotation 0 EC 13 GO

Target summary

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

Independent pocket support: FPocket + P2Rank Both predictors report a high-scoring binding site (FPocket 0.96, P2Rank 0.98). Use the 3D pocket comparison to verify whether they identify the same site. No isoenzyme backup detected Imported GPR rules do not show an alternative enzyme for the catalyzed reaction set. Strong predicted binding pocket FPocket selected-pocket score 0.96. This is a computational pocket signal, not binding validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.98. Review the complete evidence below

Risks to review

Evidence coverage

Core evidence streams are available for this target.

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 (%): 34.653 Lower values reduce human off-target concern.
Human E-value: 2.37e-25
Gut microbiome similarity: 3.1% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): N
DEG identity (%): 37.336 Higher values support similarity to known essential genes.

Localization

Localization: Cytoplasmic

Structure confidence

ColabFold pLDDT: 90.52 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

ColabFold / curated model

The 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.

FPocket 0.964

Structure CB_VK055_1436

Pocket Pocket 21

P2Rank 0.98

Structure CB_VK055_1436

Pocket Pocket 1

ColabFold model

FPocket 0.964 · Pocket 21

P2Rank 0.98 · Pocket 1

Core conservation Accessory gene

Roary core

CoreCruncher accessory

Gut microbiome 147 / 4744 genomes with a hit

Prevalence 3.1%

Cross-references

External database identifiers for this protein, its structures, ligands, and metabolic reactions.

Sequence

UniProt A0A9Q9Q9F8

Pathways

KEGG R00245 BioCyc RXN-14116

Metabolic context

Reactions catalyzed, pathway membership, and centrality in the genome-scale metabolic network.

Explore metabolic network

Relative network centrality 0.0% more central than 0.0% of genes in this genome

Chokepoint Not a chokepoint

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MGTTTMGVKLDDATRERIKSAASRIDRTPHWLIKQAIFNYLEKLENDETLPELPALLSGAANESDDASVPTEEPYQPFLEFAEQILPQSVSRAAITAAWRRPETDAVPMLLEQARLPQPLGEQAHKLAYQLAEKLRNQKTASGRAGMVQSLLQEFSLSSQEGVALMCLAEALLRIPDKATRDALIRDKISNGNWQSHIGRSPSLFVNAATWGLLFTGKLVSTHNETSLSRSLNRIIGKSGEPLIRKGVDMAMRLMGEQFVTGETIAEALANARKLEEKGFRYSYDMLGEAALTAADAQAYMVSYQQAIHAIGKASNGRGIYEGPGISIKLSALHPRYSRAQYDRVMEELYPRLKSLTLLARQYDIGINIDAEEADRLEISLDLLEKLCFEPELAGWNGIGFVIQAYQKRCPFVIDYLIDLATRSRRRLMIRLVKGAYWDSEIKRAQMEGLEGYPVYTRKVYTDVSYLACAKKLLAVPNLIYPQFATHNAHTLAAIYQLAGQNYYPGQYEFQCLHGMGEPLYEQVVGKVADGKLNRPCRIYAPVGTHETLLAYLVRRLLENGANTSFVNRIADNTLPLDELVADPVSAVEKLAQQEGQAGLPHPKIPLPRDLYGSGRSNSAGLDLANEHRLASLSSSLLNSALHKWQALPMLEQPVAEGEMQPVVNPAEPKDIVGYVREASDAEVQQALTSAINNAPIWFATPPQERAAILERAAVLMESQMPTLMGILVREAGKTFSNAIAEVREAVDFLHYYAGQVRDDFDNETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQGVAILLEAGVPPGVIQLLPGRGETVGAALTSDERVRGVMFTGSTEVATLLQRNIASRLDPQGRPTPLIAETGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRVLCLQEEVADHTLTMLRGAMSECRMGNPGRLTTDIGPVIDAEAKENIERHIQAMRAKGRTVYQAVRENSEDAREWRHGTFVPPTLIELDSFDELKKEVFGPVLHVVRYNRNELDKLVEQINASGYGLTLGVHTRIDETIAQVTGSAKVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRLLSSRPQDAVGVTFARQDAERPLDAQLKTLLEKPLQALQQWAAGRPELQALCQQYSEQAQSGTQRLLPGPTGERNTLTLMPRERVLCVADNEQDALIQLAAVLAVGCEVLWPDSALQRDLAKKLPREVSERIRFAKAEQLPGQAFDAVIYHGDSDQLRELCEQVAARDGAIVSVQGFARGETNLLLERLYIERSLSVNTAAAGGNASLMTIG

MGTTTMGVKLDDATRERIKSAASRIDRTPHWLIKQAIFNYLEKLENDETLPELPALLSGAANESDDASVPTEEPYQPFLEFAEQILPQSVSRAAITAAWRRPETDAVPMLLEQARLPQPLGEQAHKLAYQLAEKLRNQKTASGRAGMVQSLLQEFSLSSQEGVALMCLAEALLRIPDKATRDALIRDKISNGNWQSHIGRSPSLFVNAATWGLLFTGKLVSTHNETSLSRSLNRIIGKSGEPLIRKGVDMAMRLMGEQFVTGETIAEALANARKLEEKGFRYSYDMLGEAALTAADAQAYMVSYQQAIHAIGKASNGRGIYEGPGISIKLSALHPRYSRAQYDRVMEELYPRLKSLTLLARQYDIGINIDAEEADRLEISLDLLEKLCFEPELAGWNGIGFVIQAYQKRCPFVIDYLIDLATRSRRRLMIRLVKGAYWDSEIKRAQMEGLEGYPVYTRKVYTDVSYLACAKKLLAVPNLIYPQFATHNAHTLAAIYQLAGQNYYPGQYEFQCLHGMGEPLYEQVVGKVADGKLNRPCRIYAPVGTHETLLAYLVRRLLENGANTSFVNRIADNTLPLDELVADPVSAVEKLAQQEGQAGLPHPKIPLPRDLYGSGRSNSAGLDLANEHRLASLSSSLLNSALHKWQALPMLEQPVAEGEMQPVVNPAEPKDIVGYVREASDAEVQQALTSAINNAPIWFATPPQERAAILERAAVLMESQMPTLMGILVREAGKTFSNAIAEVREAVDFLHYYAGQVRDDFDNETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQGVAILLEAGVPPGVIQLLPGRGETVGAALTSDERVRGVMFTGSTEVATLLQRNIASRLDPQGRPTPLIAETGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRVLCLQEEVADHTLTMLRGAMSECRMGNPGRLTTDIGPVIDAEAKENIERHIQAMRAKGRTVYQAVRENSEDAREWRHGTFVPPTLIELDSFDELKKEVFGPVLHVVRYNRNELDKLVEQINASGYGLTLGVHTRIDETIAQVTGSAKVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRLLSSRPQDAVGVTFARQDAERPLDAQLKTLLEKPLQALQQWAAGRPELQALCQQYSEQAQSGTQRLLPGPTGERNTLTLMPRERVLCVADNEQDALIQLAAVLAVGCEVLWPDSALQRDLAKKLPREVSERIRFAKAEQLPGQAFDAVIYHGDSDQLRELCEQVAARDGAIVSVQGFARGETNLLLERLYIERSLSVNTAAAGGNASLMTIG

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

13 GO

Gene Ontology (GO)

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: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:0010133 OBSOLETE. The chemical reactions and pathways resulting in the breakdown of L-proline into L-glutamate.
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:0006355 Any process that modulates the frequency, rate or extent of cellular DNA-templated transcription.
GO:0003842 L-glutamate 5-semialdehyde + NAD+ + H2O = L-glutamate + NADH + 2 H+.
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: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 domains and features

Domain and signature matches imported from InterPro and related databases.

42 records

Show feature table

Start	End	DB	Term	Name
148	259	Pfam	PF14850	DNA-binding domain of Proline dehydrogenase
148	259	InterPro	IPR024082	Proline dehydrogenase PutA, domain II
218	610	FunFam	G3DSA:3.20.20.220:FF:000004	Bifunctional protein PutA
652	891	FunFam	G3DSA:3.40.605.10:FF:000017	Bifunctional protein PutA
3	45	SUPERFAMILY	SSF47598	Ribbon-helix-helix
3	45	InterPro	IPR010985	Ribbon-helix-helix
910	921	ProSitePatterns	PS00070	Aldehyde dehydrogenases cysteine active site.
910	921	InterPro	IPR016160	Aldehyde dehydrogenase, cysteine active site
162	187	FunFam	G3DSA:1.20.5.460:FF:000001	Bifunctional protein PutA
656	1112	SUPERFAMILY	SSF53720	ALDH-like
656	1112	InterPro	IPR016161	Aldehyde/histidinol dehydrogenase
87	138	Gene3D	G3DSA:1.20.5.550	Single Helix bin
87	138	InterPro	IPR024090	Proline dehydrogenase PutA, domain I
659	1106	Pfam	PF00171	Aldehyde dehydrogenase family
659	1106	InterPro	IPR015590	Aldehyde dehydrogenase domain
885	1082	FunFam	G3DSA:3.40.309.10:FF:000005	1-pyrroline-5-carboxylate dehydrogenase 1
237	1318	PANTHER	PTHR42862	DELTA-1-PYRROLINE-5-CARBOXYLATE DEHYDROGENASE 1, ISOFORM A-RELATED
88	261	SUPERFAMILY	SSF81935	N-terminal domain of bifunctional PutA protein
88	261	InterPro	IPR024089	Proline dehydrogenase PutA, domain I/II
885	1082	Gene3D	G3DSA:3.40.309.10	Aldehyde Dehydrogenase; Chain A, domain 2
885	1082	InterPro	IPR016163	Aldehyde dehydrogenase, C-terminal
219	610	Gene3D	G3DSA:3.20.20.220	-
262	618	SUPERFAMILY	SSF51730	FAD-linked oxidoreductase
262	618	InterPro	IPR029041	FAD-linked oxidoreductase-like
653	1113	Gene3D	G3DSA:3.40.605.10	Aldehyde Dehydrogenase; Chain A, domain 1
653	1113	InterPro	IPR016162	Aldehyde dehydrogenase, N-terminal
269	569	Pfam	PF01619	Proline dehydrogenase
269	569	InterPro	IPR002872	Proline dehydrogenase domain
610	1113	NCBIfam	TIGR01238	L-glutamate gamma-semialdehyde dehydrogenase
610	1113	InterPro	IPR005933	Bifunctional protein PutA, C-terminal domain
643	1119	CDD	cd07125	ALDH_PutA-P5CDH
74	1320	PIRSF	PIRSF000197	Bifunct_PutA
74	1320	InterPro	IPR025703	Bifunctional protein PutA
162	187	Gene3D	G3DSA:1.20.5.460	Single helix bin
11	52	Gene3D	G3DSA:1.10.1220.10	-
11	52	InterPro	IPR013321	Arc-type ribbon-helix-helix
4	46	CDD	cd22233	RHH_CopAso-like
89	136	Pfam	PF18327	Proline utilization A proline dehydrogenase N-terminal domain
89	136	InterPro	IPR041349	Proline utilization A proline dehydrogenase N-terminal domain
882	889	ProSitePatterns	PS00687	Aldehyde dehydrogenases glutamic acid active site.
882	889	InterPro	IPR029510	Aldehyde dehydrogenase, glutamic acid active site
87	138	FunFam	G3DSA:1.20.5.550:FF:000001	Bifunctional protein PutA

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.

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Pocket score High Medium Low

How colors and pocket overlays are used

Uniform protein color marks the displayed model as a single molecular object.

Experimental PDB structures may be colored by chain to distinguish subunits or copies present in the file.

Pocket colors and alpha spheres are evidence overlays for predicted binding cavities; they are not alternative protein chains.

'Alpha spheres' is FPocket's own cavity-shape geometry, imported when available and aligned with the loaded structure.

'Pocket atoms'/'Predicted site atoms' show the pocket's residue atoms instead: P2Rank reports residues rather than alpha spheres, and FPocket falls back to this when alpha-sphere geometry is unavailable or doesn't align.

'No pocket geometry' means neither alpha spheres nor residue-position data could be found for that pocket; the layer just highlights the same residues as 'Nearby residues'.

Pocket details Inspect a specific pocket, or open the full viewer

Binding pockets · FPocket

Druggability: high ≥ 0.7 · medium 0.4–0.69 · low < 0.4

Site 1 FPocket #21

0.964

Likely same site as P2Rank 1 3.4 Å 23 shared residues 96% of smaller site

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Surrounding area

Site 2 FPocket #2

0.409

Unusual size

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Surrounding area

Site 3 FPocket #56

0.302

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Surrounding area

Binding pockets · P2Rank

Probability: high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Site 1 P2Rank #1

0.98

Likely same site as FPocket 21 3.4 Å 23 shared residues 96% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.966

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Surrounding area

Site 3 P2Rank #3

0.512

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Surrounding area

Site 4 P2Rank #4

0.476

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Surrounding area

Site 5 P2Rank #5

0.255

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Surrounding area

All structural evidence 0 experimental · 1 predicted

Structural evidence

0 + 1

Experimental 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
ColabFold VK055_1436	ColabFold	—	—	full sequence	—	Viewing

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

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 17 records from similar proteins

Structural ligands 17 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

2L3 PDB via homolog 254.3 Da · LogP 1.10 · TPSA 88.5 Open detail RCSB PDB

2OP PDB via homolog Detail RCSB PDB

C15 PDB via homolog Detail RCSB PDB

DPR PDB via homolog Detail RCSB PDB

FDA PDB via homolog Detail RCSB PDB

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
2L3 RCSB PDB	4NMF	Q746X3	254.3 Da LogP 1.10 TPSA 88.5	✓ Ro5	Alert	`C[C@]1(CC(=O)c2ccccc2C1=O)S(=O)(=O)O`
2OP RCSB PDB	1TJ0	P09546	90.1 Da LogP -0.55 TPSA 57.5	✓ Ro5	✓ Clean	`C[C@@H](C(=O)O)O`
C15 RCSB PDB	4NMC	Q746X3	336.6 Da LogP 4.26 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCCCCC[N+](C)(C)CCCS(=O)(=O)O`
DPR RCSB PDB	2EJ6	Q5SI02	115.1 Da LogP -0.18 TPSA 49.3	✓ Ro5	✓ Clean	`C1C[C@@H](NC1)C(=O)O`
FDA RCSB PDB	3ITG	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 RCSB PDB	3E2Q	P09546	131.1 Da LogP -1.21 TPSA 69.6	✓ Ro5	✓ Clean	`C1[C@H](CN[C@@H]1C(=O)O)O`
P5F RCSB PDB	5UR2	Q6MNK1	—	—	—	`CC1=CC2=[N](C3=C(C(=O)NC(=O)N3)[N](=C2C=C1C)C=C…`
SO2 RCSB PDB	2FZM	P09546	64.1 Da LogP -0.67 TPSA 34.1	✓ Ro5	✓ Clean	`O=S=O`
TFB RCSB PDB	1TIW	P09546	116.1 Da LogP 0.25 TPSA 46.5	✓ Ro5	✓ Clean	`C1C[C@H](OC1)C(=O)O`
UJD RCSB PDB	7MY9	F7X6I3	150.2 Da LogP 0.88 TPSA 37.3	✓ Ro5	✓ Clean	`C1CSC(S1)C(=O)O`
UJM RCSB PDB	7MYB	F7X6I3	132.2 Da LogP 0.97 TPSA 37.3	✓ Ro5	✓ Clean	`C1C[C@H](SC1)C(=O)O`
UJP RCSB PDB	7MYB	F7X6I3	132.2 Da LogP 0.97 TPSA 37.3	✓ Ro5	✓ Clean	`C1C[C@@H](SC1)C(=O)O`
UY7 RCSB PDB	6X9A	F7X6I3	131.1 Da LogP -1.21 TPSA 69.6	✓ Ro5	✓ Clean	`C1[C@@H](CN[C@H]1C(=O)O)O`
UYA RCSB PDB	6X9B	F7X6I3	131.1 Da LogP -1.21 TPSA 69.6	✓ Ro5	✓ Clean	`C1[C@H](CN[C@H]1C(=O)O)O`
ZPJ RCSB PDB	7MWV	P09546	86.1 Da LogP 0.48 TPSA 37.3	✓ Ro5	✓ Clean	`C1CC1C(=O)O`
ZPM RCSB PDB	7MWU	P09546	100.1 Da LogP 0.87 TPSA 37.3	✓ Ro5	✓ Clean	`C1CC(C1)C(=O)O`
ZPS RCSB PDB	7MWT	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 ZINC	1.000	336.6 Da LogP 4.26 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCCCCC[N+](C)(C)CCCS(=O)(=O)O`
ZINC1999508 ZINC	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 ZINC	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 ZINC	1.000	280.5 Da LogP 2.70 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCC[N+](C)(C)CCCS(=O)(=O)O`
ZINC5029952 ZINC	1.000	200.2 Da LogP 1.74 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)C1CCCC(C(=O)O)CCC1`
ZINC58541260 ZINC	1.000	308.5 Da LogP 3.48 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCCC[N+](C)(C)CCCS(=O)(=O)O`
ZINC4521338 ZINC	0.813	212.3 Da LogP 3.99 TPSA 37.3	✓ Ro5	✓ Clean	`O=C(O)C1CCCCCCCCCCC1`
ZINC2325704365 ZINC	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 ZINC	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 ZINC	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 ZINC	0.655	212.3 Da LogP -0.67 TPSA 74.6	✓ Ro5	✓ Clean	`C[N+](C)(CCO)CCCS(=O)(=O)O`
ZINC100019805 ZINC	0.654	292.5 Da LogP 4.97 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCCS(=O)(=O)O`
ZINC1625794 ZINC	0.654	264.4 Da LogP 4.19 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCS(=O)(=O)O`
ZINC1651926 ZINC	0.654	250.4 Da LogP 3.80 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCCCCCS(=O)(=O)O`
ZINC1843748 ZINC	0.654	222.3 Da LogP 3.01 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCCCS(=O)(=O)O`
ZINC2515939 ZINC	0.654	236.4 Da LogP 3.41 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCCCCS(=O)(=O)O`
ZINC42921009 ZINC	0.654	278.5 Da LogP 4.58 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCS(=O)(=O)O`
ZINC80135680 ZINC	0.654	208.3 Da LogP 2.62 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCCS(=O)(=O)O`
ZINC3593496 ZINC	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 ZINC	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 ZINC	0.649	407.6 Da LogP 3.77 TPSA 83.5	✓ Ro5	✓ Clean	`CCCCCCCCCCCC(=O)NCCC[N+](C)(C)CCCS(=O)(=O)O`
ZINC97943292 ZINC	0.649	435.7 Da LogP 4.55 TPSA 83.5	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC(=O)NCCC[N+](C)(C)CCCS(=O)(=O)O`
ZINC14686440 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	0.611	240.3 Da LogP 2.52 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)C1CCC2(CC1)CCC(C(=O)O)CC2`
ZINC153514 ZINC	0.609	211.3 Da LogP 1.11 TPSA 57.6	✓ Ro5	✓ Clean	`O=C(O)C1CCN(C(=O)C2CCC2)CC1`
ZINC757066037 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	0.571	206.3 Da LogP 0.67 TPSA 71.4	✓ Ro5	✓ Clean	`CS(=O)(=O)C1CCC(C(=O)O)CC1`
ZINC261596316 ZINC	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 ZINC	0.571	207.3 Da LogP -0.08 TPSA 97.5	✓ Ro5	✓ Clean	`NS(=O)(=O)C1CCC(C(=O)O)CC1`
ZINC31729329 ZINC	0.571	240.3 Da LogP 2.67 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)C1(C(=O)O)CCC2(CCCCC2)CC1`
ZINC37472008 ZINC	0.571	211.3 Da LogP 1.16 TPSA 66.4	✓ Ro5	✓ Clean	`O=C(O)C1CCC(NC(=O)C2CC2)CC1`
ZINC6741121 ZINC	0.571	211.3 Da LogP 1.96 TPSA 29.5	✓ Ro5	✓ Clean	`O=C([C@@H]1CCCO1)N1CCCCCCC1`
ZINC6741122 ZINC	0.571	211.3 Da LogP 1.96 TPSA 29.5	✓ Ro5	✓ Clean	`O=C([C@H]1CCCO1)N1CCCCCCC1`
ZINC108323602 ZINC	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 ZINC	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 ZINC	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.