Protein target profile

KP13_00845

Cysteine desulfurase

Genome: KpKP13 Gene: iscS AHE43209.1 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GWQ1

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Length 404

Pocket druggability 0.469

Direct ligand evidence 0 61 total records

Functional annotation 1 EC 7 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

Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Moderate predicted binding pocket FPocket selected-pocket score 0.47. This supports review but is not experimental validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.89. Structure available AlphaFold DB model + ColabFold model Review the complete evidence below

Risks to review

Evidence gaps

No metabolic context No SBML/network-derived reaction evidence is loaded for this protein.

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 (%): 70.667 Lower values reduce human off-target concern.
Human E-value: 1.3e-29
Gut microbiome similarity: 5.5% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 96.287 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Localization

Localization: Cytoplasmic

Structure confidence

ColabFold pLDDT: 95.66 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

AlphaFold DB / UniProt 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 0.469

Structure A0A0H3GWQ1

Pocket Pocket 13

P2Rank 0.892

Structure A0A0H3GWQ1

Pocket Pocket 1

ColabFold model

FPocket 0.473 · Pocket 23

P2Rank 0.86 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 262 / 4744 genomes with a hit

Prevalence 5.5%

Cross-references

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

Sequence

UniProt A0A0H3GWQ1

Sequence

Primary amino-acid sequence viewer.

MKLPIYLDYSATTPVDPRVAEKMMQFLTMDGTFGNPASRSHRFGWQAEEAVDIARNQIAELVGADPREIVFTSGATESDNLAIKGAANFYQKKGKHIITSKTEHKAVLDTCRQLEREGFEVTYLAPQSNGIIDLKELEAAMRDDTILVSIMHVNNEIGVVQDIATIGEMCRARGIIYHVDATQSVGKLPIDLSQLKVDLMSFSGHKIYGPKGIGALYVRRKPRIRIEAQIHGGGHERGMRSGTLPVHQIVGMGEAYRIAKEEMESEMARLRTLRNRLWNGVKDMEEVYLNGDLEQGAPNILNVSFNYVEGESLIMALKDLAVSSGSACTSASLEPSYVLRALGMTDELAHSSIRFSLGRFTTEEEIDYAIDLIRKSIGRLRELSPLWEMFKQGVDLNSIEWSHH

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 7 GO

Enzyme Commission (EC)

2.8.1.7

Gene Ontology (GO)

GO:0030170 Binding to pyridoxal 5' phosphate, 3-hydroxy-5-(hydroxymethyl)-2-methyl4-pyridine carboxaldehyde 5' phosphate, the biologically active form of vitamin B6.
GO:0031071 Catalysis of the reaction: L-cysteine + [enzyme]-cysteine = L-alanine + [enzyme]-S-sulfanylcysteine.
GO:0044571 The incorporation of two iron atoms and two sulfur atoms into an iron-sulfur cluster.
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:1990221 A protein complex capable of cysteine desulfurase activity decomposing L-cysteine to L-alanine and sulfur. It belongs to a ubiquitous family of pyridoxal 5-phosphate (PLP)-dependent enzymes.
GO:0051537 Binding to a 2 iron, 2 sulfur (2Fe-2S) cluster; this cluster consists of two iron atoms, with two inorganic sulfur atoms found between the irons and acting as bridging ligands.
GO:0046872 Binding to a metal ion.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

20 records

Show feature table

Start	End	DB	Term	Name
257	368	FunFam	G3DSA:3.90.1150.10:FF:000002	Cysteine desulfurase IscS
5	390	SUPERFAMILY	SSF53383	PLP-dependent transferases
5	390	InterPro	IPR015424	Pyridoxal phosphate-dependent transferase
5	368	Pfam	PF00266	Aminotransferase class-V
5	368	InterPro	IPR000192	Aminotransferase class V domain
5	368	Gene3D	G3DSA:3.90.1150.10	Aspartate Aminotransferase, domain 1
5	368	InterPro	IPR015422	Pyridoxal phosphate-dependent transferase, small domain
256	276	Coils	Coil	Coil
2	384	PIRSF	PIRSF005572	NifS
2	384	InterPro	IPR016454	Cysteine desulfurase
197	216	ProSitePatterns	PS00595	Aminotransferases class-V pyridoxal-phosphate attachment site.
197	216	InterPro	IPR020578	Aminotransferase class-V, pyridoxal-phosphate binding site
16	263	FunFam	G3DSA:3.40.640.10:FF:000003	Cysteine desulfurase IscS
1	404	NCBIfam	TIGR02006	IscS subfamily cysteine desulfurase
1	404	InterPro	IPR010240	Cysteine desulfurase IscS
16	263	Gene3D	G3DSA:3.40.640.10	-
16	263	InterPro	IPR015421	Pyridoxal phosphate-dependent transferase, major domain
1	395	Hamap	MF_00331	Cysteine desulfurase IscS [iscS].
1	395	InterPro	IPR010240	Cysteine desulfurase IscS
3	384	PANTHER	PTHR11601	CYSTEINE DESULFURYLASE FAMILY MEMBER

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 #13

0.469

Unusual size

Show in viewer

Surrounding area

Binding pockets · P2Rank

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

Site 1 P2Rank #1

0.892

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Surrounding area

Site 2 P2Rank #2

0.02

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Surrounding area

Site 3 P2Rank #3

0.02

Show in viewer

Surrounding area

Site 4 P2Rank #4

0.001

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Surrounding area

Residue sets

UniProt: Active site:328-328 Cysteine persulfide intermediate

UniProt: Binding site:155-155

UniProt: Binding site:183-183

UniProt: Binding site:203-205

UniProt: Binding site:243-243

UniProt: Binding site:328-328 via persulfide group

UniProt: Binding site:75-76

Binding pockets · P2Rank

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

Site 1 P2Rank #1

0.86

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Surrounding area

Site 2 P2Rank #2

0.03

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Surrounding area

Site 3 P2Rank #3

0.016

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Surrounding area

All structural evidence 0 experimental · 2 predicted

Structural evidence

0 + 2

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
AlphaFold DB AF_A0A0H3GWQ1	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_00845	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.

61 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 11 records from similar proteins

Structural ligands 11 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

7TS PDB via homolog 331.2 Da · LogP 0.60 · TPSA 157.9 Open detail RCSB PDB

8Q1 PDB via homolog Detail RCSB PDB

C6P PDB via homolog Detail RCSB PDB

DTT PDB via homolog Detail RCSB PDB

EDT 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
7TS RCSB PDB	7CET	O25008	331.2 Da LogP 0.60 TPSA 157.9	✓ Ro5	✓ Clean	`Cc1c(c(c(cn1)COP(=O)(O)O)CNC2=CONC2=O)O`
8Q1 RCSB PDB	5USR	Q9Y697	540.7 Da LogP 3.29 TPSA 162.3	1 viol.	✓ Clean	`CCCCCCCCCCCC(=O)SCCNC(=O)CCNC(=O)[C@@H](C(C)(C)…`
C6P RCSB PDB	5ZSS	A0A1I5NEH3	352.3 Da LogP 0.18 TPSA 149.2	1 viol.	✓ Clean	`Cc1c(c(c(cn1)COP(=O)(O)O)CN[C@@H](CS)C(=O)O)O`
DTT RCSB PDB	6UXE	Q9Y697	154.3 Da LogP -0.43 TPSA 40.5	✓ Ro5	✓ Clean	`C([C@@H]([C@H](CS)O)O)S`
EDT RCSB PDB	6UXE	Q9Y697	292.2 Da LogP -2.07 TPSA 155.7	✓ Ro5	✓ Clean	`C(CN(CC(=O)O)CC(=O)O)N(CC(=O)O)CC(=O)O`
ETE RCSB PDB	6WI2	Q9Y697	208.3 Da LogP -0.33 TPSA 57.2	✓ Ro5	✓ Clean	`COCCOCCOCCOCCO`
FES RCSB PDB	4EB5	O29689	175.8 Da LogP 1.29 TPSA 0.0	✓ Ro5	✓ Clean	`S1[Fe]S[Fe]1`
HCS RCSB PDB	5WT5	O25008	135.2 Da LogP -0.28 TPSA 63.3	✓ Ro5	✓ Clean	`C(CS)[C@@H](C(=O)O)N`
P15 RCSB PDB	6UXE	Q9Y697	296.4 Da LogP -0.29 TPSA 75.6	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCO`
PDA RCSB PDB	5WT6	O25008	320.2 Da LogP 0.27 TPSA 149.2	✓ Ro5	✓ Clean	`Cc1c(c(c(cn1)COP(=O)(O)O)CNC(C)C(=O)O)O`
PMP RCSB PDB	4HVK	O29689	248.2 Da LogP 0.16 TPSA 125.9	✓ Ro5	✓ Clean	`Cc1c(c(c(cn1)COP(=O)(O)O)CN)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
ZINC1580161 ZINC	1.000	208.3 Da LogP -0.33 TPSA 57.2	✓ Ro5	✓ Clean	`COCCOCCOCCOCCO`
ZINC16052118 ZINC	1.000	340.4 Da LogP -0.28 TPSA 84.8	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCO`
ZINC16052257 ZINC	1.000	384.5 Da LogP -0.26 TPSA 94.1	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC19364242 ZINC	1.000	292.2 Da LogP -2.07 TPSA 155.7	✓ Ro5	✓ Clean	`O=C(O)CN(CCN(CC(=O)O)CC(=O)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`
ZINC5210101 ZINC	1.000	252.3 Da LogP -0.31 TPSA 66.4	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCO`
ZINC5997860 ZINC	1.000	296.4 Da LogP -0.29 TPSA 75.6	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCO`
ZINC19419017 ZINC	0.933	393.3 Da LogP -2.68 TPSA 196.2	✓ Ro5	✓ Clean	`O=C(O)CN(CCN(CC(=O)O)CC(=O)O)CCN(CC(=O)O)CC(=O)O`
ZINC22593216 ZINC	0.933	494.5 Da LogP -3.30 TPSA 236.8	1 viol.	✓ Clean	`O=C(O)CN(CCN(CCN(CC(=O)O)CC(=O)O)CC(=O)O)CCN(CC…`
ZINC1769289 ZINC	0.765	306.3 Da LogP -1.68 TPSA 155.7	✓ Ro5	✓ Clean	`O=C(O)CN(CCCN(CC(=O)O)CC(=O)O)CC(=O)O`
ZINC4683946 ZINC	0.765	320.3 Da LogP -1.29 TPSA 155.7	✓ Ro5	✓ Clean	`O=C(O)CN(CCCCN(CC(=O)O)CC(=O)O)CC(=O)O`
ZINC19364891 ZINC	0.737	204.2 Da LogP -0.98 TPSA 81.1	✓ Ro5	✓ Clean	`CN(C)CCN(CC(=O)O)CC(=O)O`
ZINC19364892 ZINC	0.737	232.3 Da LogP -0.20 TPSA 81.1	✓ Ro5	✓ Clean	`CCN(CC)CCN(CC(=O)O)CC(=O)O`
ZINC19366122 ZINC	0.737	278.3 Da LogP -2.16 TPSA 138.6	✓ Ro5	✓ Clean	`O=C(O)CN(CCO)CCN(CC(=O)O)CC(=O)O`
ZINC33806192 ZINC	0.737	320.3 Da LogP -1.29 TPSA 155.7	✓ Ro5	✓ Clean	`O=C(O)CCN(CCC(=O)O)CCN(CC(=O)O)CC(=O)O`
ZINC5908834 ZINC	0.737	379.3 Da LogP -2.09 TPSA 196.2	✓ Ro5	✓ Clean	`O=C(O)CN(CCN(CCN(CC(=O)O)CC(=O)O)C(=O)O)CC(=O)O`
ZINC575419714 ZINC	0.727	312.4 Da LogP 0.42 TPSA 66.4	✓ Ro5	✓ Clean	`COCCOCCOCCSCCOCCOCCO`
ZINC2527900 ZINC	0.722	205.2 Da LogP -1.07 TPSA 115.1	✓ Ro5	✓ Clean	`O=C(O)CCN(CC(=O)O)CC(=O)O`
ZINC4261886 ZINC	0.722	348.4 Da LogP -0.51 TPSA 155.7	✓ Ro5	✓ Clean	`O=C(O)CN(CCCCCCN(CC(=O)O)CC(=O)O)CC(=O)O`
ZINC115163232 ZINC	0.700	222.3 Da LogP 0.07 TPSA 57.2	✓ Ro5	✓ Clean	`COCCOCCOCCOCCCO`
ZINC149813449 ZINC	0.700	278.2 Da LogP -1.48 TPSA 155.7	✓ Ro5	✓ Clean	`O=C(O)CN(CCN(CC(=O)O)C(=O)O)CC(=O)O`
ZINC258837490 ZINC	0.700	354.4 Da LogP 0.11 TPSA 84.8	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCCO`
ZINC12501520 ZINC	0.688	458.5 Da LogP -0.88 TPSA 123.5	1 viol.	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC1692489 ZINC	0.688	222.3 Da LogP 0.33 TPSA 46.2	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOC`
ZINC3874716 ZINC	0.688	414.5 Da LogP -0.90 TPSA 114.3	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC4283769 ZINC	0.688	238.3 Da LogP -0.96 TPSA 77.4	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCO`
ZINC4521548 ZINC	0.688	282.3 Da LogP -0.95 TPSA 86.6	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCO`
ZINC4530388 ZINC	0.688	266.3 Da LogP 0.35 TPSA 55.4	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOC`
ZINC5178829 ZINC	0.688	326.4 Da LogP -0.93 TPSA 95.8	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCO`
ZINC5178830 ZINC	0.688	370.4 Da LogP -0.91 TPSA 105.1	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC5701172 ZINC	0.688	310.4 Da LogP 0.36 TPSA 64.6	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOC`
ZINC5997861 ZINC	0.688	398.5 Da LogP 0.40 TPSA 83.1	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOC`
ZINC22576460 ZINC	0.684	320.3 Da LogP -1.29 TPSA 155.7	✓ Ro5	✓ Clean	`O=C(O)CCN(CCN(CCC(=O)O)CC(=O)O)CC(=O)O`
ZINC575432150 ZINC	0.667	344.4 Da LogP -0.89 TPSA 100.5	✓ Ro5	✓ Clean	`COCCOCCOCCS(=O)(=O)CCOCCOCCO`
ZINC90669676 ZINC	0.667	377.4 Da LogP -2.57 TPSA 176.0	✓ Ro5	✓ Clean	`O=CCN(CCN(CC(=O)O)CC(=O)O)CCN(CC(=O)O)CC(=O)O`
ZINC1532705 ZINC	0.660	249.2 Da LogP 0.20 TPSA 120.1	✓ Ro5	✓ Clean	`Cc1ncc(COP(=O)(O)O)c(CO)c1O`
ZINC1857524240 ZINC	0.652	207.3 Da LogP -0.75 TPSA 60.0	✓ Ro5	✓ Clean	`COCCNCCOCCOCCO`
ZINC22052182 ZINC	0.650	336.3 Da LogP -2.05 TPSA 164.9	✓ Ro5	✓ Clean	`O=C(O)CN(CCOCCN(CC(=O)O)CC(=O)O)CC(=O)O`
ZINC217755395 ZINC	0.636	263.2 Da LogP -1.47 TPSA 147.8	✓ Ro5	✓ Clean	`O=NN(CCN(CC(=O)O)CC(=O)O)CC(=O)O`
ZINC1532708 ZINC	0.620	248.2 Da LogP 0.16 TPSA 125.9	✓ Ro5	✓ Clean	`Cc1ncc(COP(=O)(O)O)c(CN)c1O`
ZINC3055005 ZINC	0.619	204.2 Da LogP -0.63 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCCC[C@H](N)C(=O)O)C(=O)O`
ZINC3055007 ZINC	0.619	204.2 Da LogP -0.63 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCCC[C@@H](N)C(=O)O)C(=O)O`
ZINC3055010 ZINC	0.619	204.2 Da LogP -0.63 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@H](CCCC[C@@H](N)C(=O)O)C(=O)O`
ZINC3861663 ZINC	0.619	380.4 Da LogP -2.04 TPSA 174.1	✓ Ro5	✓ Clean	`O=C(O)CN(CCOCCOCCN(CC(=O)O)CC(=O)O)CC(=O)O`
ZINC21297783 ZINC	0.609	419.4 Da LogP -3.36 TPSA 179.8	✓ Ro5	✓ Clean	`CNC(=O)CN(CCN(CCN(CC(=O)O)CC(=O)NC)CC(=O)O)CC(=…`
ZINC5650743 ZINC	0.600	222.3 Da LogP 0.07 TPSA 57.2	✓ Ro5	✓ Clean	`CCOCCOCCOCCOCCO`
ZINC6403917 ZINC	0.600	354.4 Da LogP 0.11 TPSA 84.8	✓ Ro5	✓ Clean	`CCOCCOCCOCCOCCOCCOCCOCCO`
ZINC1555367 ZINC	0.591	232.3 Da LogP 0.15 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCCCCC[C@@H](N)C(=O)O)C(=O)O`
ZINC1720127 ZINC	0.591	218.3 Da LogP -0.24 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCCCC[C@H](N)C(=O)O)C(=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.