Protein target profile

KP13_00989

NADH-quinone oxidoreductase subunit F

Genome: KpKP13 Gene: AHE43481.1 nuoF 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3H110

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Length 445

Pocket druggability 0.769

Direct ligand evidence 0 70 total records

Functional annotation 1 EC 6 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 0.77, P2Rank 0.91). Use the 3D pocket comparison to verify whether they identify the same site. Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Strong predicted binding pocket FPocket selected-pocket score 0.77. This is a computational pocket signal, not binding validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.91. 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 (%): 54.135 Lower values reduce human off-target concern.
Human E-value: 3.45e-42
Gut microbiome similarity: 2.8% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 65.455 Higher values support similarity to known essential genes.
DEG E-value: 1.6699999999999999e-180 Smaller values mean stronger essential-gene similarity.

Localization

Localization: Cytoplasmic

Structure confidence

ColabFold pLDDT: 93.05 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 0.769

Structure A0A0H3H110

Pocket Pocket 7

P2Rank 0.911

Structure A0A0H3H110

Pocket Pocket 1

ColabFold model

FPocket 0.365 · Pocket 26

P2Rank 0.904 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 134 / 4744 genomes with a hit

Prevalence 2.8%

Cross-references

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

Sequence

UniProt A0A0H3H110

Sequence

Primary amino-acid sequence viewer.

MKTVIRTAETHPLTWRLRDDKQPVWLDEYRSKNGYEGARKALTGMAPDEIVTAVKDAGLKGRGGAGFSTGLKWSLMPKDESMNIRYLLCNADEMEPGTYKDRLLMEQLPHLLVEGMLISAFALKAYRGYIFLRGEYIEAAQHLRRAIAEATEAGLLGKNILGTGFDFELFVHTGAGRYICGEETALINSLEGRRANPRSKPPFPASSGVWGKPTCVNNVETLCNVPAILANGVEWYQNISTSKDAGTKLMGFSGRVKNPGVWELPFGTTAREILEDYAGGMRDGLKFKAWQPGGAGTDFLTEAHLDLPMEFESIGKAGSRLGTSLAMAVDHEINMVSLVRNLEEFFARESCGWCTPCRDGLPWSVKILRALERGEGQPGDIETLEQLCRFLGPGKTFCAHAPGAVEPLQSAIKYFREEFEAGIKQQFSNTHAINGIQPNLLKTRW

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 6 GO

Enzyme Commission (EC)

7.1.1.-

Gene Ontology (GO)

GO:0051287 Binding to nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NAD+, or the reduced form, NADH.
GO:0010181 Binding to flavin mono nucleotide. Flavin mono nucleotide (FMN) is the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes.
GO:0051539 Binding to a 4 iron, 4 sulfur (4Fe-4S) cluster; this cluster consists of four iron atoms, with the inorganic sulfur atoms found between the irons and acting as bridging ligands.
GO:0008137 Catalysis of the reaction: NADH + ubiquinone + 5 H+(in) = NAD+ + ubiquinol + 4 H+(out).
GO:0046872 Binding to a metal ion.
GO:0048038 Binding to a quinone, any member of a class of diketones derivable from aromatic compounds by conversion of two CH groups into CO groups with any necessary rearrangement of double bonds.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

27 records

Show feature table

Start	End	DB	Term	Name
349	360	ProSitePatterns	PS00645	Respiratory-chain NADH dehydrogenase 51 Kd subunit signature 2.
349	360	InterPro	IPR001949	NADH:ubiquinone oxidoreductase, 51kDa subunit, conserved site
338	421	Pfam	PF10589	NADH-ubiquinone oxidoreductase-F iron-sulfur binding region
338	421	InterPro	IPR019575	NADH-ubiquinone oxidoreductase 51kDa subunit, iron-sulphur binding domain
336	381	SMART	SM00928	NADH_4Fe_4S_2
336	381	InterPro	IPR019575	NADH-ubiquinone oxidoreductase 51kDa subunit, iron-sulphur binding domain
240	332	Gene3D	G3DSA:3.10.20.600	-
59	238	FunFam	G3DSA:3.40.50.11540:FF:000001	NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial
13	423	NCBIfam	TIGR01959	NADH-quinone oxidoreductase subunit NuoF
13	423	InterPro	IPR011537	NADH ubiquinone oxidoreductase, F subunit
334	432	Gene3D	G3DSA:1.20.1440.230	-
334	432	InterPro	IPR037207	NADH-ubiquinone oxidoreductase 51kDa subunit, iron-sulphur binding domain superfamily
5	58	Gene3D	G3DSA:6.10.250.1450	-
54	226	Pfam	PF01512	Respiratory-chain NADH dehydrogenase 51 Kd subunit
54	226	InterPro	IPR011538	NADH-ubiquinone oxidoreductase 51kDa subunit, FMN-binding domain
8	426	PANTHER	PTHR43578	NADH-QUINONE OXIDOREDUCTASE SUBUNIT F
59	238	Gene3D	G3DSA:3.40.50.11540	-
59	238	InterPro	IPR037225	NADH-ubiquinone oxidoreductase 51kDa subunit, FMN-binding domain superfamily
174	189	ProSitePatterns	PS00644	Respiratory-chain NADH dehydrogenase 51 Kd subunit signature 1.
174	189	InterPro	IPR001949	NADH:ubiquinone oxidoreductase, 51kDa subunit, conserved site
241	332	FunFam	G3DSA:3.10.20.600:FF:000002	NADH-quinone oxidoreductase subunit F
333	429	SUPERFAMILY	SSF140490	Nqo1C-terminal domain-like
333	429	InterPro	IPR037207	NADH-ubiquinone oxidoreductase 51kDa subunit, iron-sulphur binding domain superfamily
334	431	FunFam	G3DSA:1.20.1440.230:FF:000002	NADH-quinone oxidoreductase subunit F
13	247	SUPERFAMILY	SSF142019	Nqo1 FMN-binding domain-like
13	247	InterPro	IPR037225	NADH-ubiquinone oxidoreductase 51kDa subunit, FMN-binding domain superfamily
248	330	SUPERFAMILY	SSF142984	Nqo1 middle domain-like

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 #7

0.769

Unusual size

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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

0.911

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Surrounding area

Site 2 P2Rank #2

0.164

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Surrounding area

Site 3 P2Rank #3

0.049

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Surrounding area

Site 4 P2Rank #4

0.039

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Surrounding area

Site 5 P2Rank #5

0.023

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Surrounding area

Residue sets

UniProt: Binding site:351-351

UniProt: Binding site:354-354

UniProt: Binding site:357-357

UniProt: Binding site:398-398

Binding pockets · P2Rank

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

Site 1 P2Rank #1

0.904

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Surrounding area

Site 2 P2Rank #2

0.142

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Surrounding area

Site 3 P2Rank #3

0.048

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Surrounding area

Site 4 P2Rank #4

0.017

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Surrounding area

Site 5 P2Rank #5

0.011

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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_A0A0H3H110	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_00989	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.

70 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 20 records from similar proteins

Structural ligands 20 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

3PE PDB via homolog 748.1 Da · LogP 12.06 · TPSA 134.4 Open detail RCSB PDB

970 PDB via homolog Detail RCSB PDB

AYA PDB via homolog Detail RCSB PDB

CDL PDB via homolog Detail RCSB PDB

DCQ 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
3PE RCSB PDB	6QC2	W5PUX0	748.1 Da LogP 12.06 TPSA 134.4	2 viol.	✓ Clean	`CCCCCCCCCCCCCCCCCC(=O)OC[C@H](COP(=O)(O)OCCN)OC…`
970 RCSB PDB	6ZKL	W5PUX0	394.4 Da LogP 3.70 TPSA 63.2	✓ Ro5	✓ Clean	`CC(=C)[C@H]1Cc2c(ccc3c2O[C@@H]4COc5cc(c(cc5[C@@…`
AYA RCSB PDB	6ZKL	W5PUX0	131.1 Da LogP -0.40 TPSA 66.4	✓ Ro5	✓ Clean	`C[C@@H](C(=O)O)NC(=O)C`
CDL RCSB PDB	5GUP	A0A4X1SZP7	1464.1 Da LogP 23.31 TPSA 242.6	3 viol.	✓ Clean	`CCCCCCCCCCCCCCCCCC(=O)OC[C@H](COP(=O)([O-])OCC(…`
DCQ RCSB PDB	6ZKC	W5PUX0	322.4 Da LogP 4.49 TPSA 52.6	✓ Ro5	Alert	`CCCCCCCCCCC1=C(C(=O)C(=C(C1=O)OC)OC)C`
FES RCSB PDB	5LNK	W5PUX0	175.8 Da LogP 1.29 TPSA 0.0	✓ Ro5	✓ Clean	`S1[Fe]S[Fe]1`
FME RCSB PDB	6ZKL	W5PUX0	177.2 Da LogP -0.06 TPSA 66.4	✓ Ro5	✓ Clean	`CSCC[C@@H](C(=O)O)NC=O`
HQH RCSB PDB	6Q8O	Q56222	415.6 Da LogP 5.05 TPSA 71.6	1 viol.	✓ Clean	`C/C=C(\C)/[C@@H]([C@H](C)/C=C(\C)/C=C/C/C(=C/CC…`
HQK RCSB PDB	6Q8X	Q56222	364.9 Da LogP 5.24 TPSA 34.9	1 viol.	✓ Clean	`CC(C)(C)c1ccc(cc1)CSC2=C(C(=O)N(N=C2)C(C)(C)C)Cl`
HQW RCSB PDB	6Q8W	Q56222	397.4 Da LogP 4.66 TPSA 91.8	✓ Ro5	✓ Clean	`CC1=C(OC(=C(C1=O)C)OC)[C@H]2C/C(=C/C(=C/c3ccc(c…`
L3W RCSB PDB	6SAQ	O66841	697.4 Da LogP -3.38 TPSA 354.9	3 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
MYR RCSB PDB	6ZKF	W5PUX0	228.4 Da LogP 4.77 TPSA 37.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC(=O)O`
PC1 RCSB PDB	6ZKU	W5PUX0	790.2 Da LogP 12.17 TPSA 111.2	2 viol.	✓ Clean	`CCCCCCCCCCCCCCCCCC(=O)OC[C@H](CO[P@@](=O)([O-])…`
PEE RCSB PDB	5GUP	A0A4X1SZP7	744.0 Da LogP 11.61 TPSA 134.4	2 viol.	✓ Clean	`CCCCCCCC/C=C\CCCCCCCC(=O)OC[C@H](COP(=O)(O)OCCN…`
PLX RCSB PDB	5GUP	A0A4X1SZP7	767.1 Da LogP 11.61 TPSA 114.7	2 viol.	✓ Clean	`CCCCCCCCCCCCCCCCC[C@@H](O)O[C@H](CO[C@@H](CCCCC…`
PNS RCSB PDB	5LNK	W5PUX0	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`
SMA RCSB PDB	2YBB	Q56222	514.7 Da LogP 6.14 TPSA 87.4	2 viol.	✓ Clean	`C/C=C(\C)/C=C/C=C[C@@H]([C@@H](C)[C@H]([C@@H](C…`
UQ1 RCSB PDB	2YBB	Q56222	250.3 Da LogP 2.32 TPSA 52.6	✓ Ro5	Alert	`CC1=C(C(=O)C(=C(C1=O)OC)OC)CC=C(C)C`
UQ2 RCSB PDB	7DGQ	P25708	318.4 Da LogP 4.04 TPSA 52.6	✓ Ro5	Alert	`CC1=C(C(=O)C(=C(C1=O)OC)OC)C\C=C(/C)\CCC=C(C)C`
ZMP RCSB PDB	5GUP	A0A4X1SZP7	568.7 Da LogP 4.07 TPSA 162.3	1 viol.	✓ Clean	`CCCCCCCCCCCCCC(=O)SCCNC(=O)CCNC(=O)[C@H](C(C)(C…`

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
ZINC102190512 ZINC	1.000	467.5 Da LogP 4.25 TPSA 134.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@@H](CO[P@@](=O)(O)OCCN)OC(=O)C…`
ZINC13522091 ZINC	1.000	394.4 Da LogP 3.70 TPSA 63.2	✓ Ro5	✓ Clean	`C=C(C)[C@@H]1Cc2c(ccc3c2O[C@@H]2COc4cc(OC)c(OC)…`
ZINC1529498 ZINC	1.000	200.3 Da LogP 3.99 TPSA 37.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCC(=O)O`
ZINC1530417 ZINC	1.000	228.4 Da LogP 4.77 TPSA 37.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC(=O)O`
ZINC1530836 ZINC	1.000	394.4 Da LogP 3.70 TPSA 63.2	✓ Ro5	✓ Clean	`C=C(C)[C@@H]1Cc2c(ccc3c2O[C@H]2COc4cc(OC)c(OC)c…`
ZINC1628119 ZINC	1.000	214.3 Da LogP 4.38 TPSA 37.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCCC(=O)O`
ZINC2105913 ZINC	1.000	397.4 Da LogP 4.66 TPSA 91.8	✓ Ro5	✓ Clean	`COc1oc([C@@H]2C/C(=C/C(C)=C/c3ccc([N+](=O)[O-])…`
ZINC2548962 ZINC	1.000	394.4 Da LogP 3.70 TPSA 63.2	✓ Ro5	✓ Clean	`C=C(C)[C@@H]1Cc2c(ccc3c2O[C@H]2COc4cc(OC)c(OC)c…`
ZINC3860715 ZINC	1.000	394.4 Da LogP 3.70 TPSA 63.2	✓ Ro5	✓ Clean	`C=C(C)[C@H]1Cc2c(ccc3c2O[C@@H]2COc4cc(OC)c(OC)c…`
ZINC3874884 ZINC	1.000	394.4 Da LogP 3.70 TPSA 63.2	✓ Ro5	✓ Clean	`C=C(C)[C@@H]1Cc2c(ccc3c2O[C@@H]2COc4cc(OC)c(OC)…`
ZINC3874885 ZINC	1.000	394.4 Da LogP 3.70 TPSA 63.2	✓ Ro5	✓ Clean	`C=C(C)[C@H]1Cc2c(ccc3c2O[C@H]2COc4cc(OC)c(OC)cc…`
ZINC4025640 ZINC	1.000	397.4 Da LogP 4.66 TPSA 91.8	✓ Ro5	✓ Clean	`COc1oc([C@H]2C/C(=C/C(C)=C/c3ccc([N+](=O)[O-])c…`
ZINC8660420 ZINC	1.000	394.4 Da LogP 3.70 TPSA 63.2	✓ Ro5	✓ Clean	`C=C(C)[C@H]1Cc2c(ccc3c2O[C@@H]2COc4cc(OC)c(OC)c…`
ZINC27416437 ZINC	0.976	411.4 Da LogP 2.69 TPSA 134.4	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@H](CO[P@](=O)(O)OCCN)OC(=O)CCCCC`
ZINC33902364 ZINC	0.976	411.4 Da LogP 2.69 TPSA 134.4	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@@H](CO[P@@](=O)(O)OCCN)OC(=O)CCC…`
ZINC102190506 ZINC	0.872	467.5 Da LogP 4.25 TPSA 134.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@H](CO[P@@](=O)(O)OCCN)OC(=O)CC…`
ZINC226792912 ZINC	0.860	396.4 Da LogP 2.72 TPSA 80.3	✓ Ro5	✓ Clean	`COc1cc2c(cc1OC)[C@@H]1C(=O)c3ccc4c(c3O[C@@H]1CO…`
ZINC226792928 ZINC	0.860	396.4 Da LogP 2.72 TPSA 80.3	✓ Ro5	✓ Clean	`COc1cc2c(cc1OC)[C@@H]1C(=O)c3ccc4c(c3O[C@H]1CO2…`
ZINC230121190 ZINC	0.860	396.4 Da LogP 2.72 TPSA 80.3	✓ Ro5	✓ Clean	`COc1cc2c(cc1OC)[C@@H]1C(=O)c3ccc4c(c3O[C@@H]1CO…`
ZINC230121201 ZINC	0.860	396.4 Da LogP 2.72 TPSA 80.3	✓ Ro5	✓ Clean	`COc1cc2c(cc1OC)[C@@H]1C(=O)c3ccc4c(c3O[C@H]1CO2…`
ZINC138457918 ZINC	0.850	228.3 Da LogP 3.56 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)CCCCC(=O)O`
ZINC138458029 ZINC	0.850	228.3 Da LogP 3.56 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)CCCCCC(=O)O`
ZINC144395054 ZINC	0.850	242.4 Da LogP 3.95 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCC(=O)CCCCCCCC(=O)O`
ZINC14619628 ZINC	0.850	270.4 Da LogP 4.73 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCC(=O)CCCCCCCCCC(=O)O`
ZINC196749828 ZINC	0.850	214.3 Da LogP 3.17 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)CCCCC(=O)O`
ZINC2113934076 ZINC	0.850	256.4 Da LogP 4.34 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)CCCCCCCC(=O)O`
ZINC2113934082 ZINC	0.850	256.4 Da LogP 4.34 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)CCCCCCC(=O)O`
ZINC2113934083 ZINC	0.850	256.4 Da LogP 4.34 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCCC(=O)CCCCC(=O)O`
ZINC2243670 ZINC	0.850	228.3 Da LogP 3.56 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCC(=O)CCCCCCC(=O)O`
ZINC2569203 ZINC	0.850	214.3 Da LogP 3.17 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCC(=O)CCCCCC(=O)O`
ZINC4798470 ZINC	0.850	270.4 Da LogP 4.73 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)CCCCCCCCC(=O)O`
ZINC5973005 ZINC	0.850	242.4 Da LogP 3.95 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)CCCCCCC(=O)O`
ZINC71418182 ZINC	0.850	270.4 Da LogP 4.73 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCCCC(=O)CCCCC(=O)O`
ZINC79244776 ZINC	0.850	270.4 Da LogP 4.73 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)CCCCCCCC(=O)O`
ZINC86037082 ZINC	0.850	270.4 Da LogP 4.73 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCCC(=O)CCCCCC(=O)O`
ZINC86037089 ZINC	0.850	270.4 Da LogP 4.73 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCC(=O)CCCCCCC(=O)O`
ZINC86039283 ZINC	0.850	242.4 Da LogP 3.95 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCC(=O)CCCCC(=O)O`
ZINC13813085 ZINC	0.820	410.4 Da LogP 2.68 TPSA 83.5	✓ Ro5	✓ Clean	`C=C(CO)[C@@H]1Cc2c(ccc3c2O[C@H]2COc4cc(OC)c(OC)…`
ZINC13813088 ZINC	0.820	410.4 Da LogP 2.68 TPSA 83.5	✓ Ro5	✓ Clean	`C=C(CO)[C@@H]1Cc2c(ccc3c2O[C@@H]2COc4cc(OC)c(OC…`
ZINC2115043 ZINC	0.820	410.4 Da LogP 2.68 TPSA 83.5	✓ Ro5	✓ Clean	`C=C(CO)[C@@H]1Cc2c(ccc3c2O[C@@H]2COc4cc(OC)c(OC…`
ZINC36387001 ZINC	0.820	410.4 Da LogP 2.68 TPSA 83.5	✓ Ro5	✓ Clean	`C=C(CO)[C@@H]1Cc2c(ccc3c2O[C@H]2COc4cc(OC)c(OC)…`
ZINC3947515 ZINC	0.820	410.4 Da LogP 2.68 TPSA 83.5	✓ Ro5	✓ Clean	`C=C(CO)[C@H]1Cc2c(ccc3c2O[C@@H]2COc4cc(OC)c(OC)…`
ZINC2242696 ZINC	0.810	273.3 Da LogP -1.39 TPSA 124.6	✓ Ro5	✓ Clean	`CC(=O)N[C@@H](C)C(=O)N[C@@H](C)C(=O)N[C@@H](C)C…`
ZINC2566274 ZINC	0.810	344.4 Da LogP -1.89 TPSA 153.7	✓ Ro5	✓ Clean	`CC(=O)N[C@@H](C)C(=O)N[C@@H](C)C(=O)N[C@@H](C)C…`
ZINC2572098 ZINC	0.810	202.2 Da LogP -0.90 TPSA 95.5	✓ Ro5	✓ Clean	`CC(=O)N[C@@H](C)C(=O)N[C@@H](C)C(=O)O`
ZINC3160730 ZINC	0.810	214.3 Da LogP 3.17 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)CCCC(=O)O`
ZINC4582907 ZINC	0.810	200.3 Da LogP 2.78 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)CCCC(=O)O`
ZINC4727003 ZINC	0.810	312.4 Da LogP 4.69 TPSA 71.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)CCC(=O)CCCCCCCC(=O)O`
ZINC5706638 ZINC	0.810	344.4 Da LogP -1.89 TPSA 153.7	✓ Ro5	✓ Clean	`CC(=O)N[C@H](C)C(=O)N[C@@H](C)C(=O)N[C@@H](C)C(…`
ZINC5706640 ZINC	0.810	344.4 Da LogP -1.89 TPSA 153.7	✓ Ro5	✓ Clean	`CC(=O)N[C@H](C)C(=O)N[C@H](C)C(=O)N[C@@H](C)C(=…`

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.