KpATCC43816 Protein target profile

ubiquinone oxidoreductase, Na(+)-translocating, F subunit

Accession: VK055_2322

Gene: AIK80926.1 nqrF 3D evidence: Experimental + ColabFold model Metabolism Not in network UniProt A6T526

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Length 407

Pocket druggability (P2Rank · Experimental) 0.576

Direct ligand evidence 0 57 total records

Functional annotation 0 EC 6 GO

Target summary

Strong target candidate with converging metabolic, structural and chemical evidence.

Automated synthesis of the evidence currently loaded. Review the underlying records before prioritizing this protein.

Main supporting evidence

Independent pocket support: P2Rank + FPocket Both predictors report a high-scoring binding site (P2Rank 0.58, FPocket 0.97). Use the 3D pocket comparison to verify whether they identify the same site. Experimental structure available At least one PDB experimental structure is loaded, not just a predicted model - stronger structural coverage than AlphaFold/ColabFold alone. Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Strong predicted binding pocket FPocket selected-pocket score 0.97. This is a computational pocket signal, not binding validation. 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 (%): 26.531 Lower values reduce human off-target concern.
Human E-value: 2.27e-08
Gut microbiome similarity: 8.8% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): N
DEG identity (%): 28.0 Higher values support similarity to known essential genes.

Structure confidence

ColabFold pLDDT: 93.52 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

PDB experimental structure

P2Rank's binding-site probability is the primary druggability signal shown across the app; FPocket's druggability score is shown alongside it for comparison. Both estimate small-molecule pocket quality after applying the curated structure priority — neither is experimental binding evidence. The 3D viewer may show a different loaded structure, so visible pockets can differ.

Druggability (P2Rank) 0.576

Structure 7QU0

Pocket Pocket 1

Druggability (FPocket) 0.966

Structure 7QTY

Pocket Pocket 1

ColabFold model

P2Rank 0.576 · Pocket 1

FPocket 0.817 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 417 / 4744 genomes with a hit

Prevalence 8.8%

Metabolic context

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

This protein is not associated with the imported metabolic network for this genome.

Browse the genome's metabolic network

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MEIILGVVMFTLIVLVLSGLILAARSKLVNAGDVVIEINNEADKQIRTPAGDKLLNTLSSNGIFVSSACGGGGSCGQCRVTVKEGGGDILPTELSHITKRDAKAGCRLACQVAVKQNMKIELPEEIFGVKKWECEVISNDNKATFIKELKLRIPEGEVVPFRAGGYIQIECPPHKVAYADFDVPDEYRSDWDKFNLFRYVSEVKEPTLRAYSMANYPEEKGIIMLNVRIATPPPKVPDAPPGIMSSYIWSLKPGDKVTISGPFGEFFAKETDAEMVFIGGGAGMAPMRSHIFDQLKRLHSTRKISFWYGARSLREMFYDEEFEQLARDNPNFTFHVALSDPLPEDNWTGHTGFIHNVLYENYLRDHPAPEDCEFYMCGPPVMNAAVIKMLKDLGVEDENILLDDFGG

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

6 GO

Subcellular localization

Localization: Cytoplasmic

Gene Ontology (GO)

GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
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: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:0016655 Catalysis of an oxidation-reduction (redox) reaction in which NADH or NADPH acts as a hydrogen or electron donor and reduces a quinone or a similar acceptor molecule.
GO:0006814 The directed movement of sodium ions (Na+) into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
GO:0051536 Binding to an iron-sulfur cluster, a combination of iron and sulfur atoms.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

47 records

Show feature table

Start	End	DB	Term	Name
123	405	CDD	cd06188	NADH_quinone_reductase
275	393	Gene3D	G3DSA:3.40.50.80	-
275	393	InterPro	IPR039261	Ferredoxin-NADP reductase (FNR), nucleotide-binding domain
373	381	PRINTS	PR00371	Flavoprotein pyridine nucleotide cytochrome reductase signature
373	381	InterPro	IPR001709	Flavoprotein pyridine nucleotide cytochrome reductase
242	251	PRINTS	PR00371	Flavoprotein pyridine nucleotide cytochrome reductase signature
242	251	InterPro	IPR001709	Flavoprotein pyridine nucleotide cytochrome reductase
209	216	PRINTS	PR00371	Flavoprotein pyridine nucleotide cytochrome reductase signature
209	216	InterPro	IPR001709	Flavoprotein pyridine nucleotide cytochrome reductase
276	295	PRINTS	PR00371	Flavoprotein pyridine nucleotide cytochrome reductase signature
276	295	InterPro	IPR001709	Flavoprotein pyridine nucleotide cytochrome reductase
314	325	PRINTS	PR00371	Flavoprotein pyridine nucleotide cytochrome reductase signature
314	325	InterPro	IPR001709	Flavoprotein pyridine nucleotide cytochrome reductase
32	126	ProSiteProfiles	PS51085	2Fe-2S ferredoxin-type iron-sulfur binding domain profile.
32	126	InterPro	IPR001041	2Fe-2S ferredoxin-type iron-sulfur binding domain
37	124	SUPERFAMILY	SSF54292	2Fe-2S ferredoxin-like
37	124	InterPro	IPR036010	2Fe-2S ferredoxin-like superfamily
126	264	FunFam	G3DSA:2.40.30.10:FF:000064	Na(+)-translocating NADH-quinone reductase subunit F
34	125	Gene3D	G3DSA:3.10.20.30	-
34	125	InterPro	IPR012675	Beta-grasp domain superfamily
24	31	Phobius	SIGNAL_PEPTIDE_C_REGION	C-terminal region of a signal peptide.
43	115	Pfam	PF00111	2Fe-2S iron-sulfur cluster binding domain
43	115	InterPro	IPR001041	2Fe-2S ferredoxin-type iron-sulfur binding domain
2	24	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
255	402	SUPERFAMILY	SSF52343	Ferredoxin reductase-like, C-terminal NADP-linked domain
255	402	InterPro	IPR039261	Ferredoxin-NADP reductase (FNR), nucleotide-binding domain
4	23	Phobius	SIGNAL_PEPTIDE_H_REGION	Hydrophobic region of a signal peptide.
1	23	SignalP_EUK	SignalP-TM	SignalP-TM
1	3	Phobius	SIGNAL_PEPTIDE_N_REGION	N-terminal region of a signal peptide.
1	31	Phobius	SIGNAL_PEPTIDE	Signal peptide region
1	407	PIRSF	PIRSF000044	Cis_Diol_DH_RD
1	407	InterPro	IPR010205	Na(+)-translocating NADH-quinone reductase subunit F
3	407	NCBIfam	TIGR01941	NADH:ubiquinone reductase (Na(+)-transporting) subunit F
3	407	InterPro	IPR010205	Na(+)-translocating NADH-quinone reductase subunit F
204	266	Pfam	PF00970	Oxidoreductase FAD-binding domain
204	266	InterPro	IPR008333	Flavoprotein pyridine nucleotide cytochrome reductase-like, FAD-binding domain
126	264	Gene3D	G3DSA:2.40.30.10	Translation factors
129	269	ProSiteProfiles	PS51384	Ferredoxin reductase-type FAD binding domain profile.
129	269	InterPro	IPR017927	FAD-binding domain, ferredoxin reductase-type
23	407	PANTHER	PTHR43644	NA(+)-TRANSLOCATING NADH-QUINONE REDUCTASE SUBUNIT
275	393	FunFam	G3DSA:3.40.50.80:FF:000014	Na(+)-translocating NADH-quinone reductase subunit F
1	407	Hamap	MF_00430	Na(+)-translocating NADH-quinone reductase subunit F [nqrF].
105	272	SUPERFAMILY	SSF63380	Riboflavin synthase domain-like
105	272	InterPro	IPR017938	Riboflavin synthase-like beta-barrel
277	386	Pfam	PF00175	Oxidoreductase NAD-binding domain
277	386	InterPro	IPR001433	Oxidoreductase FAD/NAD(P)-binding
32	407	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.

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 (FPocket): high ≥ 0.7 · medium 0.4–0.69 · low < 0.4

Pocket 1 FPocket #1

0.966

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Surrounding area

Binding pockets · P2Rank

Druggability (P2Rank): high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Pocket 1 P2Rank #1

0.576

Likely same site as FPocket 1 2.1 Å 19 shared residues 95% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.383

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Surrounding area

Pocket 3 P2Rank #3

0.237

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Surrounding area

Pocket 4 P2Rank #4

0.045

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Surrounding area

Pocket 5 P2Rank #5

0.022

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Surrounding area

Binding pockets · FPocket

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

Pocket 1 FPocket #1

0.817 Unusual size

Likely same site as P2Rank 1 2.1 Å 19 shared residues 95% of smaller site

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Surrounding area

Pocket 2 FPocket #13

0.356

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Surrounding area

All structural evidence 2 experimental · 1 predicted

Structural evidence

2 + 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
PDB 7QTY	X-ray	—	A	—	PDBe RCSB PDBj File	Viewing
PDB 7QU0	X-ray	—	A	—	PDBe RCSB PDBj File	Loaded
ColabFold VK055_2322	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.

57 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 7 records from similar proteins

Structural ligands 7 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

BTB PDB via homolog 209.2 Da · LogP -3.01 · TPSA 104.4 Open detail RCSB PDB

DGG PDB via homolog Detail RCSB PDB

ECN PDB via homolog Detail RCSB PDB

FDA PDB via homolog Detail RCSB PDB

FES 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
BTB RCSB PDB	4WQM	Q03304	209.2 Da LogP -3.01 TPSA 104.4	✓ Ro5	✓ Clean	`C(CO)N(CCO)C(CO)(CO)CO`
DGG RCSB PDB	1CQX	P39662	735.0 Da LogP 9.75 TPSA 148.8	2 viol.	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OC[C@H](CO[P@@](=O)(O)OC[C@…`
ECN RCSB PDB	3OZV	P39662	381.7 Da LogP 5.80 TPSA 27.1	1 viol.	✓ Clean	`c1cc(ccc1COC(Cn2ccnc2)c3ccc(cc3Cl)Cl)Cl`
FDA RCSB PDB	1TVC	P22868	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…`
FES RCSB PDB	5OGX	A0A076MZ01	175.8 Da LogP 1.29 TPSA 0.0	✓ Ro5	✓ Clean	`S1[Fe]S[Fe]1`
KKK RCSB PDB	3OZW	P39662	531.4 Da LogP 4.21 TPSA 69.1	1 viol.	Alert	`CC(=O)N1CCN(CC1)c2ccc(cc2)OC[C@H]3CO[C@](O3)(Cn…`
X89 RCSB PDB	3OZU	P39662	416.1 Da LogP 6.45 TPSA 27.1	1 viol.	✓ Clean	`c1cc(c(cc1Cl)Cl)CO[C@@H](Cn2ccnc2)c3ccc(cc3Cl)Cl`

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
ZINC1615342 ZINC	1.000	209.2 Da LogP -3.01 TPSA 104.4	✓ Ro5	✓ Clean	`OCCN(CCO)C(CO)(CO)CO`
ZINC102191119 ZINC	0.824	498.6 Da LogP 3.65 TPSA 148.8	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@H](CO[P@@](=O)(O)OC[C@@H](O)CO…`
ZINC58649551 ZINC	0.824	498.6 Da LogP 3.65 TPSA 148.8	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@H](CO[P@@](=O)(O)OC[C@H](O)CO)…`
ZINC28568236 ZINC	0.795	489.4 Da LogP 3.95 TPSA 60.8	✓ Ro5	Alert	`Clc1ccc([C@@]2(Cn3ccnc3)OC[C@H](COc3ccc(N4CCNCC…`
ZINC31416683 ZINC	0.795	489.4 Da LogP 3.95 TPSA 60.8	✓ Ro5	Alert	`Clc1ccc([C@]2(Cn3ccnc3)OC[C@@H](COc3ccc(N4CCNCC…`
ZINC38944078 ZINC	0.795	489.4 Da LogP 3.95 TPSA 60.8	✓ Ro5	Alert	`Clc1ccc([C@]2(Cn3ccnc3)OC[C@H](COc3ccc(N4CCNCC4…`
ZINC38944080 ZINC	0.795	489.4 Da LogP 3.95 TPSA 60.8	✓ Ro5	Alert	`Clc1ccc([C@@]2(Cn3ccnc3)OC[C@@H](COc3ccc(N4CCNC…`
ZINC1532199 ZINC	0.729	297.2 Da LogP 4.13 TPSA 27.1	✓ Ro5	✓ Clean	`C=CCO[C@@H](Cn1ccnc1)c1ccc(Cl)cc1Cl`
ZINC1532200 ZINC	0.729	297.2 Da LogP 4.13 TPSA 27.1	✓ Ro5	✓ Clean	`C=CCO[C@H](Cn1ccnc1)c1ccc(Cl)cc1Cl`
ZINC95918118 ZINC	0.673	312.8 Da LogP 4.49 TPSA 27.1	✓ Ro5	✓ Clean	`Clc1ccc(CO[C@H](Cn2ccnc2)c2ccccc2)cc1`
ZINC95918119 ZINC	0.673	312.8 Da LogP 4.49 TPSA 27.1	✓ Ro5	✓ Clean	`Clc1ccc(CO[C@@H](Cn2ccnc2)c2ccccc2)cc1`
ZINC102191158 ZINC	0.660	456.5 Da LogP 3.08 TPSA 142.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC(=O)OC[C@H](O)CO[P@@](=O)(O)OC[C@…`
ZINC14880758 ZINC	0.660	484.6 Da LogP 3.86 TPSA 142.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OC[C@@H](O)CO[P@](=O)(O)OC[…`
ZINC14880760 ZINC	0.660	484.6 Da LogP 3.86 TPSA 142.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OC[C@H](O)CO[P@](=O)(O)OC[C…`
ZINC53683910 ZINC	0.660	484.6 Da LogP 3.86 TPSA 142.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OC[C@H](O)CO[P@@](=O)(O)OC[…`
ZINC62592202 ZINC	0.660	456.5 Da LogP 3.08 TPSA 142.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC(=O)OC[C@H](O)CO[P@@](=O)(O)OC[C@…`
ZINC62592203 ZINC	0.660	456.5 Da LogP 3.08 TPSA 142.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC(=O)OC[C@@H](O)CO[P@@](=O)(O)OC[C…`
ZINC62592204 ZINC	0.660	484.6 Da LogP 3.86 TPSA 142.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OC[C@@H](O)CO[P@@](=O)(O)OC…`
ZINC96094841 ZINC	0.660	456.5 Da LogP 3.08 TPSA 142.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC(=O)OC[C@@H](O)CO[P@@](=O)(O)OC[C…`
ZINC849188212 ZINC	0.654	327.2 Da LogP 4.13 TPSA 44.1	✓ Ro5	✓ Clean	`CC(C)C(=O)O[C@@H](Cn1ccnc1)c1ccc(Cl)cc1Cl`
ZINC849188213 ZINC	0.654	327.2 Da LogP 4.13 TPSA 44.1	✓ Ro5	✓ Clean	`CC(C)C(=O)O[C@H](Cn1ccnc1)c1ccc(Cl)cc1Cl`
ZINC38334168 ZINC	0.649	407.3 Da LogP 2.43 TPSA 79.7	✓ Ro5	✓ Clean	`CS(=O)(=O)OC[C@@H]1CO[C@](Cn2ccnc2)(c2ccc(Cl)cc…`
ZINC198375289 ZINC	0.635	299.2 Da LogP 3.49 TPSA 44.1	✓ Ro5	✓ Clean	`CC(=O)O[C@@H](Cn1ccnc1)c1ccc(Cl)cc1Cl`
ZINC198375301 ZINC	0.635	299.2 Da LogP 3.49 TPSA 44.1	✓ Ro5	✓ Clean	`CC(=O)O[C@H](Cn1ccnc1)c1ccc(Cl)cc1Cl`
ZINC5349880 ZINC	0.628	433.3 Da LogP 4.32 TPSA 62.6	✓ Ro5	✓ Clean	`O=C(OC[C@@H]1CO[C@@](Cn2ccnc2)(c2ccc(Cl)cc2Cl)O…`
ZINC5349883 ZINC	0.628	433.3 Da LogP 4.32 TPSA 62.6	✓ Ro5	✓ Clean	`O=C(OC[C@H]1CO[C@@](Cn2ccnc2)(c2ccc(Cl)cc2Cl)O1…`
ZINC638711 ZINC	0.628	433.3 Da LogP 4.32 TPSA 62.6	✓ Ro5	✓ Clean	`O=C(OC[C@H]1CO[C@](Cn2ccnc2)(c2ccc(Cl)cc2Cl)O1)…`
ZINC638717 ZINC	0.628	433.3 Da LogP 4.32 TPSA 62.6	✓ Ro5	✓ Clean	`O=C(OC[C@@H]1CO[C@](Cn2ccnc2)(c2ccc(Cl)cc2Cl)O1…`
ZINC297645 ZINC	0.620	329.2 Da LogP 2.45 TPSA 56.5	✓ Ro5	✓ Clean	`OC[C@@H]1CO[C@](Cn2ccnc2)(c2ccc(Cl)cc2Cl)O1`
ZINC297649 ZINC	0.620	329.2 Da LogP 2.45 TPSA 56.5	✓ Ro5	✓ Clean	`OC[C@@H]1CO[C@@](Cn2ccnc2)(c2ccc(Cl)cc2Cl)O1`
ZINC297652 ZINC	0.620	329.2 Da LogP 2.45 TPSA 56.5	✓ Ro5	✓ Clean	`OC[C@H]1CO[C@](Cn2ccnc2)(c2ccc(Cl)cc2Cl)O1`
ZINC297656 ZINC	0.620	329.2 Da LogP 2.45 TPSA 56.5	✓ Ro5	✓ Clean	`OC[C@H]1CO[C@@](Cn2ccnc2)(c2ccc(Cl)cc2Cl)O1`
ZINC102190506 ZINC	0.614	467.5 Da LogP 4.25 TPSA 134.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@H](CO[P@@](=O)(O)OCCN)OC(=O)CC…`
ZINC102190512 ZINC	0.614	467.5 Da LogP 4.25 TPSA 134.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@@H](CO[P@@](=O)(O)OCCN)OC(=O)C…`
ZINC4217243 ZINC	0.605	367.2 Da LogP 3.11 TPSA 45.5	✓ Ro5	✓ Clean	`C#CCOC[C@H]1CO[C@](Cn2ccnc2)(c2ccc(Cl)cc2Cl)O1`
ZINC390893 ZINC	0.604	257.1 Da LogP 2.92 TPSA 38.0	✓ Ro5	✓ Clean	`O[C@H](Cn1ccnc1)c1ccc(Cl)cc1Cl`
ZINC390894 ZINC	0.604	257.1 Da LogP 2.92 TPSA 38.0	✓ Ro5	✓ Clean	`O[C@@H](Cn1ccnc1)c1ccc(Cl)cc1Cl`
ZINC21988957 ZINC	0.600	483.4 Da LogP 4.17 TPSA 79.7	✓ Ro5	✓ Clean	`Cc1ccc(S(=O)(=O)OC[C@H]2CO[C@](Cn3ccnc3)(c3ccc(…`
ZINC22057057 ZINC	0.600	483.4 Da LogP 4.17 TPSA 79.7	✓ Ro5	✓ Clean	`Cc1ccc(S(=O)(=O)OC[C@@H]2CO[C@@](Cn3ccnc3)(c3cc…`
ZINC22057060 ZINC	0.600	483.4 Da LogP 4.17 TPSA 79.7	✓ Ro5	✓ Clean	`Cc1ccc(S(=O)(=O)OC[C@@H]2CO[C@](Cn3ccnc3)(c3ccc…`
ZINC6088320 ZINC	0.600	483.4 Da LogP 4.17 TPSA 79.7	✓ Ro5	✓ Clean	`Cc1ccc(S(=O)(=O)OC[C@H]2CO[C@@](Cn3ccnc3)(c3ccc…`
ZINC849187659 ZINC	0.600	325.2 Da LogP 3.88 TPSA 44.1	✓ Ro5	✓ Clean	`O=C(O[C@@H](Cn1ccnc1)c1ccc(Cl)cc1Cl)C1CC1`
ZINC849187660 ZINC	0.600	325.2 Da LogP 3.88 TPSA 44.1	✓ Ro5	✓ Clean	`O=C(O[C@H](Cn1ccnc1)c1ccc(Cl)cc1Cl)C1CC1`
ZINC27416437 ZINC	0.596	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	0.596	411.4 Da LogP 2.69 TPSA 134.4	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@@H](CO[P@@](=O)(O)OCCN)OC(=O)CCC…`
ZINC36178999 ZINC	0.593	424.5 Da LogP 4.27 TPSA 119.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@@H](COP(=O)(O)O)OC(=O)CCCCCCC`
ZINC36179002 ZINC	0.593	424.5 Da LogP 4.27 TPSA 119.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@H](COP(=O)(O)O)OC(=O)CCCCCCC`
ZINC849188227 ZINC	0.589	341.2 Da LogP 4.52 TPSA 44.1	✓ Ro5	✓ Clean	`CC(C)CC(=O)O[C@@H](Cn1ccnc1)c1ccc(Cl)cc1Cl`
ZINC849188228 ZINC	0.589	341.2 Da LogP 4.52 TPSA 44.1	✓ Ro5	✓ Clean	`CC(C)CC(=O)O[C@H](Cn1ccnc1)c1ccc(Cl)cc1Cl`
ZINC849188301 ZINC	0.589	355.3 Da LogP 4.91 TPSA 44.1	✓ Ro5	✓ Clean	`CCC(CC)C(=O)O[C@H](Cn1ccnc1)c1ccc(Cl)cc1Cl`

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.

Cross-references

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

Sequence

UniProt A6T526

Structure

PDB 7QTY PDB 7QU0