KpATCC43816 Protein target profile

pentaerythritol tetranitrate reductase

Accession: VK055_0488

Gene: onr AIK79111.1 3D evidence: Experimental + ColabFold model Metabolism Not in network UniProt A0A0H3GQS4

Export view

Length 365

Pocket druggability (P2Rank · Experimental) 0.868

Direct ligand evidence 0 70 total records

Functional annotation 0 EC 4 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 0.87, FPocket 0.92). 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. No similar human protein detected The current BLAST sequence screen did not find a significant human match, lowering apparent off-target risk. Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. 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: No hit
Gut microbiome similarity: 2.2% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): N
DEG identity (%): 37.681 Higher values support similarity to known essential genes.

Structure confidence

ColabFold pLDDT: 97.85 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) 0.868

Structure 7TMB

Pocket Pocket 1

Druggability (FPocket) 0.915

Structure 7TMB

Pocket Pocket 3

ColabFold model

P2Rank 0.9 · Pocket 1

FPocket 0.491 · Pocket 4

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 105 / 4744 genomes with a hit

Prevalence 2.2%

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.

MSEAKLFSPLKVGAVTVPNRVFMAPLTRLRSIEPGDIPTPLMGEYYRQRASSGLIITEATQISAQAKGYAGAPGLHSPEQIAAWQKITAGVHAENGHIAVQLWHTGRISHSSLQPGGAAPVAPSALSAGTRTSLRDENGHAIRVDTSMPRALETAEIPGIVNDFRQAVGNARDAGFDLVELHSAHGYLLHQFLSPSANQRTDQYGGSVENRARLVLEVVDAVSQEWSAERIGIRVSPIGSFQNVDNGPNEEEDALYLISELAKRGIAYLHMSEPDWAGGKPYSEAFRQKVRDRFPGVIIGAGAYTVEKANDLINKGLIDAVAFGRDYIANPDLVARLQKKAPLNPQRPESFYGGGAEGYTDYPTL

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

4 GO

Subcellular localization

Localization: Cytoplasmic

Gene Ontology (GO)

GO:0010181 Binding to flavin mono nucleotide. Flavin mono nucleotide (FMN) is the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes.
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:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
GO:0016628 Catalysis of an oxidation-reduction (redox) reaction in which a CH-CH group acts as a hydrogen or electron donor and reduces NAD or NADP.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

9 records

Show feature table

Start	End	DB	Term	Name
5	345	CDD	cd02933	OYE_like_FMN
4	364	PANTHER	PTHR22893	NADH OXIDOREDUCTASE-RELATED
4	364	InterPro	IPR045247	Oxidoreductase Oye-like
3	365	Gene3D	G3DSA:3.20.20.70	Aldolase class I
3	365	InterPro	IPR013785	Aldolase-type TIM barrel
3	365	FunFam	G3DSA:3.20.20.70:FF:000059	N-ethylmaleimide reductase, FMN-linked
5	344	Pfam	PF00724	NADH:flavin oxidoreductase / NADH oxidase family
5	344	InterPro	IPR001155	NADH:flavin oxidoreductase/NADH oxidase, N-terminal
4	364	SUPERFAMILY	SSF51395	FMN-linked oxidoreductases

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.

Download VMD script Full viewer

Loading 3D structure...

Drag to rotate — click the view, then scroll to zoom.

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 · P2Rank

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

Pocket 1 P2Rank #1

0.868

Show in viewer

Surrounding area

Pocket 2 P2Rank #2

0.023

Show in viewer

Surrounding area

Binding pockets · FPocket

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

Pocket 1 FPocket #3

0.915

Show in viewer

Surrounding area

Binding pockets · FPocket

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

Pocket 1 FPocket #4

0.491

Show in viewer

Surrounding area

Pocket 2 FPocket #1

0.283 Unusual size

Likely same site as P2Rank 1 1.3 Å 27 shared residues 96% of smaller site

Show in viewer

Surrounding area

Residue sets

UniProt: Binding site:101-101

UniProt: Binding site:182-182

UniProt: Binding site:234-234

UniProt: Binding site:25-25

UniProt: Binding site:27-27

UniProt: Binding site:303-303

UniProt: Binding site:324-324

UniProt: Binding site:325-325

UniProt: Binding site:59-59

All structural evidence 1 experimental · 1 predicted

Structural evidence

1 + 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 7TMB	X-ray	2.10 Å	A,B,C,D,E,F	100.0% 1-365	PDBe RCSB PDBj File	Viewing
ColabFold VK055_0488	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

1L5 PDB via homolog 163.2 Da · LogP 2.32 · TPSA 43.1 Open detail RCSB PDB

8OZ PDB via homolog Detail RCSB PDB

A2Q PDB via homolog Detail RCSB PDB

ANB PDB via homolog Detail RCSB PDB

BEN 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
1L5 RCSB PDB	4JIQ	O31246	163.2 Da LogP 2.32 TPSA 43.1	✓ Ro5	✓ Clean	`C/C(=C\N(=O)=O)/c1ccccc1`
8OZ RCSB PDB	5N6G	O31246	148.2 Da LogP 1.78 TPSA 37.3	✓ Ro5	✓ Clean	`C=C(c1ccccc1)C(=O)O`
A2Q RCSB PDB	1GVQ	P71278	96.1 Da LogP 1.30 TPSA 17.1	✓ Ro5	✓ Clean	`C1CC=CC(=O)C1`
ANB RCSB PDB	1H62	P71278	284.4 Da LogP 3.86 TPSA 34.1	✓ Ro5	✓ Clean	`C[C@]12CC[C@H]3[C@H]([C@@H]1CCC2=O)CCC4=CC(=O)C…`
BEN RCSB PDB	6S32	K9TVC9	120.2 Da LogP 0.97 TPSA 49.9	✓ Ro5	✓ Clean	`[H]/N=C(\c1ccccc1)/N`
DNF RCSB PDB	1GVO	P71278	184.1 Da LogP 1.21 TPSA 106.5	✓ Ro5	✓ Clean	`c1cc(c(cc1[N+](=O)[O-])[N+](=O)[O-])O`
FNR RCSB PDB	5LGZ	P71278	458.4 Da LogP -0.93 TPSA 208.4	1 viol.	✓ Clean	`Cc1cc2c(cc1C)N(C3=C(N2)C(=O)NC(=O)N3)C[C@@H]([C…`
HBA RCSB PDB	4JIP	O31246	122.1 Da LogP 1.20 TPSA 37.3	✓ Ro5	✓ Clean	`c1cc(ccc1C=O)O`
KSW RCSB PDB	6S23	M2XAQ9	94.1 Da LogP 1.07 TPSA 17.1	✓ Ro5	✓ Clean	`CC1=CC=CC1=O`
NYH RCSB PDB	3F03	P71278	127.1 Da LogP 1.72 TPSA 43.1	✓ Ro5	✓ Clean	`C1CCC(=CC1)[N+](=O)[O-]`
P7Y RCSB PDB	3P7Y	P71278	165.1 Da LogP 1.64 TPSA 63.4	✓ Ro5	✓ Clean	`c1ccc(c(c1)/C=C/[N+](=O)[O-])O`
P80 RCSB PDB	3P80	P71278	165.1 Da LogP 1.64 TPSA 63.4	✓ Ro5	✓ Clean	`c1cc(cc(c1)O)/C=C/[N+](=O)[O-]`
P81 RCSB PDB	3P81	P71278	165.1 Da LogP 1.64 TPSA 63.4	✓ Ro5	✓ Clean	`c1cc(ccc1/C=C/[N+](=O)[O-])O`
PDN RCSB PDB	1H61	P71278	358.4 Da LogP 3.16 TPSA 94.8	✓ Ro5	✓ Clean	`C[C@]12CC(=O)[C@H]3[C@H]([C@@H]1CC[C@@]2(C(=CO)…`
STR RCSB PDB	1H60	P71278	314.5 Da LogP 4.72 TPSA 34.1	✓ Ro5	✓ Clean	`CC(=O)[C@H]1CC[C@@H]2[C@@]1(CC[C@H]3[C@H]2CCC4=…`
TNF RCSB PDB	1GVS	P71278	229.1 Da LogP 1.12 TPSA 149.7	✓ Ro5	✓ Clean	`c1c(cc(c(c1[N+](=O)[O-])O)[N+](=O)[O-])[N+](=O)…`
TNL RCSB PDB	1GVR	P71278	227.1 Da LogP 1.72 TPSA 129.4	✓ Ro5	✓ Clean	`Cc1c(cc(cc1[N+](=O)[O-])[N+](=O)[O-])[N+](=O)[O…`
TXD RCSB PDB	2R14	Q51990	667.5 Da LogP -3.30 TPSA 317.6	3 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
U5N RCSB PDB	7BN6	M2XAQ9	98.1 Da LogP 0.49 TPSA 26.3	✓ Ro5	✓ Clean	`C[C@@H]1C=CC(=O)O1`
U6W RCSB PDB	7BO0	M2XAQ9	98.1 Da LogP 0.84 TPSA 26.3	✓ Ro5	✓ Clean	`CC1=CCC(=O)O1`

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
ZINC13521486 ZINC	1.000	314.5 Da LogP 4.72 TPSA 34.1	✓ Ro5	✓ Clean	`CC(=O)[C@H]1CC[C@@H]2[C@@H]3CCC4=CC(=O)CC[C@]4(…`
ZINC13542968 ZINC	1.000	314.5 Da LogP 4.72 TPSA 34.1	✓ Ro5	✓ Clean	`CC(=O)[C@H]1CC[C@H]2[C@@H]3CCC4=CC(=O)CC[C@@]4(…`
ZINC14880028 ZINC	1.000	227.1 Da LogP 1.72 TPSA 129.4	✓ Ro5	✓ Clean	`Cc1c([N+](=O)[O-])cc([N+](=O)[O-])cc1[N+](=O)[O…`
ZINC156796 ZINC	1.000	284.4 Da LogP 3.86 TPSA 34.1	✓ Ro5	✓ Clean	`C[C@]12C=CC(=O)C=C1CC[C@@H]1[C@@H]2CC[C@@]2(C)C…`
ZINC1683141 ZINC	1.000	314.5 Da LogP 4.72 TPSA 34.1	✓ Ro5	✓ Clean	`CC(=O)[C@@H]1CC[C@H]2[C@@H]3CCC4=CC(=O)CC[C@]4(…`
ZINC1883067 ZINC	1.000	229.1 Da LogP 1.12 TPSA 149.7	✓ Ro5	✓ Clean	`O=[N+]([O-])c1cc([N+](=O)[O-])c(O)c([N+](=O)[O-…`
ZINC2100022 ZINC	1.000	284.4 Da LogP 3.86 TPSA 34.1	✓ Ro5	✓ Clean	`C[C@]12C=CC(=O)C=C1CC[C@@H]1[C@@H]2CC[C@@]2(C)C…`
ZINC2159863 ZINC	1.000	314.5 Da LogP 4.72 TPSA 34.1	✓ Ro5	✓ Clean	`CC(=O)[C@@H]1CC[C@@H]2[C@@H]3CCC4=CC(=O)CC[C@]4…`
ZINC238924247 ZINC	1.000	314.5 Da LogP 4.72 TPSA 34.1	✓ Ro5	✓ Clean	`CC(=O)[C@H]1CC[C@@H]2[C@H]3CCC4=CC(=O)CC[C@]4(C…`
ZINC242548813 ZINC	1.000	284.4 Da LogP 3.86 TPSA 34.1	✓ Ro5	✓ Clean	`C[C@]12C=CC(=O)C=C1CC[C@H]1[C@H]2CC[C@]2(C)C(=O…`
ZINC242648889 ZINC	1.000	314.5 Da LogP 4.72 TPSA 34.1	✓ Ro5	✓ Clean	`CC(=O)[C@@H]1CC[C@@H]2[C@H]3CCC4=CC(=O)CC[C@]4(…`
ZINC253502176 ZINC	1.000	284.4 Da LogP 3.86 TPSA 34.1	✓ Ro5	✓ Clean	`C[C@]12CC[C@@H]3[C@H](CCC4=CC(=O)C=C[C@]43C)[C@…`
ZINC3132721 ZINC	1.000	314.5 Da LogP 4.72 TPSA 34.1	✓ Ro5	✓ Clean	`CC(=O)[C@H]1CC[C@@H]2[C@H]3CCC4=CC(=O)CC[C@]4(C…`
ZINC3874744 ZINC	1.000	314.5 Da LogP 4.72 TPSA 34.1	✓ Ro5	✓ Clean	`CC(=O)[C@@H]1CC[C@@H]2[C@H]3CCC4=CC(=O)CC[C@@]4…`
ZINC3881421 ZINC	1.000	284.4 Da LogP 3.86 TPSA 34.1	✓ Ro5	✓ Clean	`C[C@]12C=CC(=O)C=C1CC[C@@H]1[C@@H]2CC[C@]2(C)C(…`
ZINC4023563 ZINC	1.000	284.4 Da LogP 3.86 TPSA 34.1	✓ Ro5	✓ Clean	`C[C@]12CC[C@@H]3[C@@H](CCC4=CC(=O)C=C[C@@]43C)[…`
ZINC4023564 ZINC	1.000	284.4 Da LogP 3.86 TPSA 34.1	✓ Ro5	✓ Clean	`C[C@]12C=CC(=O)C=C1CC[C@@H]1[C@H]2CC[C@]2(C)C(=…`
ZINC4023565 ZINC	1.000	284.4 Da LogP 3.86 TPSA 34.1	✓ Ro5	✓ Clean	`C[C@]12C=CC(=O)C=C1CC[C@@H]1[C@@H]2CC[C@]2(C)C(…`
ZINC4081602 ZINC	1.000	314.5 Da LogP 4.72 TPSA 34.1	✓ Ro5	✓ Clean	`CC(=O)[C@H]1CC[C@H]2[C@@H]3CCC4=CC(=O)CC[C@]4(C…`
ZINC4081603 ZINC	1.000	314.5 Da LogP 4.72 TPSA 34.1	✓ Ro5	✓ Clean	`CC(=O)[C@H]1CC[C@@H]2[C@@H]3CCC4=CC(=O)CC[C@]4(…`
ZINC4428529 ZINC	1.000	314.5 Da LogP 4.72 TPSA 34.1	✓ Ro5	✓ Clean	`CC(=O)[C@H]1CC[C@H]2[C@@H]3CCC4=CC(=O)CC[C@]4(C…`
ZINC4534007 ZINC	1.000	284.4 Da LogP 3.86 TPSA 34.1	✓ Ro5	✓ Clean	`C[C@@]12C=CC(=O)C=C1CC[C@H]1[C@H]2CC[C@@]2(C)C(…`
ZINC5260762 ZINC	1.000	314.5 Da LogP 4.72 TPSA 34.1	✓ Ro5	✓ Clean	`CC(=O)[C@@H]1CC[C@@H]2[C@H]3CCC4=CC(=O)CC[C@@]4…`
ZINC58482279 ZINC	1.000	284.4 Da LogP 3.86 TPSA 34.1	✓ Ro5	✓ Clean	`C[C@]12C=CC(=O)C=C1CC[C@H]1[C@H]2CC[C@@]2(C)C(=…`
ZINC675050365 ZINC	1.000	314.5 Da LogP 4.72 TPSA 34.1	✓ Ro5	✓ Clean	`CC(=O)[C@@H]1CC[C@H]2[C@H]3CCC4=CC(=O)CC[C@]4(C…`
ZINC8580672 ZINC	1.000	314.5 Da LogP 4.72 TPSA 34.1	✓ Ro5	✓ Clean	`CC(=O)[C@@H]1CC[C@@H]2[C@H]3CCC4=CC(=O)CC[C@]4(…`
ZINC9212411 ZINC	1.000	314.5 Da LogP 4.72 TPSA 34.1	✓ Ro5	✓ Clean	`CC(=O)[C@H]1CC[C@H]2[C@H]3CCC4=CC(=O)CC[C@]4(C)…`
ZINC69592773 ZINC	0.843	344.4 Da LogP 2.29 TPSA 91.7	✓ Ro5	✓ Clean	`C[C@]12CC(=O)[C@H]3[C@H](CCC4=CC(=O)C=C[C@@]43C…`
ZINC69592779 ZINC	0.843	344.4 Da LogP 2.29 TPSA 91.7	✓ Ro5	✓ Clean	`C[C@]12CC(=O)[C@H]3[C@@H](CCC4=CC(=O)C=C[C@@]43…`
ZINC1857666496 ZINC	0.826	316.4 Da LogP 4.22 TPSA 54.4	✓ Ro5	✓ Clean	`C[C@]12CC[C@H]3[C@@H](CCC4=CC(=O)CC[C@@]43C)[C@…`
ZINC245224552 ZINC	0.826	316.4 Da LogP 4.22 TPSA 54.4	✓ Ro5	✓ Clean	`C[C@]12CC[C@@H]3[C@H](CCC4=CC(=O)CC[C@@]43C)[C@…`
ZINC253618173 ZINC	0.826	316.4 Da LogP 4.22 TPSA 54.4	✓ Ro5	✓ Clean	`C[C@]12CCC(=O)C=C1CC[C@H]1[C@H]2CC[C@@]2(C)[C@H…`
ZINC253618174 ZINC	0.826	316.4 Da LogP 4.22 TPSA 54.4	✓ Ro5	✓ Clean	`C[C@@]12CCC(=O)C=C1CC[C@H]1[C@H]2CC[C@]2(C)[C@H…`
ZINC253648944 ZINC	0.826	316.4 Da LogP 4.22 TPSA 54.4	✓ Ro5	✓ Clean	`C[C@]12CC[C@H]3[C@@H](CCC4=CC(=O)CC[C@@]43C)[C@…`
ZINC32911458 ZINC	0.826	316.4 Da LogP 4.22 TPSA 54.4	✓ Ro5	✓ Clean	`C[C@]12CC[C@H]3[C@@H](CCC4=CC(=O)CC[C@@]43C)[C@…`
ZINC3927796 ZINC	0.826	316.4 Da LogP 4.22 TPSA 54.4	✓ Ro5	✓ Clean	`C[C@]12CC[C@H]3[C@@H](CCC4=CC(=O)CC[C@@]43C)[C@…`
ZINC44830435 ZINC	0.826	316.4 Da LogP 4.22 TPSA 54.4	✓ Ro5	✓ Clean	`C[C@@]12CCC(=O)C=C1CC[C@H]1[C@H]2CC[C@@]2(C)[C@…`
ZINC4706032 ZINC	0.826	300.4 Da LogP 4.33 TPSA 34.1	✓ Ro5	✓ Clean	`CC(=O)[C@@H]1CC[C@H]2[C@H]3CCC4=CC(=O)C[C@@]4(C…`
ZINC4706033 ZINC	0.826	300.4 Da LogP 4.33 TPSA 34.1	✓ Ro5	✓ Clean	`CC(=O)[C@H]1CC[C@H]2[C@H]3CCC4=CC(=O)C[C@@]4(C)…`
ZINC4706034 ZINC	0.826	300.4 Da LogP 4.33 TPSA 34.1	✓ Ro5	✓ Clean	`CC(=O)[C@@H]1CC[C@@H]2[C@H]3CCC4=CC(=O)C[C@@]4(…`
ZINC4706035 ZINC	0.826	300.4 Da LogP 4.33 TPSA 34.1	✓ Ro5	✓ Clean	`CC(=O)[C@H]1CC[C@@H]2[C@H]3CCC4=CC(=O)C[C@@]4(C…`
ZINC1857667003 ZINC	0.792	330.5 Da LogP 4.31 TPSA 43.4	✓ Ro5	✓ Clean	`COC(=O)[C@@H]1CC[C@H]2[C@@H]3CCC4=CC(=O)CC[C@]4…`
ZINC2170217 ZINC	0.792	200.1 Da LogP 0.91 TPSA 126.7	✓ Ro5	Alert	`O=[N+]([O-])c1cc(O)c(O)c([N+](=O)[O-])c1`
ZINC21991584 ZINC	0.792	330.5 Da LogP 4.31 TPSA 43.4	✓ Ro5	✓ Clean	`COC(=O)[C@H]1CC[C@@H]2[C@H]3CCC4=CC(=O)CC[C@]4(…`
ZINC244882669 ZINC	0.792	330.5 Da LogP 4.31 TPSA 43.4	✓ Ro5	✓ Clean	`COC(=O)[C@@H]1CC[C@@H]2[C@H]3CCC4=CC(=O)CC[C@]4…`
ZINC253498633 ZINC	0.792	330.5 Da LogP 4.31 TPSA 43.4	✓ Ro5	✓ Clean	`COC(=O)[C@@H]1CC[C@@H]2[C@H]3CCC4=CC(=O)CC[C@@]…`
ZINC253618167 ZINC	0.792	330.5 Da LogP 4.31 TPSA 43.4	✓ Ro5	✓ Clean	`COC(=O)[C@H]1CC[C@@H]2[C@@H]3CCC4=CC(=O)CC[C@]4…`
ZINC253618168 ZINC	0.792	330.5 Da LogP 4.31 TPSA 43.4	✓ Ro5	✓ Clean	`COC(=O)[C@H]1CC[C@@H]2[C@H]3CCC4=CC(=O)CC[C@]4(…`
ZINC3927798 ZINC	0.792	330.5 Da LogP 4.31 TPSA 43.4	✓ Ro5	✓ Clean	`COC(=O)[C@H]1CC[C@H]2[C@@H]3CCC4=CC(=O)CC[C@]4(…`
ZINC68564159 ZINC	0.792	366.2 Da LogP 2.40 TPSA 213.0	✓ Ro5	✓ Clean	`O=[N+]([O-])c1cc(-c2cc([N+](=O)[O-])cc([N+](=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.

Cross-references

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

Sequence

UniProt A0A0H3GQS4

Structure

PDB 7TMB