KpKP13 Protein target profile

Succinate dehydrogenase cytochrome b556 subunit

Accession: KP13_03281

Gene: sdhC AHE45660.1 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0V9SNE0

Export view

Length 134

Pocket druggability (P2Rank · AlphaFold DB model) 0.068

Direct ligand evidence 0 61 total records

Functional annotation 0 EC 9 GO

Target summary

Target candidate with partial support; inspect missing evidence before prioritizing.

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

Main supporting evidence

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: No hit
Gut microbiome similarity: 2.3% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 64.567 Higher values support similarity to known essential genes.
DEG E-value: 2.31e-51 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 95.01 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

AlphaFold DB / UniProt model

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) 0.068

Structure A0A0V9SNE0

Pocket Pocket 1

Druggability (FPocket) 0.676

Structure A0A0V9SNE0

Pocket Pocket 1

ColabFold model

P2Rank 0.105 · Pocket 1

FPocket 0.687 · Pocket 1

Core conservation Accessory gene

Roary core

CoreCruncher accessory

Gut microbiome 107 / 4744 genomes with a hit

Prevalence 2.3%

Sequence

Primary amino-acid sequence viewer.

MWALFMVRNVKKQRPVNLDLQTIRFPITAIASILHRVSGVITFVAVGILLWLLGTSLSSPEGFLTAASIMDSFFVKFIMWGILTALAYHVVVGIRHLMMDFGYLDETLEAGKRSAKISFVITVVLSLLAGVLVW

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

9 GO

Subcellular localization

Localization: CytoplasmicMembrane

Gene Ontology (GO)

GO:0009055 A molecular function representing the directed movement of electrons from one molecular entity to another, typically mediated by electron carriers or acceptors, resulting in the transfer of energy and/or the reduction-oxidation (redox) transformation of chemical species. This activity is fundamental to various biological processes, including cellular respiration and photosynthesis, as well as numerous enzymatic reactions involved in metabolic pathways.
GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
GO:0016627 Catalysis of an oxidation-reduction (redox) reaction in which a CH-CH group acts as a hydrogen or electron donor and reduces a hydrogen or electron acceptor.
GO:0045281 OBSOLETE. A multimeric complex which consists of flavoprotein (subunit A ; InterPro:IPR003952), iron-sulfur protein (subunit B) and membrane-bound cytochrome b560 (subunit C; InterPro:IPR000701). In some Archaea, the membrane-bound subunits (C or C and D) do not necessarily contain heme. Membrane-bound subunits can bind or react with quinones.
GO:0006099 A nearly universal metabolic pathway in which the acetyl group of acetyl coenzyme A is effectively oxidized to two CO2 and four pairs of electrons are transferred to coenzymes. The acetyl group combines with oxaloacetate to form citrate, which undergoes successive transformations to isocitrate, 2-oxoglutarate, succinyl-CoA, succinate, fumarate, malate, and oxaloacetate again, thus completing the cycle. In eukaryotes the tricarboxylic acid is confined to the mitochondria. See also glyoxylate cycle.
GO:0000104 Catalysis of the reaction: succinate + acceptor = fumarate + reduced acceptor.
GO:0005886 The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
GO:0046872 Binding to a metal ion.
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.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

28 records

Show feature table

Start	End	DB	Term	Name
12	131	NCBIfam	TIGR02970	succinate dehydrogenase, cytochrome b556 subunit
12	131	InterPro	IPR014314	Succinate dehydrogenase, cytochrome b556 subunit
14	131	CDD	cd03499	SQR_TypeC_SdhC
14	131	InterPro	IPR014314	Succinate dehydrogenase, cytochrome b556 subunit
14	38	ProSitePatterns	PS01000	Succinate dehydrogenase cytochrome b subunit signature 1.
14	38	InterPro	IPR018495	Succinate dehydrogenase, cytochrome b subunit, conserved site
33	55	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
33	53	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
77	94	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
114	133	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
11	128	Pfam	PF01127	Succinate dehydrogenase/Fumarate reductase transmembrane subunit
11	128	InterPro	IPR000701	Succinate dehydrogenase/fumarate reductase type B, transmembrane subunit
1	134	PIRSF	PIRSF000178	SDH_cyt_b560
1	134	InterPro	IPR014314	Succinate dehydrogenase, cytochrome b556 subunit
6	134	Gene3D	G3DSA:1.20.1300.10	Fumarate reductase/succinate dehydrogenase, transmembrane subunit
6	134	InterPro	IPR034804	Fumarate reductase/succinate dehydrogenase, transmembrane subunit
6	134	FunFam	G3DSA:1.20.1300.10:FF:000005	Succinate dehydrogenase cytochrome b556 subunit
134	134	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
95	114	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
89	102	ProSitePatterns	PS01001	Succinate dehydrogenase cytochrome b subunit signature 2.
89	102	InterPro	IPR018495	Succinate dehydrogenase, cytochrome b subunit, conserved site
6	134	SUPERFAMILY	SSF81343	Fumarate reductase respiratory complex transmembrane subunits
73	94	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
7	129	PANTHER	PTHR10978	SUCCINATE DEHYDROGENASE CYTOCHROME B560 SUBUNIT
7	129	InterPro	IPR014314	Succinate dehydrogenase, cytochrome b556 subunit
115	133	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
1	32	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
54	72	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.

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

0.068

Show in viewer

Surrounding area

Pocket 2 P2Rank #2

0.052

Show in viewer

Surrounding area

Pocket 3 P2Rank #3

0.027

Show in viewer

Surrounding area

Pocket 4 P2Rank #4

0.026

Show in viewer

Surrounding area

Pocket 5 P2Rank #5

0.021

Show in viewer

Surrounding area

Binding pockets · FPocket

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

Pocket 1 FPocket #1

0.676

Show in viewer

Surrounding area

Pocket 2 FPocket #3

0.395

Show in viewer

Surrounding area

Pocket 3 FPocket #4

0.299

Show in viewer

Surrounding area

Binding pockets · P2Rank

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

Pocket 1 P2Rank #1

0.105

Show in viewer

Surrounding area

Pocket 2 P2Rank #2

0.069

Show in viewer

Surrounding area

Pocket 3 P2Rank #3

0.064

Show in viewer

Surrounding area

Pocket 4 P2Rank #4

0.059

Show in viewer

Surrounding area

Pocket 5 P2Rank #5

0.022

Show in viewer

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_A0A0V9SNE0	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_03281	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

AT5 PDB via homolog 366.2 Da · LogP 2.79 · TPSA 88.6 Open detail RCSB PDB

CBE PDB via homolog Detail RCSB PDB

CDN PDB via homolog Detail RCSB PDB

DNT PDB via homolog Detail RCSB PDB

EPH 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
AT5 RCSB PDB	2ACZ	P69054	366.2 Da LogP 2.79 TPSA 88.6	✓ Ro5	✓ Clean	`C[C@@H](C[C@H](C)C(=O)C1=C(C(=C(NC1=O)OC)OC)O)[…`
CBE RCSB PDB	2WDQ	P69054	235.3 Da LogP 2.62 TPSA 38.3	✓ Ro5	✓ Clean	`CC1=C(SCCO1)C(=O)Nc2ccccc2`
CDN RCSB PDB	1NEK	P69054	1151.5 Da LogP 14.77 TPSA 249.6	4 viol.	✓ Clean	`CCCCCCCCCCCCCCC(O)O[C@H](COC(CCCCC)O)CO[P@@](=O…`
DNT RCSB PDB	1NEN	P69054	282.3 Da LogP 3.89 TPSA 106.5	✓ Ro5	✓ Clean	`CCCCCC(C)c1cc(cc(c1O)[N+](=O)[O-])[N+](=O)[O-]`
EPH RCSB PDB	1NEK	P69054	709.9 Da LogP 10.16 TPSA 134.4	2 viol.	✓ Clean	`CCCC=CCC=CCCCCCCCC(=O)O[C@H](COC(=O)CCCCCCC=CCC…`
F3S RCSB PDB	1NEK	P69054	295.8 Da LogP 2.59 TPSA 0.0	✓ Ro5	✓ Clean	`S1[Fe]2S[Fe]3[S]2[Fe]1S3`
FES RCSB PDB	1NEK	P69054	175.8 Da LogP 1.29 TPSA 0.0	✓ Ro5	✓ Clean	`S1[Fe]S[Fe]1`
OAA RCSB PDB	1NEK	P69054	131.1 Da LogP -2.22 TPSA 94.5	✓ Ro5	✓ Clean	`C(C(=O)C(=O)O)C(=O)[O-]`
PCI RCSB PDB	2WDR	P69054	266.3 Da LogP 4.66 TPSA 20.2	✓ Ro5	✓ Clean	`c1(c(c(c(c(c1Cl)Cl)Cl)Cl)Cl)O`
TEO RCSB PDB	2WDQ	P69054	132.1 Da LogP -3.14 TPSA 103.7	✓ Ro5	✓ Clean	`C(=C(\O)/[O-])\[C@H](C(=O)[O-])O`
UQ2 RCSB PDB	1NEK	P69054	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`

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
ZINC1529471 ZINC	1.000	266.3 Da LogP 4.66 TPSA 20.2	✓ Ro5	✓ Clean	`Oc1c(Cl)c(Cl)c(Cl)c(Cl)c1Cl`
ZINC1532641 ZINC	1.000	318.4 Da LogP 4.04 TPSA 52.6	✓ Ro5	Alert	`COC1=C(OC)C(=O)C(C/C=C(\C)CCC=C(C)C)=C(C)C1=O`
ZINC43478 ZINC	1.000	235.3 Da LogP 2.62 TPSA 38.3	✓ Ro5	✓ Clean	`CC1=C(C(=O)Nc2ccccc2)SCCO1`
ZINC33649281 ZINC	0.974	296.3 Da LogP 4.28 TPSA 106.5	✓ Ro5	✓ Clean	`CCCCCC[C@@H](C)c1cc([N+](=O)[O-])cc([N+](=O)[O-…`
ZINC33649283 ZINC	0.974	296.3 Da LogP 4.28 TPSA 106.5	✓ Ro5	✓ Clean	`CCCCCC[C@H](C)c1cc([N+](=O)[O-])cc([N+](=O)[O-]…`
ZINC225408 ZINC	0.900	247.9 Da LogP 3.71 TPSA 40.5	✓ Ro5	✓ Clean	`Oc1c(Cl)c(Cl)c(O)c(Cl)c1Cl`
ZINC1583639 ZINC	0.821	254.2 Da LogP 3.11 TPSA 106.5	✓ Ro5	✓ Clean	`CCC[C@@H](C)c1cc([N+](=O)[O-])cc([N+](=O)[O-])c…`
ZINC2038099 ZINC	0.821	254.2 Da LogP 3.11 TPSA 106.5	✓ Ro5	✓ Clean	`CCC[C@H](C)c1cc([N+](=O)[O-])cc([N+](=O)[O-])c1O`
ZINC154748 ZINC	0.818	247.9 Da LogP 3.71 TPSA 40.5	✓ Ro5	Alert	`Oc1c(O)c(Cl)c(Cl)c(Cl)c1Cl`
ZINC1559692 ZINC	0.750	250.3 Da LogP 2.32 TPSA 52.6	✓ Ro5	Alert	`COC1=C(OC)C(=O)C(CC=C(C)C)=C(C)C1=O`
ZINC13828017 ZINC	0.725	240.2 Da LogP 2.72 TPSA 106.5	✓ Ro5	✓ Clean	`CC[C@@H](C)c1cc([N+](=O)[O-])cc([N+](=O)[O-])c1O`
ZINC13828020 ZINC	0.725	240.2 Da LogP 2.72 TPSA 106.5	✓ Ro5	✓ Clean	`CC[C@H](C)c1cc([N+](=O)[O-])cc([N+](=O)[O-])c1O`
ZINC102190506 ZINC	0.696	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	0.696	467.5 Da LogP 4.25 TPSA 134.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@@H](CO[P@@](=O)(O)OCCN)OC(=O)C…`
ZINC27416437 ZINC	0.679	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	0.679	411.4 Da LogP 2.69 TPSA 134.4	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@@H](CO[P@@](=O)(O)OCCN)OC(=O)CCC…`
ZINC2513914 ZINC	0.675	235.3 Da LogP 2.62 TPSA 38.3	✓ Ro5	✓ Clean	`CC1=C(C(=O)Nc2ccccc2)OCCS1`
ZINC32918592 ZINC	0.652	307.4 Da LogP 2.80 TPSA 64.6	✓ Ro5	✓ Clean	`CCOC(=O)c1ccc(NC(=O)C2=C(C)OCCS2)cc1`
ZINC1687159 ZINC	0.625	226.2 Da LogP 2.33 TPSA 106.5	✓ Ro5	✓ Clean	`CC(C)c1cc([N+](=O)[O-])cc([N+](=O)[O-])c1O`
ZINC9115226 ZINC	0.625	360.5 Da LogP 3.64 TPSA 58.6	✓ Ro5	✓ Clean	`CC1=C(C(=O)Nc2ccc(C(=O)N3CCCCCC3)cc2)SCCO1`
ZINC1501016364 ZINC	0.623	465.6 Da LogP 4.63 TPSA 128.3	✓ Ro5	✓ Clean	`CCCCCC/C=C\CCCCCCCCC(=O)OC[C@@H](O)CO[P@](=O)(O…`
ZINC20919537 ZINC	0.612	388.5 Da LogP 4.46 TPSA 67.4	✓ Ro5	✓ Clean	`CC1=C(C(=O)Nc2ccc(C(=O)NC3CCCCCCC3)cc2)SCCO1`
ZINC9115252 ZINC	0.612	374.5 Da LogP 4.07 TPSA 67.4	✓ Ro5	✓ Clean	`CC1=C(C(=O)Nc2ccc(C(=O)NC3CCCCCC3)cc2)SCCO1`
ZINC9115309 ZINC	0.612	360.5 Da LogP 3.68 TPSA 67.4	✓ Ro5	✓ Clean	`CC1=C(C(=O)Nc2ccc(C(=O)NC3CCCCC3)cc2)SCCO1`
ZINC6895037 ZINC	0.604	382.5 Da LogP 3.86 TPSA 67.4	✓ Ro5	✓ Clean	`CC1=C(C(=O)Nc2cccc(C(=O)NCc3ccccc3C)c2)SCCO1`
ZINC12323380 ZINC	0.595	297.4 Da LogP 3.76 TPSA 38.3	✓ Ro5	✓ Clean	`O=C(Nc1ccccc1)C1=C(c2ccccc2)SCCO1`
ZINC6895073 ZINC	0.588	374.5 Da LogP 3.57 TPSA 58.6	✓ Ro5	✓ Clean	`CC1=C(C(=O)Nc2ccc(CC(=O)N3CCCCCC3)cc2)SCCO1`
ZINC28404190 ZINC	0.565	311.4 Da LogP 4.07 TPSA 38.3	✓ Ro5	✓ Clean	`Cc1ccc(NC(=O)C2=C(c3ccccc3)SCCO2)cc1`
ZINC98180109 ZINC	0.563	246.9 Da LogP 3.59 TPSA 46.2	✓ Ro5	✓ Clean	`Nc1c(O)c(Cl)c(Cl)c(Cl)c1Cl`
ZINC1492540 ZINC	0.558	355.8 Da LogP 3.84 TPSA 64.6	✓ Ro5	✓ Clean	`CC1=C(C(=O)Nc2ccc(Cl)c(C(=O)OC(C)C)c2)SCCO1`
ZINC13544781 ZINC	0.556	482.6 Da LogP 4.22 TPSA 108.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)OC[C@@H](CO[P@](=O)(O)OCC[N+](C)(C)C…`
ZINC13544783 ZINC	0.556	482.6 Da LogP 4.22 TPSA 108.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)OC[C@H](CO[P@](=O)(O)OCC[N+](C)(C)C)…`
ZINC12322718 ZINC	0.543	354.4 Da LogP 3.72 TPSA 67.4	✓ Ro5	✓ Clean	`CC(=O)Nc1ccc(NC(=O)C2=C(c3ccccc3)SCCO2)cc1`
ZINC13543439 ZINC	0.540	454.5 Da LogP 3.44 TPSA 108.4	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@@H](CO[P@](=O)(O)OCC[N+](C)(C)C)…`
ZINC13543441 ZINC	0.540	454.5 Da LogP 3.44 TPSA 108.4	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@H](CO[P@](=O)(O)OCC[N+](C)(C)C)O…`
ZINC6894966 ZINC	0.537	374.5 Da LogP 3.61 TPSA 67.4	✓ Ro5	✓ Clean	`CC1=C(C(=O)Nc2ccccc2C(=O)NCc2cccs2)SCCO1`
ZINC9115097 ZINC	0.537	369.4 Da LogP 2.95 TPSA 80.3	✓ Ro5	✓ Clean	`CC1=C(C(=O)Nc2ccccc2C(=O)NCc2ccccn2)SCCO1`
ZINC129184 ZINC	0.533	267.3 Da LogP 1.30 TPSA 72.5	✓ Ro5	✓ Clean	`CC1=C(C(=O)Nc2ccccc2)S(=O)(=O)CCO1`
ZINC102190945 ZINC	0.525	411.5 Da LogP 3.29 TPSA 128.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCCC(=O)OC[C@@H](O)CO[P@@](=O)(O)OCCN`
ZINC32840692 ZINC	0.525	425.5 Da LogP 3.68 TPSA 128.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC(=O)OC[C@@H](O)CO[P@](=O)(O)OCCN`
ZINC32840693 ZINC	0.525	425.5 Da LogP 3.68 TPSA 128.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC(=O)OC[C@H](O)CO[P@](=O)(O)OCCN`
ZINC32840704 ZINC	0.525	453.6 Da LogP 4.46 TPSA 128.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OC[C@@H](O)CO[P@](=O)(O)OCCN`
ZINC32840705 ZINC	0.525	453.6 Da LogP 4.46 TPSA 128.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OC[C@H](O)CO[P@](=O)(O)OCCN`
ZINC95635984 ZINC	0.525	397.4 Da LogP 2.90 TPSA 128.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCC(=O)OC[C@@H](O)CO[P@@](=O)(O)OCCN`
ZINC102191119 ZINC	0.524	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…`
ZINC33822387 ZINC	0.524	426.5 Da LogP 2.66 TPSA 108.4	✓ Ro5	✓ Clean	`CCCCC(=O)OC[C@H](CO[P@@](=O)(O)OCC[N+](C)(C)C)O…`
ZINC33822389 ZINC	0.524	426.5 Da LogP 2.66 TPSA 108.4	✓ Ro5	✓ Clean	`CCCCC(=O)OC[C@@H](CO[P@@](=O)(O)OCC[N+](C)(C)C)…`
ZINC58649551 ZINC	0.524	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)…`
ZINC5956205 ZINC	0.524	212.2 Da LogP 1.77 TPSA 106.5	✓ Ro5	✓ Clean	`CCc1cc([N+](=O)[O-])cc([N+](=O)[O-])c1O`
ZINC2046309 ZINC	0.523	254.2 Da LogP 3.11 TPSA 106.5	✓ Ro5	✓ Clean	`CCC[C@H](C)c1cc([N+](=O)[O-])c(O)c([N+](=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.

Cross-references

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

Sequence

UniProt A0A0V9SNE0