KpKP13 Protein target profile

Autoinducer 2-binding protein lsrB

Accession: KP13_02857

Gene: lsrB AHE42574.1 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GTJ1

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Length 333

Pocket druggability (P2Rank · AlphaFold DB model) 0.109

Direct ligand evidence 0 53 total records

Functional annotation 0 EC 4 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

Microbiome similarity 59 of 4744 screened genomes (1.2%) have a significant similarity hit. Weak predicted binding pocket FPocket selected-pocket score 0.37. Weak second pocket-predictor signal P2Rank predicted binding-site probability 0.11.

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: 1.2% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): N
DEG identity (%): 0.0 Higher values support similarity to known essential genes.

Structure confidence

ColabFold pLDDT: 95.37 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) 0.109

Structure A0A0H3GTJ1

Pocket Pocket 1

Druggability (FPocket) 0.369

Structure A0A0H3GTJ1

Pocket Pocket 2

ColabFold model

P2Rank 0.317 · Pocket 1

FPocket 0.544 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 59 / 4744 genomes with a hit

Prevalence 1.2%

Sequence

Primary amino-acid sequence viewer.

MKLKLIVLALAMSVVTAQAADRIAFIPKLVGVGFFTSGGNGAKEAGKALGVDVTYDGPTEPSVSGQVQLINNFVNQGYNAIIVSAVSPDGLCPALKRAMQRGVKVLTWDSDTKPECRSIYINQGTPQQLGGLLVEMAEKQVSKPAAKVAFFYSSPTVTDQNQWVKEAKAKIEKEHPQWQIVTTQFGYNDATKSLQTAEGILKAYPDLDAIIAPDANALPAAAQAAENLKRQGVAIVGFSTPNVMRPYVERGTVKAFGLWDVVQQGKIAVNVADRLLKKGDLNVGDSVEVKDIGSLKVEPNSVQGYQYEAKGNGIVLLPERVVFSKENINNYDF

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

4 GO

Subcellular localization

Localization: Periplasmic

Gene Ontology (GO)

GO:0043190 A complex for the transport of metabolites into and out of the cell, typically comprised of four domains; two membrane-associated domains and two ATP-binding domains at the intracellular face of the membrane, that form a central pore through the plasma membrane. Each of the four core domains may be encoded as a separate polypeptide or the domains can be fused in any one of a number of ways into multidomain polypeptides. In Bacteria and Archaebacteria, ABC transporters also include substrate binding proteins to bind substrate external to the cytoplasm and deliver it to the transporter.
GO:0030288 The region between the inner (cytoplasmic or plasma) membrane and outer membrane of organisms with two membranes such as Gram negative bacteria. These periplasmic spaces are relatively thick and contain a thin peptidoglycan layer (PGL), also referred to as a thin cell wall.
GO:0030246 Binding to a carbohydrate, which includes monosaccharides, oligosaccharides and polysaccharides as well as substances derived from monosaccharides by reduction of the carbonyl group (alditols), by oxidation of one or more hydroxy groups to afford the corresponding aldehydes, ketones, or carboxylic acids, or by replacement of one or more hydroxy group(s) by a hydrogen atom. Cyclitols are generally not regarded as carbohydrates.
GO:0055085 The process in which a solute is transported across a lipid bilayer, from one side of a membrane to the other.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

16 records

Show feature table

Start	End	DB	Term	Name
22	329	CDD	cd20003	PBP1_LsrB_Quorum_Sensing
22	329	InterPro	IPR030159	Autoinducer 2 ABC transporter, substrate-binding protein LsrB
22	317	Gene3D	G3DSA:3.40.50.2300	-
5	332	PANTHER	PTHR30036	D-XYLOSE-BINDING PERIPLASMIC PROTEIN
1	19	SignalP_EUK	SignalP-noTM	SignalP-noTM
123	333	Gene3D	G3DSA:3.40.50.2300	-
16	19	Phobius	SIGNAL_PEPTIDE_C_REGION	C-terminal region of a signal peptide.
5	15	Phobius	SIGNAL_PEPTIDE_H_REGION	Hydrophobic region of a signal peptide.
23	278	Pfam	PF13407	Periplasmic binding protein domain
23	278	InterPro	IPR025997	Periplasmic binding protein
21	333	SUPERFAMILY	SSF53822	Periplasmic binding protein-like I
21	333	InterPro	IPR028082	Periplasmic binding protein-like I
20	333	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
1	19	Phobius	SIGNAL_PEPTIDE	Signal peptide region
1	19	SignalP_GRAM_POSITIVE	SignalP-TM	SignalP-TM
1	4	Phobius	SIGNAL_PEPTIDE_N_REGION	N-terminal region of a signal peptide.

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 · P2Rank

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

Pocket 1 P2Rank #1

0.109

Likely same site as FPocket 2 0.5 Å 14 shared residues 100% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.024

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Surrounding area

Pocket 3 P2Rank #3

0.011

Likely same site as FPocket 1 2.1 Å 8 shared residues 100% of smaller site

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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 #2

0.369

Likely same site as P2Rank 1 0.5 Å 14 shared residues 100% of smaller site

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Surrounding area

Pocket 2 FPocket #1

0.225 Unusual size

Likely same site as P2Rank 3 2.1 Å 8 shared residues 100% of smaller site

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_A0A0H3GTJ1	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_02857	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.

53 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 3 records from similar proteins

Structural ligands 3 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

PAV PDB via homolog 150.1 Da · LogP -2.23 · TPSA 90.2 Open detail RCSB PDB

RIP PDB via homolog Detail RCSB PDB

TLZ PDB via homolog Detail RCSB PDB

ZINC100055463 ZINC proposed compound · Tanimoto 0.917 Detail ZINC

ZINC100064885 ZINC proposed compound · Tanimoto 0.917 Detail ZINC

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
PAV RCSB PDB	4PZ0	A0A6H3AKG3	150.1 Da LogP -2.23 TPSA 90.2	✓ Ro5	✓ Clean	`C[C@@]1(C([C@H](CO1)O)(O)O)O`
RIP RCSB PDB	7E7M	Q8E283	150.1 Da LogP -2.58 TPSA 90.2	✓ Ro5	✓ Clean	`C1[C@H]([C@H]([C@H]([C@@H](O1)O)O)O)O`
TLZ RCSB PDB	4RY9	A1WJM2	182.2 Da LogP -3.59 TPSA 121.4	1 viol.	✓ Clean	`C([C@H]([C@H]([C@H]([C@@H](CO)O)O)O)O)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
ZINC100055463 ZINC	0.917	212.2 Da LogP -4.22 TPSA 141.6	1 viol.	✓ Clean	`OC[C@H](O)[C@@H](O)[C@H](O)[C@H](O)[C@H](O)CO`
ZINC100064885 ZINC	0.917	212.2 Da LogP -4.22 TPSA 141.6	1 viol.	✓ Clean	`OC[C@H](O)[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)CO`
ZINC17780060 ZINC	0.917	212.2 Da LogP -4.22 TPSA 141.6	1 viol.	✓ Clean	`OC[C@@H](O)[C@H](O)C(O)[C@H](O)[C@H](O)CO`
ZINC17952732 ZINC	0.917	212.2 Da LogP -4.22 TPSA 141.6	1 viol.	✓ Clean	`OC[C@H](O)[C@@H](O)C(O)[C@H](O)[C@H](O)CO`
ZINC18042331 ZINC	0.917	242.2 Da LogP -4.86 TPSA 161.8	1 viol.	✓ Clean	`OC[C@H](O)[C@H](O)[C@H](O)[C@H](O)[C@H](O)[C@H]…`
ZINC18120313 ZINC	0.917	212.2 Da LogP -4.22 TPSA 141.6	1 viol.	✓ Clean	`OC[C@H](O)[C@H](O)C(O)[C@H](O)[C@H](O)CO`
ZINC3979006 ZINC	0.917	212.2 Da LogP -4.22 TPSA 141.6	1 viol.	✓ Clean	`OC[C@@H](O)[C@@H](O)C(O)[C@H](O)[C@H](O)CO`
ZINC4403103 ZINC	0.917	242.2 Da LogP -4.86 TPSA 161.8	1 viol.	✓ Clean	`OC[C@@H](O)[C@H](O)[C@H](O)[C@H](O)[C@H](O)[C@H…`
ZINC4403105 ZINC	0.917	242.2 Da LogP -4.86 TPSA 161.8	1 viol.	✓ Clean	`OC[C@H](O)[C@@H](O)[C@H](O)[C@H](O)[C@H](O)[C@H…`
ZINC4403107 ZINC	0.917	242.2 Da LogP -4.86 TPSA 161.8	1 viol.	✓ Clean	`OC[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)[C@H](O)[C@…`
ZINC9212412 ZINC	0.917	212.2 Da LogP -4.22 TPSA 141.6	1 viol.	✓ Clean	`OC[C@H](O)[C@@H](O)C(O)[C@H](O)[C@@H](O)CO`
ZINC5201837 ZINC	0.647	345.3 Da LogP -6.55 TPSA 214.3	2 viol.	✓ Clean	`OC[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O)CNC[C@H](…`
ZINC5201838 ZINC	0.647	345.3 Da LogP -6.55 TPSA 214.3	2 viol.	✓ Clean	`OC[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O)CNC[C@@H]…`
ZINC5201839 ZINC	0.647	345.3 Da LogP -6.55 TPSA 214.3	2 viol.	✓ Clean	`OC[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O)CNC[C@H](…`
ZINC5201841 ZINC	0.647	345.3 Da LogP -6.55 TPSA 214.3	2 viol.	✓ Clean	`OC[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O)CNC[C@@H]…`
ZINC101356848 ZINC	0.579	388.4 Da LogP -6.96 TPSA 226.4	2 viol.	✓ Clean	`OC[C@H](O)[C@H](O)[C@H](O)[C@H](O)CNCCNC[C@H](O…`
ZINC215968865 ZINC	0.579	388.4 Da LogP -6.96 TPSA 226.4	2 viol.	✓ Clean	`OC[C@H](O)[C@H](O)[C@H](O)[C@H](O)CNCCNC[C@H](O…`
ZINC215968917 ZINC	0.579	388.4 Da LogP -6.96 TPSA 226.4	2 viol.	✓ Clean	`OC[C@H](O)[C@H](O)[C@H](O)[C@H](O)CNCCNC[C@H](O…`
ZINC215968963 ZINC	0.579	388.4 Da LogP -6.96 TPSA 226.4	2 viol.	✓ Clean	`OC[C@H](O)[C@H](O)[C@@H](O)[C@@H](O)CNCCNC[C@@H…`
ZINC216185927 ZINC	0.579	209.2 Da LogP -3.02 TPSA 104.4	✓ Ro5	✓ Clean	`CN(C)C[C@H](O)[C@H](O)[C@H](O)[C@@H](O)CO`
ZINC216185976 ZINC	0.579	209.2 Da LogP -3.02 TPSA 104.4	✓ Ro5	✓ Clean	`CN(C)C[C@H](O)[C@H](O)[C@@H](O)[C@H](O)CO`
ZINC216186168 ZINC	0.579	224.3 Da LogP -2.87 TPSA 101.2	✓ Ro5	✓ Clean	`C[N+](C)(C)C[C@H](O)[C@H](O)[C@H](O)[C@@H](O)CO`
ZINC216186206 ZINC	0.579	224.3 Da LogP -2.87 TPSA 101.2	✓ Ro5	✓ Clean	`C[N+](C)(C)C[C@H](O)[C@H](O)[C@@H](O)[C@H](O)CO`
ZINC25624721 ZINC	0.579	209.2 Da LogP -3.02 TPSA 104.4	✓ Ro5	✓ Clean	`CN(C)C[C@H](O)[C@H](O)[C@@H](O)[C@@H](O)CO`
ZINC25624980 ZINC	0.579	224.3 Da LogP -2.87 TPSA 101.2	✓ Ro5	✓ Clean	`C[N+](C)(C)C[C@H](O)[C@H](O)[C@@H](O)[C@@H](O)CO`
ZINC4566610 ZINC	0.579	209.2 Da LogP -3.02 TPSA 104.4	✓ Ro5	✓ Clean	`CN(C)C[C@H](O)[C@H](O)[C@H](O)[C@H](O)CO`
ZINC4566614 ZINC	0.579	224.3 Da LogP -2.87 TPSA 101.2	✓ Ro5	✓ Clean	`C[N+](C)(C)C[C@H](O)[C@H](O)[C@H](O)[C@H](O)CO`
ZINC255980408 ZINC	0.577	414.4 Da LogP -5.66 TPSA 208.0	2 viol.	✓ Clean	`O[C@H]1OC[C@@H](O[C@H]2OC[C@@H](O[C@H]3OC[C@@H]…`
ZINC255980409 ZINC	0.577	414.4 Da LogP -5.66 TPSA 208.0	2 viol.	✓ Clean	`O[C@H]1OC[C@@H](O[C@H]2OC[C@@H](O[C@H]3OC[C@@H]…`
ZINC255980410 ZINC	0.577	414.4 Da LogP -5.66 TPSA 208.0	2 viol.	✓ Clean	`O[C@@H]1[C@H](O)[C@@H](O[C@@H]2CO[C@H](O[C@@H]3…`
ZINC255980411 ZINC	0.577	414.4 Da LogP -5.66 TPSA 208.0	2 viol.	✓ Clean	`O[C@H]1OC[C@@H](O[C@H]2OC[C@@H](O[C@H]3OC[C@@H]…`
ZINC263584059 ZINC	0.577	414.4 Da LogP -5.66 TPSA 208.0	2 viol.	✓ Clean	`O[C@@H]1[C@@H](O[C@@H]2OC[C@@H](O)[C@H](O)[C@H]…`
ZINC263584060 ZINC	0.577	414.4 Da LogP -5.66 TPSA 208.0	2 viol.	✓ Clean	`O[C@H]1[C@H](O)[C@@H](O[C@@H]2CO[C@@H](O)[C@H](…`
ZINC263584061 ZINC	0.577	414.4 Da LogP -5.66 TPSA 208.0	2 viol.	✓ Clean	`O[C@@H]1[C@@H](O[C@H]2OC[C@@H](O)[C@H](O)[C@H]2…`
ZINC4095690 ZINC	0.577	282.2 Da LogP -4.12 TPSA 149.1	1 viol.	✓ Clean	`O[C@H]1[C@H](O)CO[C@@H](O[C@@H]2CO[C@H](O)[C@H]…`
ZINC4095691 ZINC	0.577	282.2 Da LogP -4.12 TPSA 149.1	1 viol.	✓ Clean	`O[C@H]1[C@H](O)CO[C@@H](O[C@@H]2CO[C@@H](O)[C@H…`
ZINC64622127 ZINC	0.577	414.4 Da LogP -5.66 TPSA 208.0	2 viol.	✓ Clean	`O[C@H]1[C@H](O)CO[C@@H](O[C@@H]2CO[C@@H](O[C@@H…`
ZINC78590548 ZINC	0.577	414.4 Da LogP -5.66 TPSA 208.0	2 viol.	✓ Clean	`O[C@H]1[C@H](O)CO[C@@H](O[C@@H]2CO[C@@H](O[C@@H…`
ZINC85546060 ZINC	0.577	414.4 Da LogP -5.66 TPSA 208.0	2 viol.	✓ Clean	`O[C@H]1[C@H](O)[C@@H](O[C@@H]2CO[C@@H](O)[C@H](…`
ZINC100036265 ZINC	0.550	210.2 Da LogP -4.02 TPSA 138.5	1 viol.	✓ Clean	`O=C(CO)[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)CO`
ZINC11592820 ZINC	0.550	226.2 Da LogP -4.13 TPSA 158.7	1 viol.	✓ Clean	`O=C(O)[C@H](O)[C@H](O)[C@H](O)[C@H](O)[C@@H](O)…`
ZINC12953159 ZINC	0.550	210.2 Da LogP -4.02 TPSA 138.5	1 viol.	✓ Clean	`O=C[C@H](O)[C@H](O)[C@H](O)[C@H](O)[C@@H](O)CO`
ZINC12953168 ZINC	0.550	210.2 Da LogP -4.02 TPSA 138.5	1 viol.	✓ Clean	`O=C[C@H](O)[C@H](O)[C@H](O)[C@@H](O)[C@@H](O)CO`
ZINC3843093 ZINC	0.550	256.4 Da LogP -0.11 TPSA 80.9	✓ Ro5	✓ Clean	`CCSC(SCC)[C@@H](O)[C@H](O)[C@H](O)CO`
ZINC4353167 ZINC	0.550	240.2 Da LogP -4.66 TPSA 158.7	1 viol.	✓ Clean	`O=C[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O…`
ZINC4353168 ZINC	0.550	240.2 Da LogP -4.66 TPSA 158.7	1 viol.	✓ Clean	`O=C[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O)[C@H](O)…`
ZINC4403706 ZINC	0.550	256.2 Da LogP -4.77 TPSA 178.9	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O)[C@@H…`
ZINC4403707 ZINC	0.550	256.2 Da LogP -4.77 TPSA 178.9	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O)[C@@H…`
ZINC4403708 ZINC	0.550	256.2 Da LogP -4.77 TPSA 178.9	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O)[C@H]…`
ZINC4691944 ZINC	0.550	256.4 Da LogP -0.11 TPSA 80.9	✓ Ro5	✓ Clean	`CCSC(SCC)[C@@H](O)[C@@H](O)[C@H](O)CO`

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 A0A0H3GTJ1