KpKP13 Protein target profile

Beta-galactosidase 1

Accession: KP13_05294

Gene: AHE44701.1 lacZ1 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A6A8EMV2

Export view

Length 1035

Pocket druggability (P2Rank · AlphaFold DB model) 0.909

Direct ligand evidence 0 67 total records

Functional annotation 1 EC 9 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

Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Moderate predicted binding pocket FPocket selected-pocket score 0.69. This supports review but is not experimental validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.91. Structure available AlphaFold DB model + ColabFold model 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 (%): 23.516 Lower values reduce human off-target concern.
Human E-value: 4.84e-20
Gut microbiome similarity: 2.1% 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: 96.2 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) 0.909

Structure A0A6A8EMV2

Pocket Pocket 1

Druggability (FPocket) 0.693

Structure A0A6A8EMV2

Pocket Pocket 1

ColabFold model

P2Rank 0.915 · Pocket 1

FPocket 0.471 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 98 / 4744 genomes with a hit

Prevalence 2.1%

Sequence

Primary amino-acid sequence viewer.

MQISDTGRSHTPDFHAVLAREDWQNQTITHLNRLPAHPVFASWRDELAARDNLPSSRRRQLDGEWQFSYARSPFAVDAQWLTQDLPDCRGTPVPSNWQMEGYDAPIYTNVRYPIDTTPPRVPEDNPTGCYSLHFTVEDTWRENGQTQIIFDGVNSAFHLWCNGVWVGYSQDSRLPAAFDLSPFLRPGDNRLCVMVMRWSAGSWLEDQDMWRMSGIFRSVWLLNKPQQRLCDVQLTPALDALYRDGTLQVQATIEATEAALAGLSVGVSLWRGEEQIAAGRQPLGTPTVDERGHYAERVDFSLAVATPAHWSAETPNCFRAVVTLWRGDELLEAEAWDIGFRRIEIADGLLRLNGKPLLIRGVNRHEHHHLRGQVVTEADMVQDILLMKQNNFNAVRCSHYPNAPRWYELCNRYGLYVVDEANIETHGMVPMNRLSDDPAWLPAFSARVTRMVQSNRNHPCIIIWSLGNESGGGGNHEALYHWLKRNDPSRPVQYEGGGADTTATDIICPMYARVERDQPIPAVPKWGIKKWISLPGEQRPLILCEYAHAMGNSLGNFADYWQAFREYPRLQGGFIWDWADQAIRKTFADGSVGWAYGGDFGDKPNDRQFCMNGLVFPDRTPHPSLVEAKHAQQYFQFTLLSTSPLRVRIISEYLFRPTDNEVLRWQVQAAGEPLYHGDLTLALPPEGSDEITLLDSLILPEGARAVWLTLEVTQPQATAWSEAEHRVAWQQFPLPAPLALPAPTVSAGAPDLIVSDEVWQIRAGSQCWTIDRRTGLLSRWSVGGQEQLLTPLRDQFIRAPLDNDIGVSEVERIDPNAWVERWKSAGLYDLEVHCVQCDAQRLANETLVDCRWHYLRGEEVVIVSHWRMHFTADGTLRLAVDGERAETLPPLPRVGLHFQVADQQAPVSWLGLGPHENYPDRRSSACFARWEQPLAAMTTPYIFPTENGLRCDTQALDWGRWHISGHFHFSVQPWSTRQLMETDHWHKMQAEDGVWITLDGLHMGVGGDDSWTPSVLPQWLLSQTRWQYEVSLRCF

MQISDTGRSHTPDFHAVLAREDWQNQTITHLNRLPAHPVFASWRDELAARDNLPSSRRRQLDGEWQFSYARSPFAVDAQWLTQDLPDCRGTPVPSNWQMEGYDAPIYTNVRYPIDTTPPRVPEDNPTGCYSLHFTVEDTWRENGQTQIIFDGVNSAFHLWCNGVWVGYSQDSRLPAAFDLSPFLRPGDNRLCVMVMRWSAGSWLEDQDMWRMSGIFRSVWLLNKPQQRLCDVQLTPALDALYRDGTLQVQATIEATEAALAGLSVGVSLWRGEEQIAAGRQPLGTPTVDERGHYAERVDFSLAVATPAHWSAETPNCFRAVVTLWRGDELLEAEAWDIGFRRIEIADGLLRLNGKPLLIRGVNRHEHHHLRGQVVTEADMVQDILLMKQNNFNAVRCSHYPNAPRWYELCNRYGLYVVDEANIETHGMVPMNRLSDDPAWLPAFSARVTRMVQSNRNHPCIIIWSLGNESGGGGNHEALYHWLKRNDPSRPVQYEGGGADTTATDIICPMYARVERDQPIPAVPKWGIKKWISLPGEQRPLILCEYAHAMGNSLGNFADYWQAFREYPRLQGGFIWDWADQAIRKTFADGSVGWAYGGDFGDKPNDRQFCMNGLVFPDRTPHPSLVEAKHAQQYFQFTLLSTSPLRVRIISEYLFRPTDNEVLRWQVQAAGEPLYHGDLTLALPPEGSDEITLLDSLILPEGARAVWLTLEVTQPQATAWSEAEHRVAWQQFPLPAPLALPAPTVSAGAPDLIVSDEVWQIRAGSQCWTIDRRTGLLSRWSVGGQEQLLTPLRDQFIRAPLDNDIGVSEVERIDPNAWVERWKSAGLYDLEVHCVQCDAQRLANETLVDCRWHYLRGEEVVIVSHWRMHFTADGTLRLAVDGERAETLPPLPRVGLHFQVADQQAPVSWLGLGPHENYPDRRSSACFARWEQPLAAMTTPYIFPTENGLRCDTQALDWGRWHISGHFHFSVQPWSTRQLMETDHWHKMQAEDGVWITLDGLHMGVGGDDSWTPSVLPQWLLSQTRWQYEVSLRCF

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 9 GO

Subcellular localization

Localization: Unknown

Enzyme Commission (EC)

3.2.1.23

Gene Ontology (GO)

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:0005975 The chemical reactions and pathways involving carbohydrates, any of a group of organic compounds based of the general formula Cx(H2O)y.
GO:0009341 A protein complex that possesses beta-galactosidase activity, i.e. catalyzes the hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides. In E. coli, the complex is a homotetramer; dimeric and hexameric beta-galactosidase complexes have been observed in other species.
GO:0016798 Catalysis of the hydrolysis of any glycosyl bond.
GO:0004553 Catalysis of the hydrolysis of any O-glycosyl bond.
GO:0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.
GO:0004565 Catalysis of the hydrolysis of terminal, non-reducing beta-D-galactose residues in beta-D-galactosides.
GO:0000287 Binding to a magnesium (Mg) ion.
GO:0005990 The chemical reactions and pathways resulting in the breakdown of lactose, the disaccharide galactopyranosyl-glucose.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

48 records

Show feature table

Start	End	DB	Term	Name
227	341	Gene3D	G3DSA:2.60.40.10	Immunoglobulins
227	341	InterPro	IPR013783	Immunoglobulin-like fold
393	418	ProSitePatterns	PS00719	Glycosyl hydrolases family 2 signature 1.
393	418	InterPro	IPR023230	Glycoside hydrolase, family 2, conserved site
342	632	FunFam	G3DSA:3.20.20.80:FF:000018	Beta-galactosidase
760	1033	SMART	SM01038	Bgal_small_N_2
760	1033	InterPro	IPR004199	Beta galactosidase small chain/ domain 5
629	738	SUPERFAMILY	SSF49303	beta-Galactosidase/glucuronidase domain
629	738	InterPro	IPR036156	Beta-Galactosidase/glucuronidase domain superfamily
11	225	Gene3D	G3DSA:2.60.120.260	-
59	225	Pfam	PF02837	Glycosyl hydrolases family 2, sugar binding domain
59	225	InterPro	IPR006104	Glycosyl hydrolases family 2, sugar binding domain
12	1035	Hamap	MF_01687	Beta-galactosidase [lacZ].
12	1035	InterPro	IPR023933	Glycoside hydrolase, family 2, beta-galactosidase
647	735	Pfam	PF16353	Beta-galactosidase, domain 4
647	735	InterPro	IPR032312	Beta-galactosidase, domain 4
745	1033	SUPERFAMILY	SSF74650	Galactose mutarotase-like
745	1033	InterPro	IPR011013	Galactose mutarotase-like domain superfamily
744	1034	Gene3D	G3DSA:2.70.98.10	-
744	1034	InterPro	IPR014718	Glycoside hydrolase-type carbohydrate-binding
539	554	PRINTS	PR00132	Glycosyl hydrolase family 2 signature
539	554	InterPro	IPR006101	Glycoside hydrolase, family 2
352	366	PRINTS	PR00132	Glycosyl hydrolase family 2 signature
352	366	InterPro	IPR006101	Glycoside hydrolase, family 2
153	168	PRINTS	PR00132	Glycosyl hydrolase family 2 signature
153	168	InterPro	IPR006101	Glycoside hydrolase, family 2
455	470	PRINTS	PR00132	Glycosyl hydrolase family 2 signature
455	470	InterPro	IPR006101	Glycoside hydrolase, family 2
383	401	PRINTS	PR00132	Glycosyl hydrolase family 2 signature
383	401	InterPro	IPR006101	Glycoside hydrolase, family 2
633	741	Gene3D	G3DSA:2.60.40.10	Immunoglobulins
633	741	InterPro	IPR013783	Immunoglobulin-like fold
17	1033	PANTHER	PTHR46323	BETA-GALACTOSIDASE
343	632	SUPERFAMILY	SSF51445	(Trans)glycosidases
343	632	InterPro	IPR017853	Glycoside hydrolase superfamily
342	632	Gene3D	G3DSA:3.20.20.80	Glycosidases
21	225	SUPERFAMILY	SSF49785	Galactose-binding domain-like
21	225	InterPro	IPR008979	Galactose-binding-like domain superfamily
766	1031	Pfam	PF02929	Beta galactosidase small chain
766	1031	InterPro	IPR004199	Beta galactosidase small chain/ domain 5
455	469	ProSitePatterns	PS00608	Glycosyl hydrolases family 2 acid/base catalyst.
455	469	InterPro	IPR023232	Glycoside hydrolase, family 2, active site
343	636	Pfam	PF02836	Glycosyl hydrolases family 2, TIM barrel domain
343	636	InterPro	IPR006103	Glycoside hydrolase family 2, catalytic domain
230	341	Pfam	PF00703	Glycosyl hydrolases family 2
230	341	InterPro	IPR006102	Glycoside hydrolase, family 2, immunoglobulin-like beta-sandwich
228	341	SUPERFAMILY	SSF49303	beta-Galactosidase/glucuronidase domain
228	341	InterPro	IPR036156	Beta-Galactosidase/glucuronidase domain superfamily

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

0.909

Likely same site as FPocket 1 1.9 Å 19 shared residues 83% of smaller site

Show in viewer

Surrounding area

Pocket 2 P2Rank #2

0.611

Likely same site as FPocket 6 6.0 Å 13 shared residues 52% of smaller site

Show in viewer

Surrounding area

Pocket 3 P2Rank #3

0.416

Show in viewer

Surrounding area

Pocket 4 P2Rank #4

0.306

Show in viewer

Surrounding area

Pocket 5 P2Rank #5

0.261

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

0.693 Unusual size

Likely same site as P2Rank 1 1.9 Å 19 shared residues 83% of smaller site

Show in viewer

Surrounding area

Pocket 2 FPocket #6

0.6

Likely same site as P2Rank 2 6.0 Å 13 shared residues 52% of smaller site

Show in viewer

Surrounding area

Pocket 3 FPocket #2

0.384 Unusual size

Show in viewer

Surrounding area

Pocket 4 FPocket #22

0.248

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

0.915

Likely same site as FPocket 1 2.3 Å 20 shared residues 80% of smaller site

Show in viewer

Surrounding area

Pocket 2 P2Rank #2

0.714

Show in viewer

Surrounding area

Pocket 3 P2Rank #3

0.409

Show in viewer

Surrounding area

Pocket 4 P2Rank #4

0.4

Show in viewer

Surrounding area

Pocket 5 P2Rank #5

0.347

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

0.471

Likely same site as P2Rank 1 2.3 Å 20 shared residues 80% of smaller site

Show in viewer

Surrounding area

Pocket 2 FPocket #31

0.372

Show in viewer

Surrounding area

Pocket 3 FPocket #61

0.218

Show in viewer

Surrounding area

Pocket 4 FPocket #13

0.204

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_A0A6A8EMV2	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_05294	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.

67 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 17 records from similar proteins

Structural ligands 11 0 loaded crystals

Measured bioactivity 6 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

149 PDB via homolog 178.1 Da · LogP -3.01 · TPSA 107.2 Open detail RCSB PDB

2DG PDB via homolog Detail RCSB PDB

BTB PDB via homolog Detail RCSB PDB

DGJ PDB via homolog Detail RCSB PDB

DVL 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
149 RCSB PDB	3CZJ	P00722	178.1 Da LogP -3.01 TPSA 107.2	✓ Ro5	✓ Clean	`C([C@@H]1[C@@H]([C@@H]([C@H](C(=O)O1)O)O)O)O`
2DG RCSB PDB	4DUV	P00722	164.2 Da LogP -2.19 TPSA 90.2	✓ Ro5	✓ Clean	`C1[C@H]([C@H]([C@H](O[C@@H]1O)CO)O)O`
BTB RCSB PDB	4DUV	P00722	209.2 Da LogP -3.01 TPSA 104.4	✓ Ro5	✓ Clean	`C(CO)N(CCO)C(CO)(CO)CO`
DGJ RCSB PDB	6TSH	P00722	163.2 Da LogP -2.97 TPSA 93.0	✓ Ro5	✓ Clean	`C1[C@@H]([C@H]([C@H]([C@H](N1)CO)O)O)O`
DVL RCSB PDB	6KUZ	P00722	537.6 Da LogP 2.84 TPSA 138.6	1 viol.	✓ Clean	`Cc1cc(c(c(c1)c2nc3ccccc3s2)OCc4ccc(cc4)O[C@H]5[…`
F4X RCSB PDB	7BRS	P00722	568.7 Da LogP 3.38 TPSA 139.7	1 viol.	✓ Clean	`CC1(c2ccccc2[N+](=C1/C=C/c3ccc(cc3)O[C@H]4[C@@H…`
F6L RCSB PDB	7BTK	P00722	560.6 Da LogP 2.85 TPSA 139.7	1 viol.	✓ Clean	`CC1(c2ccccc2[N+](=C1/C=C/c3ccc(cc3)O[C@H]4[C@@H…`
GIF RCSB PDB	5T99	A0A2D0TCC8	147.2 Da LogP -2.08 TPSA 72.7	✓ Ro5	✓ Clean	`C1[C@@H]([C@@H]([C@@H](CN1)O)O)CO`
GTZ RCSB PDB	1JZ6	P00722	202.2 Da LogP -3.02 TPSA 124.5	✓ Ro5	✓ Clean	`C([C@@H]1[C@@H]([C@@H]([C@H](c2n1nnn2)O)O)O)O`
MLI RCSB PDB	6SE8	A0A023UGN9	102.0 Da LogP -3.12 TPSA 80.3	✓ Ro5	✓ Clean	`C(C(=O)[O-])C(=O)[O-]`
PTQ RCSB PDB	5A1A	P00722	300.4 Da LogP -0.24 TPSA 90.2	✓ Ro5	✓ Clean	`c1ccc(cc1)CCS[C@H]2[C@@H]([C@H]([C@H]([C@H](O2)…`

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).

Ligand	UniProt (homolog)	pchembl	MW · LogP · TPSA	Lipinski	PAINS	SMILES
SJ5 ChEMBL	A3KMY8	7.91 ~12.3 nM	161.2 Da LogP -1.99 TPSA 89.8	✓ Ro5	✓ Clean	`C1[C@@H]([C@H]([C@@H](CN1)O)O)C(=O)O`
CHEMBL3770764 ChEMBL	Q8VNN2	7.31 ~49.0 nM	191.2 Da LogP -2.33 TPSA 93.0	✓ Ro5	✓ Clean	`OCC[C@H]1NC[C@@H](O)[C@@H](O)[C@H]1CO`
EVA ChEMBL	A3KMY8	6.88 ~131.8 nM	191.1 Da LogP -3.35 TPSA 127.1	✓ Ro5	✓ Clean	`[C@@H]1([C@@H]([C@H](NC(=O)[C@@H]1O)C(=O)O)O)O`
CHEMBL3770736 ChEMBL	Q8VNN2	6.55 ~281.8 nM	218.3 Da LogP -1.58 TPSA 98.7	✓ Ro5	✓ Clean	`NCCCC[C@H]1NC[C@@H](O)[C@@H](O)[C@H]1CO`
CHEMBL593646 ChEMBL	Q8VNN2	—	402.5 Da LogP -0.79 TPSA 128.8	✓ Ro5	✓ Clean	`OC[C@H]1O[C@@H](S[C@@H]2CO[C@@H](OCc3ccccc3)[C@…`
CHEMBL594698 ChEMBL	Q8VNN2	—	402.5 Da LogP -0.79 TPSA 128.8	✓ Ro5	✓ Clean	`OC[C@H]1O[C@@H](S[C@@H]2CO[C@@H](OCc3ccccc3)[C@…`

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`
ZINC12376523 ZINC	0.580	270.3 Da LogP -1.00 TPSA 99.4	✓ Ro5	✓ Clean	`OC[C@H]1O[C@H](OCc2ccccc2)[C@@H](O)[C@@H](O)[C@…`
ZINC144515738 ZINC	0.580	270.3 Da LogP -1.00 TPSA 99.4	✓ Ro5	✓ Clean	`OC[C@H]1O[C@@H](OCc2ccccc2)[C@@H](O)[C@H](O)[C@…`
ZINC144515945 ZINC	0.580	270.3 Da LogP -1.00 TPSA 99.4	✓ Ro5	✓ Clean	`OC[C@H]1O[C@H](OCc2ccccc2)[C@@H](O)[C@H](O)[C@H…`
ZINC14859230 ZINC	0.580	270.3 Da LogP -1.00 TPSA 99.4	✓ Ro5	✓ Clean	`OC[C@@H]1O[C@H](OCc2ccccc2)[C@@H](O)[C@@H](O)[C…`
ZINC22050930 ZINC	0.580	270.3 Da LogP -1.00 TPSA 99.4	✓ Ro5	✓ Clean	`OC[C@@H]1O[C@H](OCc2ccccc2)[C@H](O)[C@@H](O)[C@…`
ZINC5736909 ZINC	0.580	270.3 Da LogP -1.00 TPSA 99.4	✓ Ro5	✓ Clean	`OC[C@H]1O[C@@H](OCc2ccccc2)[C@H](O)[C@@H](O)[C@…`
ZINC6223245 ZINC	0.580	270.3 Da LogP -1.00 TPSA 99.4	✓ Ro5	✓ Clean	`OC[C@H]1O[C@H](OCc2ccccc2)[C@H](O)[C@@H](O)[C@@…`
ZINC535386643 ZINC	0.579	402.4 Da LogP -2.53 TPSA 158.3	1 viol.	✓ Clean	`OC[C@H]1O[C@@H](O[C@@H]2CO[C@@H](OCc3ccccc3)[C@…`
ZINC953122127 ZINC	0.579	402.4 Da LogP -2.53 TPSA 158.3	1 viol.	✓ Clean	`OC[C@H]1O[C@H](O[C@H]2CO[C@H](OCc3ccccc3)[C@@H]…`
ZINC31169037 ZINC	0.561	402.4 Da LogP -2.53 TPSA 158.3	1 viol.	✓ Clean	`OC[C@H]1O[C@@H](OCc2ccccc2)[C@H](O[C@@H]2OC[C@@…`
ZINC1319685 ZINC	0.560	240.3 Da LogP -0.36 TPSA 79.2	✓ Ro5	✓ Clean	`OC[C@@H]1O[C@@H](OCc2ccccc2)[C@H](O)[C@@H]1O`
ZINC402464 ZINC	0.560	240.3 Da LogP -0.36 TPSA 79.2	✓ Ro5	✓ Clean	`OC[C@@H]1O[C@@H](OCc2ccccc2)[C@H](O)[C@H]1O`
ZINC4831535 ZINC	0.560	240.3 Da LogP -0.36 TPSA 79.2	✓ Ro5	✓ Clean	`OC[C@@H]1O[C@@H](OCc2ccccc2)[C@@H](O)[C@@H]1O`
ZINC5736912 ZINC	0.560	240.3 Da LogP -0.36 TPSA 79.2	✓ Ro5	✓ Clean	`OC[C@@H]1O[C@@H](OCc2ccccc2)[C@@H](O)[C@H]1O`
ZINC101178340 ZINC	0.545	219.2 Da LogP -2.87 TPSA 116.1	✓ Ro5	✓ Clean	`CC(=O)N[C@@H]1C(=O)O[C@H](CO)[C@@H](O)[C@H]1O`
ZINC12502675 ZINC	0.545	219.2 Da LogP -2.87 TPSA 116.1	✓ Ro5	✓ Clean	`CC(=O)N[C@@H]1C(=O)O[C@H](CO)[C@H](O)[C@@H]1O`
ZINC12502679 ZINC	0.545	219.2 Da LogP -2.87 TPSA 116.1	✓ Ro5	✓ Clean	`CC(=O)N[C@@H]1C(=O)O[C@H](CO)[C@H](O)[C@H]1O`
ZINC4096202 ZINC	0.545	219.2 Da LogP -2.87 TPSA 116.1	✓ Ro5	✓ Clean	`CC(=O)N[C@@H]1C(=O)O[C@H](CO)[C@@H](O)[C@@H]1O`
ZINC5438581 ZINC	0.545	219.2 Da LogP -2.87 TPSA 116.1	✓ Ro5	✓ Clean	`CC(=O)N[C@H]1C(=O)O[C@H](CO)[C@@H](O)[C@@H]1O`
ZINC6761404 ZINC	0.545	219.2 Da LogP -2.87 TPSA 116.1	✓ Ro5	✓ Clean	`CC(=O)N[C@@H]1C(=O)O[C@@H](CO)[C@@H](O)[C@H]1O`
ZINC6761412 ZINC	0.545	219.2 Da LogP -2.87 TPSA 116.1	✓ Ro5	✓ Clean	`CC(=O)N[C@@H]1C(=O)O[C@@H](CO)[C@@H](O)[C@@H]1O`
ZINC34064260 ZINC	0.537	432.4 Da LogP -3.17 TPSA 178.5	2 viol.	✓ Clean	`OC[C@H]1O[C@@H](OC[C@H]2O[C@@H](OCc3ccccc3)[C@H…`
ZINC34556482 ZINC	0.536	432.4 Da LogP -3.17 TPSA 178.5	2 viol.	✓ Clean	`OC[C@H]1O[C@@H](OCc2ccccc2)[C@H](O)[C@@H](O)[C@…`
ZINC22050618 ZINC	0.528	450.5 Da LogP 3.45 TPSA 77.4	✓ Ro5	✓ Clean	`OC[C@H]1O[C@@H](OCc2ccccc2)[C@@H](OCc2ccccc2)[C…`
ZINC2334905 ZINC	0.522	261.4 Da LogP 1.10 TPSA 63.9	✓ Ro5	✓ Clean	`CC(C)CCN(CCC(C)C)C(CO)(CO)CO`
ZINC3159953 ZINC	0.522	261.4 Da LogP 1.38 TPSA 63.9	✓ Ro5	✓ Clean	`CCCCCN(CCCCC)C(CO)(CO)CO`
ZINC101136391 ZINC	0.519	269.3 Da LogP -1.03 TPSA 105.2	✓ Ro5	✓ Clean	`N[C@@H]1[C@H](O)[C@H](O)[C@@H](CO)O[C@H]1OCc1cc…`
ZINC25631134 ZINC	0.519	269.3 Da LogP -1.03 TPSA 105.2	✓ Ro5	✓ Clean	`N[C@@H]1[C@H](O)[C@@H](O)[C@@H](CO)O[C@H]1OCc1c…`
ZINC33619130 ZINC	0.519	269.3 Da LogP -1.03 TPSA 105.2	✓ Ro5	✓ Clean	`N[C@H]1[C@@H](OCc2ccccc2)O[C@H](CO)[C@H](O)[C@@…`
ZINC44699326 ZINC	0.519	269.3 Da LogP -1.03 TPSA 105.2	✓ Ro5	✓ Clean	`N[C@@H]1[C@H](O)[C@@H](O)[C@H](CO)O[C@H]1OCc1cc…`
ZINC4531111 ZINC	0.519	269.3 Da LogP -1.03 TPSA 105.2	✓ Ro5	✓ Clean	`N[C@@H]1[C@H](O)[C@H](O)[C@H](CO)O[C@H]1OCc1ccc…`
ZINC4097095 ZINC	0.515	244.1 Da LogP -2.08 TPSA 136.7	✓ Ro5	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@H](O)C[C@@H](O)[C@@H]1O`
ZINC4097096 ZINC	0.515	244.1 Da LogP -2.08 TPSA 136.7	✓ Ro5	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@@H](O)C[C@@H](O)[C@@H]1O`
ZINC13542697 ZINC	0.515	326.3 Da LogP -1.04 TPSA 136.7	✓ Ro5	✓ Clean	`O=C(O)/C=C\c1ccc(O[C@@H]2O[C@H](CO)[C@@H](O)[C@…`
ZINC13542698 ZINC	0.515	326.3 Da LogP -1.04 TPSA 136.7	✓ Ro5	✓ Clean	`O=C(O)/C=C/c1ccc(O[C@@H]2O[C@H](CO)[C@@H](O)[C@…`
ZINC71756574 ZINC	0.515	326.3 Da LogP -1.04 TPSA 136.7	✓ Ro5	✓ Clean	`O=C(O)/C=C\c1ccc(O[C@H]2O[C@@H](CO)[C@H](O)[C@@…`
ZINC206655256 ZINC	0.509	402.4 Da LogP -2.53 TPSA 158.3	1 viol.	✓ Clean	`O[C@H]1CO[C@@H](OC[C@H]2O[C@@H](OCc3ccccc3)[C@H…`
ZINC6096445 ZINC	0.509	402.4 Da LogP -2.53 TPSA 158.3	1 viol.	✓ Clean	`O[C@H]1[C@H](O)[C@@H](O)[C@H](OCc2ccccc2)O[C@@H…`
ZINC100055794 ZINC	0.500	208.2 Da LogP -3.65 TPSA 127.5	✓ Ro5	✓ Clean	`O=C1O[C@@H]([C@H](O)[C@H](O)CO)[C@@H](O)[C@H]1O`
ZINC198239203 ZINC	0.500	208.2 Da LogP -3.65 TPSA 127.5	✓ Ro5	✓ Clean	`O=C1O[C@H]([C@H](O)[C@H](O)CO)[C@@H](O)[C@@H]1O`
ZINC205407530 ZINC	0.500	208.2 Da LogP -3.65 TPSA 127.5	✓ Ro5	✓ Clean	`O=C1O[C@H]([C@@H](O)[C@H](O)CO)[C@H](O)[C@H]1O`
ZINC247750132 ZINC	0.500	208.2 Da LogP -3.65 TPSA 127.5	✓ Ro5	✓ Clean	`O=C1O[C@H]([C@H](O)[C@H](O)CO)[C@H](O)[C@H]1O`
ZINC25540717 ZINC	0.500	208.2 Da LogP -3.65 TPSA 127.5	✓ Ro5	✓ Clean	`O=C1O[C@H]([C@@H](O)[C@H](O)CO)[C@@H](O)[C@@H]1O`
ZINC43919341 ZINC	0.500	208.2 Da LogP -3.65 TPSA 127.5	✓ Ro5	✓ Clean	`O=C1O[C@H]([C@@H](O)[C@H](O)CO)[C@@H](O)[C@H]1O`
ZINC4403640 ZINC	0.500	208.2 Da LogP -3.65 TPSA 127.5	✓ Ro5	✓ Clean	`O=C1O[C@H]([C@@H](O)[C@@H](O)CO)[C@H](O)[C@@H]1O`
ZINC4403643 ZINC	0.500	208.2 Da LogP -3.65 TPSA 127.5	✓ Ro5	✓ Clean	`O=C1O[C@H]([C@H](O)[C@H](O)CO)[C@H](O)[C@@H]1O`
ZINC5220312 ZINC	0.500	208.2 Da LogP -3.65 TPSA 127.5	✓ Ro5	✓ Clean	`O=C1O[C@@H]([C@@H](O)[C@@H](O)CO)[C@H](O)[C@@H]…`
ZINC5297554 ZINC	0.500	289.5 Da LogP 2.16 TPSA 63.9	✓ Ro5	✓ Clean	`CCCCCCN(CCCCCC)C(CO)(CO)CO`
ZINC97942927 ZINC	0.500	373.6 Da LogP 4.51 TPSA 63.9	✓ Ro5	✓ Clean	`CCCCCCCCCN(CCCCCCCCC)C(CO)(CO)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 A0A6A8EMV2

Chemistry

ChEMBL SJ5 ChEMBL CHEMBL3770764 ChEMBL EVA ChEMBL CHEMBL3770736 ChEMBL CHEMBL593646 ChEMBL CHEMBL594698