KpKP13 Protein target profile

2,5-diketo-D-gluconic acid reductase B

Accession: KP13_02944

Gene: dkgB AHE46216.1 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GN15

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Length 267

Pocket druggability (P2Rank · AlphaFold DB model) 0.92

Direct ligand evidence 0 54 total records

Functional annotation 0 EC 4 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 0.46. This supports review but is not experimental validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.92. 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 (%): 45.455 Lower values reduce human off-target concern.
Human E-value: 3.11e-10
Gut microbiome similarity: 2.2% 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: 97.89 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) 0.92

Structure A0A0H3GN15

Pocket Pocket 1

Druggability (FPocket) 0.46

Structure A0A0H3GN15

Pocket Pocket 1

ColabFold model

P2Rank 0.906 · Pocket 1

FPocket 0.567 · Pocket 2

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 103 / 4744 genomes with a hit

Prevalence 2.2%

Sequence

Primary amino-acid sequence viewer.

MAIPAFGLGTFRLKDDVVIASVKTALELGYRAIDTAQIYDNEAAVGQAIAESGVPRDELFITTKIWIENLSKDKLIASLQESLQKLRTDYVDLTLIHWPAPNDAVAVEEFMAALMEAKKLGLTRQIGISNFTIPLMERAIAAVGAENIATNQIELSPYLQNRKVVDWAREHGIHITSYMTLAYGKALKDEVIARIAAKHNATPAQVILAWAMGEGYAVIPSSTKRDNLASNLKALDLQLDDEDRQAIAALDCNDRLVSPEGLAPQWD

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

4 GO

Subcellular localization

Localization: Cytoplasmic

Gene Ontology (GO)

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:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:1990002 Catalysis of the reaction: hydroxyacetone + NADP+ = H+ + methylglyoxal + NADPH.
GO:0051596 The chemical reactions and pathways resulting in the breakdown of methylglyoxal, CH3-CO-CHO, the aldehyde of pyruvic acid.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

27 records

Show feature table

Start	End	DB	Term	Name
81	99	PRINTS	PR00069	Aldo-keto reductase signature
81	99	InterPro	IPR020471	Aldo-keto reductase
149	178	PRINTS	PR00069	Aldo-keto reductase signature
149	178	InterPro	IPR020471	Aldo-keto reductase
186	210	PRINTS	PR00069	Aldo-keto reductase signature
186	210	InterPro	IPR020471	Aldo-keto reductase
114	131	PRINTS	PR00069	Aldo-keto reductase signature
114	131	InterPro	IPR020471	Aldo-keto reductase
25	49	PRINTS	PR00069	Aldo-keto reductase signature
25	49	InterPro	IPR020471	Aldo-keto reductase
1	265	PIRSF	PIRSF000097	AKR
1	265	InterPro	IPR020471	Aldo-keto reductase
225	245	Coils	Coil	Coil
3	250	CDD	cd19139	AKR_AKR3F2
29	46	ProSitePatterns	PS00798	Aldo/keto reductase family signature 1.
29	46	InterPro	IPR018170	Aldo/keto reductase, conserved site
1	265	FunFam	G3DSA:3.20.20.100:FF:000016	2,5-diketo-D-gluconic acid reductase B
1	266	Gene3D	G3DSA:3.20.20.100	-
1	266	InterPro	IPR036812	NADP-dependent oxidoreductase domain superfamily
12	250	Pfam	PF00248	Aldo/keto reductase family
12	250	InterPro	IPR023210	NADP-dependent oxidoreductase domain
114	131	ProSitePatterns	PS00062	Aldo/keto reductase family signature 2.
114	131	InterPro	IPR018170	Aldo/keto reductase, conserved site
2	257	PANTHER	PTHR43827	2,5-DIKETO-D-GLUCONIC ACID REDUCTASE
2	257	InterPro	IPR020471	Aldo-keto reductase
2	257	SUPERFAMILY	SSF51430	NAD(P)-linked oxidoreductase
2	257	InterPro	IPR036812	NADP-dependent oxidoreductase 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.

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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

0.92

Likely same site as FPocket 1 1.2 Å 23 shared residues 92% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.03

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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

0.46 Unusual size

Likely same site as P2Rank 1 1.2 Å 23 shared residues 92% of smaller site

Show in viewer

Surrounding area

Residue sets

UniProt: Active site:39-39 Proton donor

UniProt: Binding site:97-97

UniProt: Site:64-64 Lowers pKa of active site Tyr

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_A0A0H3GN15	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_02944	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.

54 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 4 records from similar proteins

Structural ligands 4 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

EPR PDB via homolog 319.4 Da · LogP 2.92 · TPSA 57.6 Open detail RCSB PDB

MLI PDB via homolog Detail RCSB PDB

NA7 PDB via homolog Detail RCSB PDB

TOL PDB via homolog Detail RCSB PDB

ZINC13507152 ZINC proposed compound · Tanimoto 1.000 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
EPR RCSB PDB	6KIY	Q9X265	319.4 Da LogP 2.92 TPSA 57.6	✓ Ro5	Alert	`C/C(=C\c1ccccc1)/C=C2C(=O)N(C(=S)S2)CC(=O)O`
MLI RCSB PDB	4OTK	P9WQA5	102.0 Da LogP -3.12 TPSA 80.3	✓ Ro5	✓ Clean	`C(C(=O)[O-])C(=O)[O-]`
NA7 RCSB PDB	2WZM	A0QV09	623.3 Da LogP -2.48 TPSA 317.8	3 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
TOL RCSB PDB	6KIK	Q9X265	357.4 Da LogP 3.56 TPSA 49.8	✓ Ro5	✓ Clean	`CN(CC(=O)O)C(=S)c1cccc2c1ccc(c2C(F)(F)F)OC`

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
ZINC13507152 ZINC	1.000	319.4 Da LogP 2.92 TPSA 57.6	✓ Ro5	Alert	`CC(=C\c1ccccc1)/C=C1/SC(=S)N(CC(=O)O)C1=O`
ZINC1533688 ZINC	1.000	319.4 Da LogP 2.92 TPSA 57.6	✓ Ro5	Alert	`CC(/C=C1\SC(=S)N(CC(=O)O)C1=O)=C\c1ccccc1`
ZINC1857626813 ZINC	1.000	319.4 Da LogP 2.92 TPSA 57.6	✓ Ro5	Alert	`CC(=Cc1ccccc1)C=C1SC(=S)N(CC(=O)O)C1=O`
ZINC3780343 ZINC	1.000	357.4 Da LogP 3.56 TPSA 49.8	✓ Ro5	✓ Clean	`COc1ccc2c(C(=S)N(C)CC(=O)O)cccc2c1C(F)(F)F`
ZINC967120 ZINC	1.000	319.4 Da LogP 2.92 TPSA 57.6	✓ Ro5	Alert	`CC(=C/c1ccccc1)/C=C1/SC(=S)N(CC(=O)O)C1=O`
ZINC967122 ZINC	1.000	319.4 Da LogP 2.92 TPSA 57.6	✓ Ro5	Alert	`CC(=C/c1ccccc1)/C=C1\SC(=S)N(CC(=O)O)C1=O`
ZINC12342798 ZINC	0.822	333.4 Da LogP 3.31 TPSA 57.6	✓ Ro5	Alert	`CC(/C=C1\SC(=S)N(CCC(=O)O)C1=O)=C\c1ccccc1`
ZINC4812718 ZINC	0.822	333.4 Da LogP 3.31 TPSA 57.6	✓ Ro5	Alert	`CC(=C\c1ccccc1)/C=C1/SC(=S)N(CCC(=O)O)C1=O`
ZINC966742 ZINC	0.822	333.4 Da LogP 3.31 TPSA 57.6	✓ Ro5	Alert	`CC(=C/c1ccccc1)/C=C1/SC(=S)N(CCC(=O)O)C1=O`
ZINC966743 ZINC	0.822	333.4 Da LogP 3.31 TPSA 57.6	✓ Ro5	Alert	`CC(=C/c1ccccc1)/C=C1\SC(=S)N(CCC(=O)O)C1=O`
ZINC5459256 ZINC	0.809	333.4 Da LogP 3.01 TPSA 46.6	✓ Ro5	Alert	`COC(=O)CN1C(=O)/C(=C/C(C)=C/c2ccccc2)SC1=S`
ZINC2999256 ZINC	0.795	384.3 Da LogP 3.25 TPSA 57.6	✓ Ro5	Alert	`O=C(O)CN1C(=O)/C(=C\C(Br)=C\c2ccccc2)SC1=S`
ZINC4477968 ZINC	0.795	289.4 Da LogP 3.85 TPSA 20.3	✓ Ro5	Alert	`CCN1C(=O)/C(=C\C(C)=C\c2ccccc2)SC1=S`
ZINC27530463 ZINC	0.792	347.5 Da LogP 3.40 TPSA 46.6	✓ Ro5	Alert	`CCOC(=O)CN1C(=O)/C(=C\C(C)=C\c2ccccc2)SC1=S`
ZINC4745646 ZINC	0.792	347.5 Da LogP 3.40 TPSA 46.6	✓ Ro5	Alert	`CCOC(=O)CN1C(=O)/C(=C/C(C)=C/c2ccccc2)SC1=S`
ZINC13786276 ZINC	0.791	303.3 Da LogP 2.75 TPSA 74.7	✓ Ro5	✓ Clean	`CC(/C=C1\SC(=O)N(CC(=O)O)C1=O)=C\c1ccccc1`
ZINC966749 ZINC	0.791	303.3 Da LogP 2.75 TPSA 74.7	✓ Ro5	✓ Clean	`CC(=C/c1ccccc1)/C=C1\SC(=O)N(CC(=O)O)C1=O`
ZINC3871401 ZINC	0.790	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@@H](…`
ZINC3871402 ZINC	0.790	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@@H]…`
ZINC3871403 ZINC	0.790	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@@H](…`
ZINC3871404 ZINC	0.790	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@@H]…`
ZINC4096223 ZINC	0.790	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](…`
ZINC12342801 ZINC	0.787	347.5 Da LogP 3.70 TPSA 57.6	✓ Ro5	Alert	`CC(/C=C1\SC(=S)N(CCCC(=O)O)C1=O)=C\c1ccccc1`
ZINC1870868 ZINC	0.787	347.5 Da LogP 3.70 TPSA 57.6	✓ Ro5	Alert	`CC(=C/c1ccccc1)/C=C1\SC(=S)N(CCCC(=O)O)C1=O`
ZINC2293031015 ZINC	0.787	347.5 Da LogP 3.70 TPSA 57.6	✓ Ro5	Alert	`CC(=Cc1ccccc1)C=C1SC(=S)N(CCCC(=O)O)C1=O`
ZINC4837502 ZINC	0.787	347.5 Da LogP 3.70 TPSA 57.6	✓ Ro5	Alert	`CC(=C\c1ccccc1)/C=C1/SC(=S)N(CCCC(=O)O)C1=O`
ZINC27530468 ZINC	0.776	372.5 Da LogP 3.46 TPSA 40.6	✓ Ro5	Alert	`CC(=C\c1ccccc1)/C=C1/SC(=S)N(CC(=O)N2CCCC2)C1=O`
ZINC4745624 ZINC	0.776	372.5 Da LogP 3.46 TPSA 40.6	✓ Ro5	Alert	`CC(/C=C1\SC(=S)N(CC(=O)N2CCCC2)C1=O)=C\c1ccccc1`
ZINC26466134 ZINC	0.771	375.5 Da LogP 4.48 TPSA 57.6	✓ Ro5	Alert	`CC(=C\c1ccccc1)/C=C1/SC(=S)N(CCCCCC(=O)O)C1=O`
ZINC27530469 ZINC	0.760	386.5 Da LogP 3.85 TPSA 40.6	✓ Ro5	Alert	`CC(=C\c1ccccc1)/C=C1/SC(=S)N(CC(=O)N2CCCCC2)C1=O`
ZINC27530488 ZINC	0.760	374.5 Da LogP 3.75 TPSA 49.4	✓ Ro5	Alert	`CC(=C\c1ccccc1)/C=C1/SC(=S)N(CC(=O)NC(C)(C)C)C1…`
ZINC4263573 ZINC	0.760	374.5 Da LogP 3.75 TPSA 49.4	✓ Ro5	Alert	`CC(/C=C1\SC(=S)N(CC(=O)NC(C)(C)C)C1=O)=C\c1cccc…`
ZINC4745627 ZINC	0.760	386.5 Da LogP 3.85 TPSA 40.6	✓ Ro5	Alert	`CC(/C=C1\SC(=S)N(CC(=O)N2CCCCC2)C1=O)=C\c1ccccc1`
ZINC5370996 ZINC	0.760	400.6 Da LogP 4.24 TPSA 40.6	✓ Ro5	Alert	`CC(/C=C1\SC(=S)N(CC(=O)N2CCCCCC2)C1=O)=C\c1cccc…`
ZINC20226865 ZINC	0.745	401.6 Da LogP 2.61 TPSA 43.9	✓ Ro5	Alert	`CC(/C=C1\SC(=S)N(CC(=O)N2CCN(C)CC2)C1=O)=C\c1cc…`
ZINC27530475 ZINC	0.745	401.6 Da LogP 2.61 TPSA 43.9	✓ Ro5	Alert	`CC(=C\c1ccccc1)/C=C1/SC(=S)N(CC(=O)N2CCN(C)CC2)…`
ZINC5371008 ZINC	0.745	361.5 Da LogP 3.79 TPSA 46.6	✓ Ro5	Alert	`CCCOC(=O)CN1C(=O)/C(=C/C(C)=C/c2ccccc2)SC1=S`
ZINC4478027 ZINC	0.745	301.4 Da LogP 4.02 TPSA 20.3	✓ Ro5	Alert	`C=CCN1C(=O)/C(=C\C(C)=C\c2ccccc2)SC1=S`
ZINC18008817 ZINC	0.739	339.8 Da LogP 3.10 TPSA 57.6	✓ Ro5	Alert	`O=C(O)CN1C(=O)/C(=C/C(Cl)=C/c2ccccc2)SC1=S`
ZINC2414424 ZINC	0.739	339.8 Da LogP 3.10 TPSA 57.6	✓ Ro5	Alert	`O=C(O)CN1C(=O)/C(=C\C(Cl)=C\c2ccccc2)SC1=S`
ZINC1268728 ZINC	0.731	408.5 Da LogP 4.78 TPSA 49.4	✓ Ro5	Alert	`CC(/C=C1\SC(=S)N(CC(=O)Nc2ccccc2C)C1=O)=C\c1ccc…`
ZINC16746049 ZINC	0.731	408.5 Da LogP 4.78 TPSA 49.4	✓ Ro5	Alert	`CC(=C\c1ccccc1)/C=C1/SC(=S)N(CC(=O)Nc2ccccc2C)C…`
ZINC27530471 ZINC	0.731	388.5 Da LogP 2.69 TPSA 49.9	✓ Ro5	Alert	`CC(=C\c1ccccc1)/C=C1/SC(=S)N(CC(=O)N2CCOCC2)C1=O`
ZINC4263572 ZINC	0.731	388.5 Da LogP 2.69 TPSA 49.9	✓ Ro5	Alert	`CC(/C=C1\SC(=S)N(CC(=O)N2CCOCC2)C1=O)=C\c1ccccc1`
ZINC5370983 ZINC	0.731	410.5 Da LogP 4.18 TPSA 69.6	✓ Ro5	Alert	`CC(/C=C1\SC(=S)N(CC(=O)Nc2ccccc2O)C1=O)=C\c1ccc…`
ZINC5371006 ZINC	0.731	374.5 Da LogP 3.75 TPSA 49.4	✓ Ro5	Alert	`CCCCNC(=O)CN1C(=O)/C(=C/C(C)=C/c2ccccc2)SC1=S`
ZINC8820670 ZINC	0.731	422.6 Da LogP 4.49 TPSA 40.6	✓ Ro5	Alert	`CC(/C=C1\SC(=S)N(CC(=O)N(C)Cc2ccccc2)C1=O)=C\c1…`
ZINC12360703 ZINC	0.719	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC8586020 ZINC	0.719	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC8586021 ZINC	0.719	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@@](=O)(O)OP(=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 A0A0H3GN15