KpKP13 Protein target profile

2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase

Accession: KP13_02254

Gene: AHE42827.1 kduD 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3H2F1

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Length 253

Pocket druggability (P2Rank · AlphaFold DB model) 0.911

Direct ligand evidence 0 57 total records

Functional annotation 1 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

Moderate predicted binding pocket FPocket selected-pocket score 0.41. 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 Ligand evidence via structure/bioactivity 2 structural and 5 bioactivity records.

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 (%): 34.746 Lower values reduce human off-target concern.
Human E-value: 2.19e-09
Gut microbiome similarity: 5.2% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 44.358 Higher values support similarity to known essential genes.
DEG E-value: 2.48e-66 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 97.58 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) 0.911

Structure A0A0H3H2F1

Pocket Pocket 1

Druggability (FPocket) 0.409

Structure A0A0H3H2F1

Pocket Pocket 1

ColabFold model

P2Rank 0.91 · Pocket 1

FPocket 0.919 · Pocket 1

Core conservation Accessory gene

Roary accessory

CoreCruncher accessory

Gut microbiome 246 / 4744 genomes with a hit

Prevalence 5.2%

Sequence

Primary amino-acid sequence viewer.

MILDAFSLQGKVAVVSGCDTGLGQGMALGLAEAGCDIVGINIVEPVETIERVTALGRRFLSLTADLRQIDGIPQLLERAVAEFGHIDILVNNAGLIRREDALAFSEKDWDDVMNLNIKSVFFMSQAAAKHFIAQGSGGKIINIASMLSFQGGIRVPSYTASKSAVMGVTRLLANEWAKHNINVNAIAPGYMATNNTQQLRADEQRSSEILDRIPAGRWGLPADLMGPVVFLASSASDYINGYTVAVDGGWLAR

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 4 GO

Subcellular localization

Localization: Cytoplasmic

Enzyme Commission (EC)

1.1.1.127

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:0008678 Catalysis of the reaction: 2-deoxy-D-gluconate + NAD+ = 3-dehydro-2-deoxy-D-gluconate + NADH + H+.
GO:0051287 Binding to nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NAD+, or the reduced form, NADH.
GO:0047001 Catalysis of the reaction: NAD+ + 2-dehydro-3-deoxy-D-gluconate = NADH + (4S)-4,6-dihydroxy-2,5-dioxohexanoate.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

27 records

Show feature table

Start	End	DB	Term	Name
1	253	FunFam	G3DSA:3.40.50.720:FF:000081	2-deoxy-D-gluconate 3-dehydrogenase
20	250	Pfam	PF13561	Enoyl-(Acyl carrier protein) reductase
6	252	CDD	cd05347	Ga5DH-like_SDR_c
4	250	PANTHER	PTHR42760	SHORT-CHAIN DEHYDROGENASES/REDUCTASES FAMILY MEMBER
145	173	ProSitePatterns	PS00061	Short-chain dehydrogenases/reductases family signature.
145	173	InterPro	IPR020904	Short-chain dehydrogenase/reductase, conserved site
1	253	Gene3D	G3DSA:3.40.50.720	-
214	234	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
214	234	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
158	177	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
158	177	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
12	29	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
12	29	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
84	95	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
84	95	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
132	148	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
132	148	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
179	196	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
179	196	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
9	252	SUPERFAMILY	SSF51735	NAD(P)-binding Rossmann-fold domains
9	252	InterPro	IPR036291	NAD(P)-binding domain superfamily
6	253	NCBIfam	TIGR01832	2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD
6	253	InterPro	IPR011286	2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase
84	95	PRINTS	PR00080	Short-chain dehydrogenase/reductase (SDR) superfamily signature
158	177	PRINTS	PR00080	Short-chain dehydrogenase/reductase (SDR) superfamily signature
138	146	PRINTS	PR00080	Short-chain dehydrogenase/reductase (SDR) superfamily signature
138	146	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR

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

0.911

Likely same site as FPocket 1 3.5 Å 19 shared residues 95% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.043

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Surrounding area

Pocket 3 P2Rank #3

0.005

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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

0.409

Likely same site as P2Rank 1 3.5 Å 19 shared residues 95% 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_A0A0H3H2F1	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_02254	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.

57 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 7 records from similar proteins

Structural ligands 2 0 loaded crystals

Measured bioactivity 5 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

3HL PDB via homolog 104.1 Da · LogP -0.16 · TPSA 57.5 Open detail RCSB PDB

TLA PDB via homolog Detail RCSB PDB

KDH ChEMBL via homolog · pchembl 6.50 (~316.2 nM) Detail ChEMBL

LU2 ChEMBL via homolog · pchembl 6.10 (~794.3 nM) Detail ChEMBL

CHEMBL129451 ChEMBL via homolog · pchembl 6.00 (~1.0 µM) Detail ChEMBL

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
3HL RCSB PDB	2ZTL	Q5KST5	104.1 Da LogP -0.16 TPSA 57.5	✓ Ro5	✓ Clean	`C[C@@H](CC(=O)O)O`
TLA RCSB PDB	5U9P	B4EEX4	150.1 Da LogP -2.12 TPSA 115.1	✓ Ro5	✓ Clean	`[C@@H]([C@H](C(=O)O)O)(C(=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).

Ligand	UniProt (homolog)	pchembl	MW · LogP · TPSA	Lipinski	PAINS	SMILES
KDH ChEMBL	Q8I2S7	6.50 ~316.2 nM	458.4 Da LogP 2.23 TPSA 197.4	2 viol.	Alert	`c1c(cc(c(c1O)O)O)[C@@H]2[C@@H](Cc3c(cc(cc3O2)O)…`
LU2 ChEMBL	Q965D6	6.10 ~794.3 nM	286.2 Da LogP 2.28 TPSA 111.1	✓ Ro5	Alert	`c1cc(c(cc1C2=CC(=O)c3c(cc(cc3O2)O)O)O)O`
CHEMBL129451 ChEMBL	Q965D6	6.00 ~1.0 µM	442.4 Da LogP 2.53 TPSA 177.1	1 viol.	Alert	`O=C(O[C@@H]1Cc2c(O)cc(O)cc2O[C@H]1c1ccc(O)c(O)c…`
CHEMBL36327 ChEMBL	Q965D6	6.00 ~1.0 µM	442.4 Da LogP 2.53 TPSA 177.1	1 viol.	Alert	`O=C(O[C@@H]1Cc2c(O)cc(O)cc2O[C@@H]1c1ccc(O)c(O)…`
NAR ChEMBL	Q965D6	—	272.3 Da LogP 2.51 TPSA 87.0	✓ Ro5	✓ Clean	`c1cc(ccc1[C@@H]2CC(=O)c3c(cc(cc3O2)O)O)O`

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
ZINC18185774 ZINC	1.000	286.2 Da LogP 2.28 TPSA 111.1	✓ Ro5	Alert	`O=c1cc(-c2ccc(O)c(O)c2)oc2cc(O)cc(O)c12`
ZINC3870412 ZINC	1.000	458.4 Da LogP 2.23 TPSA 197.4	2 viol.	Alert	`O=C(O[C@@H]1Cc2c(O)cc(O)cc2O[C@@H]1c1cc(O)c(O)c…`
ZINC3870413 ZINC	1.000	458.4 Da LogP 2.23 TPSA 197.4	2 viol.	Alert	`O=C(O[C@@H]1Cc2c(O)cc(O)cc2O[C@H]1c1cc(O)c(O)c(…`
ZINC3870414 ZINC	1.000	458.4 Da LogP 2.23 TPSA 197.4	2 viol.	Alert	`O=C(O[C@H]1Cc2c(O)cc(O)cc2O[C@@H]1c1cc(O)c(O)c(…`
ZINC3870415 ZINC	1.000	458.4 Da LogP 2.23 TPSA 197.4	2 viol.	Alert	`O=C(O[C@H]1Cc2c(O)cc(O)cc2O[C@H]1c1cc(O)c(O)c(O…`
ZINC14436185 ZINC	0.854	472.4 Da LogP 2.54 TPSA 186.4	2 viol.	Alert	`COc1cc(C(=O)O[C@@H]2Cc3c(O)cc(O)cc3O[C@@H]2c2cc…`
ZINC3978503 ZINC	0.851	442.4 Da LogP 2.53 TPSA 177.1	1 viol.	Alert	`O=C(O[C@@H]1Cc2c(O)cc(O)cc2O[C@@H]1c1ccc(O)c(O)…`
ZINC4534390 ZINC	0.851	442.4 Da LogP 2.53 TPSA 177.1	1 viol.	Alert	`O=C(O[C@H]1Cc2c(O)cc(O)cc2O[C@@H]1c1ccc(O)c(O)c…`
ZINC4544252 ZINC	0.851	442.4 Da LogP 2.53 TPSA 177.1	1 viol.	Alert	`O=C(O[C@H]1Cc2c(O)cc(O)cc2O[C@H]1c1ccc(O)c(O)c1…`
ZINC8681494 ZINC	0.851	442.4 Da LogP 2.53 TPSA 177.1	1 viol.	Alert	`O=C(O[C@@H]1Cc2c(O)cc(O)cc2O[C@H]1c1ccc(O)c(O)c…`
ZINC14727965 ZINC	0.848	426.4 Da LogP 2.82 TPSA 156.9	1 viol.	Alert	`O=C(O[C@@H]1Cc2c(O)cc(O)cc2O[C@@H]1c1ccc(O)cc1)…`
ZINC3871576 ZINC	0.778	270.2 Da LogP 2.58 TPSA 90.9	✓ Ro5	✓ Clean	`O=c1cc(-c2ccc(O)cc2)oc2cc(O)cc(O)c12`
ZINC4348965 ZINC	0.775	270.3 Da LogP 3.11 TPSA 66.8	✓ Ro5	✓ Clean	`Cc1cc(O)c2c(c1)O[C@H](c1ccc(O)cc1)CC2=O`
ZINC4348970 ZINC	0.775	270.3 Da LogP 3.11 TPSA 66.8	✓ Ro5	✓ Clean	`Cc1cc(O)c2c(c1)O[C@@H](c1ccc(O)cc1)CC2=O`
ZINC21992193 ZINC	0.760	458.4 Da LogP 2.23 TPSA 197.4	2 viol.	Alert	`O=C(O[C@@H]1Cc2c(O)cc(O)cc2O[C@@H]1c1cc(O)c(O)c…`
ZINC21992196 ZINC	0.760	458.4 Da LogP 2.23 TPSA 197.4	2 viol.	Alert	`O=C(O[C@H]1Cc2c(O)cc(O)cc2O[C@@H]1c1cc(O)c(O)c(…`
ZINC21992198 ZINC	0.760	458.4 Da LogP 2.23 TPSA 197.4	2 viol.	Alert	`O=C(O[C@@H]1Cc2c(O)cc(O)cc2O[C@H]1c1cc(O)c(O)c(…`
ZINC21992201 ZINC	0.760	458.4 Da LogP 2.23 TPSA 197.4	2 viol.	Alert	`O=C(O[C@H]1Cc2c(O)cc(O)cc2O[C@H]1c1cc(O)c(O)c(O…`
ZINC14813714 ZINC	0.750	300.3 Da LogP 2.59 TPSA 100.1	✓ Ro5	Alert	`COc1cc(O)c2c(=O)cc(-c3ccc(O)c(O)c3)oc2c1`
ZINC338283 ZINC	0.738	286.3 Da LogP 2.81 TPSA 76.0	✓ Ro5	✓ Clean	`COc1cc(O)c2c(c1)O[C@@H](c1ccc(O)cc1)CC2=O`
ZINC338284 ZINC	0.738	286.3 Da LogP 2.81 TPSA 76.0	✓ Ro5	✓ Clean	`COc1cc(O)c2c(c1)O[C@H](c1ccc(O)cc1)CC2=O`
ZINC13520048 ZINC	0.730	302.2 Da LogP 1.99 TPSA 131.4	✓ Ro5	Alert	`O=c1cc(-c2cc(O)c(O)c(O)c2)oc2cc(O)cc(O)c12`
ZINC39317 ZINC	0.730	270.2 Da LogP 2.58 TPSA 90.9	✓ Ro5	Alert	`O=c1cc(-c2ccc(O)c(O)c2)oc2cccc(O)c12`
ZINC14642643 ZINC	0.722	456.4 Da LogP 2.83 TPSA 166.1	1 viol.	Alert	`COc1cc(C(=O)O[C@@H]2Cc3c(O)cc(O)cc3O[C@@H]2c2cc…`
ZINC6536308 ZINC	0.718	288.7 Da LogP 3.52 TPSA 70.7	✓ Ro5	✓ Clean	`O=c1cc(-c2ccc(Cl)cc2)oc2cc(O)cc(O)c12`
ZINC14813748 ZINC	0.714	300.3 Da LogP 2.59 TPSA 100.1	✓ Ro5	Alert	`COc1cc(O)cc2oc(-c3ccc(O)c(O)c3)cc(=O)c12`
ZINC519621 ZINC	0.714	300.3 Da LogP 2.59 TPSA 100.1	✓ Ro5	✓ Clean	`COc1cc(-c2cc(=O)c3c(O)cc(O)cc3o2)ccc1O`
ZINC5733652 ZINC	0.714	300.3 Da LogP 2.59 TPSA 100.1	✓ Ro5	✓ Clean	`COc1ccc(-c2cc(=O)c3c(O)cc(O)cc3o2)cc1O`
ZINC3872070 ZINC	0.711	254.2 Da LogP 2.87 TPSA 70.7	✓ Ro5	✓ Clean	`O=c1cc(-c2ccccc2)oc2cc(O)cc(O)c12`
ZINC1532902 ZINC	0.700	206.2 Da LogP -0.86 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(O)CC[C@@](O)(CC(=O)O)C(=O)O`
ZINC2018106 ZINC	0.700	206.2 Da LogP -0.86 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(O)CC[C@](O)(CC(=O)O)C(=O)O`
ZINC14757037 ZINC	0.698	366.3 Da LogP 1.76 TPSA 154.5	✓ Ro5	Alert	`O=c1cc(-c2ccc(O)c(O)c2)oc2cc(OS(=O)(=O)O)cc(O)c…`
ZINC5999024 ZINC	0.698	286.3 Da LogP 2.81 TPSA 76.0	✓ Ro5	✓ Clean	`COc1cc(O)cc2c1C(=O)C[C@H](c1ccc(O)cc1)O2`
ZINC5999025 ZINC	0.698	286.3 Da LogP 2.81 TPSA 76.0	✓ Ro5	✓ Clean	`COc1cc(O)cc2c1C(=O)C[C@@H](c1ccc(O)cc1)O2`
ZINC12359024 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@H](O)[C@H](O)[C@@H](O)C(=O)O`
ZINC13533920 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@H](O)[C@@H](O)[C@@H](O)C(=O)O`
ZINC1532740 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@H](O)[C@@H](O)[C@H](O)C(=O)O`
ZINC1549593 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@H](O)[C@H](O)[C@@H](O)[C@@H](O)C(=O)O`
ZINC2013424 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@@H](O)[C@H](O)C(=O)O`
ZINC3581021 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@H](O)[C@@H](O)[C@@H](O)[C@@H](O)C(=O)O`
ZINC3860635 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)C(=O)O`
ZINC5783661 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@H](O)[C@@H](O)C(=O)O`
ZINC6072527 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O)C(=O)O`
ZINC1730318 ZINC	0.674	286.3 Da LogP 2.82 TPSA 87.0	✓ Ro5	✓ Clean	`Cc1c(O)cc2c(c1O)C(=O)C[C@H](c1ccc(O)cc1)O2`
ZINC5202283 ZINC	0.674	286.3 Da LogP 2.82 TPSA 87.0	✓ Ro5	✓ Clean	`Cc1c(O)cc2c(c1O)C(=O)C[C@@H](c1ccc(O)cc1)O2`
ZINC6018693 ZINC	0.674	314.3 Da LogP 2.89 TPSA 89.1	✓ Ro5	✓ Clean	`COc1ccc(-c2cc(=O)c3c(O)cc(O)cc3o2)cc1OC`
ZINC3871358 ZINC	0.667	284.3 Da LogP 2.88 TPSA 79.9	✓ Ro5	✓ Clean	`COc1ccc(-c2cc(=O)c3c(O)cc(O)cc3o2)cc1`
ZINC6092199 ZINC	0.667	270.2 Da LogP 2.58 TPSA 90.9	✓ Ro5	Alert	`O=c1cc(-c2ccc(O)c(O)c2)oc2cc(O)ccc12`
ZINC1561069 ZINC	0.659	300.3 Da LogP 3.12 TPSA 65.0	✓ Ro5	✓ Clean	`COc1ccc([C@H]2CC(=O)c3c(O)cc(OC)cc3O2)cc1`
ZINC2030112 ZINC	0.659	300.3 Da LogP 3.12 TPSA 65.0	✓ Ro5	✓ Clean	`COc1ccc([C@@H]2CC(=O)c3c(O)cc(OC)cc3O2)cc1`

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 A0A0H3H2F1

Chemistry

ChEMBL KDH ChEMBL LU2 ChEMBL CHEMBL129451 ChEMBL CHEMBL36327 ChEMBL NAR