KpKP13 Protein target profile

1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase

Accession: KP13_04523

Gene: AHE44399.1 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GTD3

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Length 257

Pocket druggability (P2Rank · AlphaFold DB model) 0.908

Direct ligand evidence 0 56 total records

Functional annotation 0 EC 3 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 0.62. 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 (%): 36.09 Lower values reduce human off-target concern.
Human E-value: 3.73e-13
Gut microbiome similarity: 0.7% 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: 97.29 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) 0.908

Structure A0A0H3GTD3

Pocket Pocket 1

Druggability (FPocket) 0.618

Structure A0A0H3GTD3

Pocket Pocket 6

ColabFold model

P2Rank 0.92 · Pocket 1

FPocket 0.439 · Pocket 8

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 33 / 4744 genomes with a hit

Prevalence 0.7%

Sequence

Primary amino-acid sequence viewer.

MRFTDKVVIITGAAQGIGRQTAEQAAAEGAALLLIDRSSYVHELAATLAQSGCLVLALEADLEAWESTEQAFAAGVAHFGRIDVLINNVGGTIWARPFAEYQPEQIEKEIRRSLFPTLWGCRAALPWMLKQGKGSIVNISSVATAGVNRVPYSAAKGGVNALTRSIAMEYSGSGIRINAVAPGGTEAPPRLTPRNEEQPSEQEKAWYQQVVDQTVASSLLHRYGTLAEQANAILFLASDEASYITGVTLPVAGGDLG

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

3 GO

Subcellular localization

Localization: CytoplasmicMembrane

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:0016616 Catalysis of an oxidation-reduction (redox) reaction in which a CH-OH group acts as a hydrogen or electron donor and reduces NAD+ or NADP.
GO:0030497 The elongation of a fatty acid chain by the sequential addition of two-carbon units.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

28 records

Show feature table

Start	End	DB	Term	Name
6	185	SMART	SM00822	This enzymatic domain is part of bacterial polyketide synthases and catalyses the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.
12	254	Pfam	PF13561	Enoyl-(Acyl carrier protein) reductase
152	171	PRINTS	PR00080	Short-chain dehydrogenase/reductase (SDR) superfamily signature
152	171	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
80	91	PRINTS	PR00080	Short-chain dehydrogenase/reductase (SDR) superfamily signature
80	91	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
134	142	PRINTS	PR00080	Short-chain dehydrogenase/reductase (SDR) superfamily signature
134	142	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
1	256	Gene3D	G3DSA:3.40.50.720	-
1	256	FunFam	G3DSA:3.40.50.720:FF:000084	Short-chain dehydrogenase reductase
152	171	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
7	24	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
7	24	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
128	144	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
128	144	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
219	239	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
219	239	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
80	91	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
173	190	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
173	190	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
181	201	MobiDBLite	mobidb-lite	consensus disorder prediction
2	257	NCBIfam	NF040811	benzoate diol dehydrogenase BenD
2	257	InterPro	IPR047686	Benzoate diol dehydrogenase BenD
139	167	ProSitePatterns	PS00061	Short-chain dehydrogenases/reductases family signature.
139	167	InterPro	IPR020904	Short-chain dehydrogenase/reductase, conserved site
2	254	PANTHER	PTHR42760	SHORT-CHAIN DEHYDROGENASES/REDUCTASES FAMILY MEMBER
5	254	SUPERFAMILY	SSF51735	NAD(P)-binding Rossmann-fold domains
5	254	InterPro	IPR036291	NAD(P)-binding 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

0.908

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Surrounding area

Pocket 2 P2Rank #2

0.108

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Surrounding area

Pocket 3 P2Rank #3

0.082

Likely same site as FPocket 6 3.6 Å 6 shared residues 67% 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 #6

0.618

Likely same site as P2Rank 3 3.6 Å 6 shared residues 67% of smaller site

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Surrounding area

Pocket 2 FPocket #7

0.312

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Surrounding area

Binding pockets · P2Rank

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

Pocket 1 P2Rank #1

0.92

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Surrounding area

Pocket 2 P2Rank #2

0.068

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Surrounding area

Pocket 3 P2Rank #3

0.064

Likely same site as FPocket 8 2.5 Å 10 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 #8

0.439

Likely same site as P2Rank 3 2.5 Å 10 shared residues 100% of smaller site

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Surrounding area

Pocket 2 FPocket #6

0.321

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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_A0A0H3GTD3	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_04523	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.

56 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 6 records from similar proteins

Structural ligands 6 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

1PS PDB via homolog 201.2 Da · LogP -0.09 · TPSA 61.1 Open detail RCSB PDB

A6O PDB via homolog Detail RCSB PDB

B3P PDB via homolog Detail RCSB PDB

HBR PDB via homolog Detail RCSB PDB

TAM 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
1PS RCSB PDB	4URE	Q5P8S7	201.2 Da LogP -0.09 TPSA 61.1	✓ Ro5	✓ Clean	`c1cc[n+](cc1)CCCS(=O)(=O)[O-]`
A6O RCSB PDB	6IHH	C0IR58	314.4 Da LogP 3.93 TPSA 46.5	✓ Ro5	✓ Clean	`CC[C@]1([C@H](CCC1=O)O)C/C=C/2\CCCc3c2ccc(c3)OC`
B3P RCSB PDB	4NBV	B3R6T4	282.3 Da LogP -4.01 TPSA 145.4	1 viol.	✓ Clean	`C(CNC(CO)(CO)CO)CNC(CO)(CO)CO`
HBR RCSB PDB	6XEW	H9XP47	88.1 Da LogP -0.04 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@H](C(=O)C)O`
TAM RCSB PDB	4BMN	C0IR58	163.2 Da LogP -1.17 TPSA 86.7	✓ Ro5	✓ Clean	`C(CO)C(CCO)(CCO)N`
TUD RCSB PDB	5EPO	G9FRD7	499.7 Da LogP 3.40 TPSA 123.9	✓ Ro5	✓ Clean	`C[C@H](CCC(=O)NCCS(=O)(=O)O)[C@H]1CC[C@@H]2[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
ZINC118914627 ZINC	1.000	499.7 Da LogP 3.40 TPSA 123.9	✓ Ro5	✓ Clean	`C[C@H](CCC(=O)NCCS(=O)(=O)O)[C@H]1CC[C@H]2[C@@H…`
ZINC118915233 ZINC	1.000	499.7 Da LogP 3.40 TPSA 123.9	✓ Ro5	✓ Clean	`C[C@@H](CCC(=O)NCCS(=O)(=O)O)[C@H]1CC[C@H]2[C@H…`
ZINC118915234 ZINC	1.000	499.7 Da LogP 3.40 TPSA 123.9	✓ Ro5	✓ Clean	`C[C@H](CCC(=O)NCCS(=O)(=O)O)[C@H]1CC[C@H]2[C@H]…`
ZINC118915235 ZINC	1.000	499.7 Da LogP 3.40 TPSA 123.9	✓ Ro5	✓ Clean	`C[C@@H](CCC(=O)NCCS(=O)(=O)O)[C@H]1CC[C@H]2[C@@…`
ZINC13515755 ZINC	1.000	499.7 Da LogP 3.40 TPSA 123.9	✓ Ro5	✓ Clean	`C[C@H](CCC(=O)NCCS(=O)(=O)O)[C@H]1CC[C@@H]2[C@@…`
ZINC14984492 ZINC	1.000	499.7 Da LogP 3.40 TPSA 123.9	✓ Ro5	✓ Clean	`C[C@H](CCC(=O)NCCS(=O)(=O)O)[C@H]1CC[C@@H]2[C@H…`
ZINC1857687 ZINC	1.000	499.7 Da LogP 3.40 TPSA 123.9	✓ Ro5	✓ Clean	`C[C@H](CCC(=O)NCCS(=O)(=O)O)[C@@H]1CC[C@H]2[C@@…`
ZINC1857777820 ZINC	1.000	499.7 Da LogP 3.40 TPSA 123.9	✓ Ro5	✓ Clean	`C[C@H](CCC(=O)NCCS(=O)(=O)O)[C@@H]1CC[C@H]2[C@H…`
ZINC1857777821 ZINC	1.000	499.7 Da LogP 3.40 TPSA 123.9	✓ Ro5	✓ Clean	`C[C@@H](CCC(=O)NCCS(=O)(=O)O)[C@@H]1CC[C@H]2[C@…`
ZINC1888841 ZINC	1.000	499.7 Da LogP 3.40 TPSA 123.9	✓ Ro5	✓ Clean	`C[C@H](CCC(=O)NCCS(=O)(=O)O)[C@@H]1CC[C@H]2[C@H…`
ZINC252584587 ZINC	1.000	499.7 Da LogP 3.40 TPSA 123.9	✓ Ro5	✓ Clean	`C[C@H](CCC(=O)NCCS(=O)(=O)O)[C@@H]1CC[C@@H]2[C@…`
ZINC253534622 ZINC	1.000	499.7 Da LogP 3.40 TPSA 123.9	✓ Ro5	✓ Clean	`C[C@H](CCC(=O)NCCS(=O)(=O)O)[C@@H]1CC[C@@H]2[C@…`
ZINC253534623 ZINC	1.000	499.7 Da LogP 3.40 TPSA 123.9	✓ Ro5	✓ Clean	`C[C@@H](CCC(=O)NCCS(=O)(=O)O)[C@@H]1CC[C@@H]2[C…`
ZINC253534624 ZINC	1.000	499.7 Da LogP 3.40 TPSA 123.9	✓ Ro5	✓ Clean	`C[C@@H](CCC(=O)NCCS(=O)(=O)O)[C@@H]1CC[C@@H]2[C…`
ZINC253558526 ZINC	1.000	499.7 Da LogP 3.40 TPSA 123.9	✓ Ro5	✓ Clean	`C[C@H](CCC(=O)NCCS(=O)(=O)O)[C@H]1CC[C@@H]2[C@@…`
ZINC29552512 ZINC	1.000	499.7 Da LogP 3.40 TPSA 123.9	✓ Ro5	✓ Clean	`C[C@H](CCC(=O)NCCS(=O)(=O)O)[C@H]1CC[C@@H]2[C@H…`
ZINC33650236 ZINC	1.000	499.7 Da LogP 3.40 TPSA 123.9	✓ Ro5	✓ Clean	`C[C@H](CCC(=O)NCCS(=O)(=O)O)[C@H]1CC[C@H]2[C@H]…`
ZINC33650237 ZINC	1.000	499.7 Da LogP 3.40 TPSA 123.9	✓ Ro5	✓ Clean	`C[C@H](CCC(=O)NCCS(=O)(=O)O)[C@H]1CC[C@@H]2[C@H…`
ZINC38324520 ZINC	1.000	499.7 Da LogP 3.40 TPSA 123.9	✓ Ro5	✓ Clean	`C[C@H](CCC(=O)NCCS(=O)(=O)O)[C@H]1CC[C@@H]2[C@H…`
ZINC3914813 ZINC	1.000	499.7 Da LogP 3.40 TPSA 123.9	✓ Ro5	✓ Clean	`C[C@H](CCC(=O)NCCS(=O)(=O)O)[C@H]1CC[C@H]2[C@@H…`
ZINC40164308 ZINC	1.000	499.7 Da LogP 3.40 TPSA 123.9	✓ Ro5	✓ Clean	`C[C@H](CCC(=O)NCCS(=O)(=O)O)[C@H]1CC[C@H]2[C@@H…`
ZINC4521259 ZINC	1.000	282.3 Da LogP -4.01 TPSA 145.4	1 viol.	✓ Clean	`OCC(CO)(CO)NCCCNC(CO)(CO)CO`
ZINC55161741 ZINC	1.000	499.7 Da LogP 3.40 TPSA 123.9	✓ Ro5	✓ Clean	`C[C@H](CCC(=O)NCCS(=O)(=O)O)[C@@H]1CC[C@H]2[C@@…`
ZINC5822376 ZINC	1.000	499.7 Da LogP 3.40 TPSA 123.9	✓ Ro5	✓ Clean	`C[C@H](CCC(=O)NCCS(=O)(=O)O)[C@H]1CC[C@H]2[C@H]…`
ZINC58475681 ZINC	1.000	499.7 Da LogP 3.40 TPSA 123.9	✓ Ro5	✓ Clean	`C[C@H](CCC(=O)NCCS(=O)(=O)O)[C@H]1CC[C@H]2[C@H]…`
ZINC60292561 ZINC	1.000	499.7 Da LogP 3.40 TPSA 123.9	✓ Ro5	✓ Clean	`C[C@H](CCC(=O)NCCS(=O)(=O)O)[C@H]1CC[C@H]2[C@@H…`
ZINC60292564 ZINC	1.000	499.7 Da LogP 3.40 TPSA 123.9	✓ Ro5	✓ Clean	`C[C@H](CCC(=O)NCCS(=O)(=O)O)[C@H]1CC[C@@H]2[C@@…`
ZINC85345450 ZINC	1.000	499.7 Da LogP 3.40 TPSA 123.9	✓ Ro5	✓ Clean	`C[C@H](CCC(=O)NCCS(=O)(=O)O)[C@H]1CC[C@@H]2[C@H…`
ZINC8551820 ZINC	1.000	499.7 Da LogP 3.40 TPSA 123.9	✓ Ro5	✓ Clean	`C[C@H](CCC(=O)NCCS(=O)(=O)O)[C@H]1CC[C@@H]2[C@H…`
ZINC91297636 ZINC	1.000	499.7 Da LogP 3.40 TPSA 123.9	✓ Ro5	✓ Clean	`C[C@H](CCC(=O)NCCS(=O)(=O)O)[C@H]1CC[C@@H]2[C@@…`
ZINC953115464 ZINC	1.000	499.7 Da LogP 3.40 TPSA 123.9	✓ Ro5	✓ Clean	`C[C@H](CCC(=O)NCCS(=O)(=O)O)[C@@H]1CC[C@H]2[C@H…`
ZINC118912555 ZINC	0.790	483.7 Da LogP 4.43 TPSA 103.7	✓ Ro5	✓ Clean	`C[C@@H](CCC(=O)NCCS(=O)(=O)O)[C@H]1CC[C@H]2[C@@…`
ZINC118912557 ZINC	0.790	483.7 Da LogP 4.43 TPSA 103.7	✓ Ro5	✓ Clean	`C[C@@H](CCC(=O)NCCS(=O)(=O)O)[C@H]1CC[C@H]2[C@@…`
ZINC13551300 ZINC	0.790	483.7 Da LogP 4.43 TPSA 103.7	✓ Ro5	✓ Clean	`C[C@H](CCC(=O)NCCS(=O)(=O)O)[C@H]1CC[C@H]2[C@@H…`
ZINC13551303 ZINC	0.790	483.7 Da LogP 4.43 TPSA 103.7	✓ Ro5	✓ Clean	`C[C@H](CCC(=O)NCCS(=O)(=O)O)[C@H]1CC[C@H]2[C@@H…`
ZINC13551306 ZINC	0.790	483.7 Da LogP 4.43 TPSA 103.7	✓ Ro5	✓ Clean	`C[C@H](CCC(=O)NCCS(=O)(=O)O)[C@H]1CC[C@H]2[C@@H…`
ZINC2038155210 ZINC	0.790	483.7 Da LogP 4.43 TPSA 103.7	✓ Ro5	✓ Clean	`C[C@@H](CCC(=O)NCCS(=O)(=O)O)[C@@H]1CC[C@H]2[C@…`
ZINC2038155211 ZINC	0.790	483.7 Da LogP 4.43 TPSA 103.7	✓ Ro5	✓ Clean	`C[C@H](CCC(=O)NCCS(=O)(=O)O)[C@@H]1CC[C@H]2[C@@…`
ZINC4095893 ZINC	0.790	483.7 Da LogP 4.43 TPSA 103.7	✓ Ro5	✓ Clean	`C[C@H](CCC(=O)NCCS(=O)(=O)O)[C@H]1CC[C@H]2[C@@H…`
ZINC118938028 ZINC	0.746	499.7 Da LogP 3.40 TPSA 123.9	✓ Ro5	✓ Clean	`C[C@@H](CCC(=O)NCCS(=O)(=O)O)[C@H]1CC[C@H]2[C@@…`
ZINC3927571 ZINC	0.746	499.7 Da LogP 3.40 TPSA 123.9	✓ Ro5	✓ Clean	`C[C@H](CCC(=O)NCCS(=O)(=O)O)[C@H]1CC[C@H]2[C@@H…`
ZINC83291831 ZINC	0.746	499.7 Da LogP 3.40 TPSA 123.9	✓ Ro5	✓ Clean	`C[C@H](CCC(=O)NCCS(=O)(=O)O)[C@H]1CC[C@H]2[C@@H…`
ZINC118912614 ZINC	0.742	449.6 Da LogP 3.59 TPSA 106.9	✓ Ro5	✓ Clean	`C[C@@H](CCC(=O)NCC(=O)O)[C@H]1CC[C@H]2[C@@H]3[C…`
ZINC118912615 ZINC	0.742	449.6 Da LogP 3.59 TPSA 106.9	✓ Ro5	✓ Clean	`C[C@H](CCC(=O)NCC(=O)O)[C@H]1CC[C@H]2[C@@H]3[C@…`
ZINC12494227 ZINC	0.742	449.6 Da LogP 3.59 TPSA 106.9	✓ Ro5	✓ Clean	`C[C@H](CCC(=O)NCC(=O)O)[C@H]1CC[C@@H]2[C@H]3[C@…`
ZINC1903846414 ZINC	0.742	449.6 Da LogP 3.59 TPSA 106.9	✓ Ro5	✓ Clean	`C[C@@H](CCC(=O)NCC(=O)O)[C@@H]1CC[C@H]2[C@H]3[C…`
ZINC1903846415 ZINC	0.742	449.6 Da LogP 3.59 TPSA 106.9	✓ Ro5	✓ Clean	`C[C@H](CCC(=O)NCC(=O)O)[C@@H]1CC[C@H]2[C@H]3[C@…`
ZINC3914812 ZINC	0.742	449.6 Da LogP 3.59 TPSA 106.9	✓ Ro5	✓ Clean	`C[C@H](CCC(=O)NCC(=O)O)[C@H]1CC[C@H]2[C@H]3[C@H…`
ZINC58475559 ZINC	0.742	449.6 Da LogP 3.59 TPSA 106.9	✓ Ro5	✓ Clean	`C[C@H](CCC(=O)NCC(=O)O)[C@H]1CC[C@H]2[C@H]3[C@H…`
ZINC96533565 ZINC	0.742	449.6 Da LogP 3.59 TPSA 106.9	✓ Ro5	✓ Clean	`C[C@H](CCC(=O)NCC(=O)O)[C@H]1CC[C@H]2[C@H]3[C@H…`

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 A0A0H3GTD3