KpKP13 Protein target profile

dTDP-4-dehydrorhamnose 3,5-epimerase in cps region

Accession: KP13_03795

Gene: AHE43667.1 rmlC 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GSI9

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Length 184

Pocket druggability (P2Rank · AlphaFold DB model) 0.641

Direct ligand evidence 0 60 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

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: No hit
Gut microbiome similarity: 32.9% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 64.481 Higher values support similarity to known essential genes.
DEG E-value: 1.24e-82 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 97.83 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) 0.641

Structure A0A0H3GSI9

Pocket Pocket 1

Druggability (FPocket) 0.188

Structure A0A0H3GSI9

Pocket Pocket 2

ColabFold model

P2Rank 0.738 · Pocket 1

FPocket 0.291 · Pocket 6

Core conservation Accessory gene

Roary accessory

CoreCruncher accessory

Gut microbiome 1559 / 4744 genomes with a hit

Prevalence 32.9%

Sequence

Primary amino-acid sequence viewer.

MNIIKTDIPDVLIFEPRVFGDARGFFFESFSSKVFNEAVGRQVDFVQDNHSQSQKGVLRGLHYQLDPHAQGKLVRCVEGEVFDVAVDIRRSSPTFGKWVGAVLSAENKRQLWIPEGFAHGFMALSDTVQFVYKATNYYAPQSERSIIWNDPEIGIDWPALGDCALSLSEKDLQAHTLATAEVYK

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 4 GO

Subcellular localization

Localization: Unknown

Enzyme Commission (EC)

5.1.3.13

Gene Ontology (GO)

GO:0008830 Catalysis of the reaction: dTDP-4-dehydro-6-deoxy-alpha-D-glucose = dTDP-4-dehydro-6-deoxy-L-mannose.
GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
GO:0019305 The chemical reactions and pathways resulting in the formation of dTDP-rhamnose, a substance composed of rhamnose in glycosidic linkage with deoxyribosylthymine diphosphate.
GO:0000271 The chemical reactions and pathways resulting in the formation of a polysaccharide, a polymer of many (typically more than 10) monosaccharide residues linked glycosidically.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

12 records

Show feature table

Start	End	DB	Term	Name
5	178	Pfam	PF00908	dTDP-4-dehydrorhamnose 3,5-epimerase
5	178	InterPro	IPR000888	dTDP-4-dehydrorhamnose 3,5-epimerase-related
2	180	NCBIfam	TIGR01221	dTDP-4-dehydrorhamnose 3,5-epimerase
2	180	InterPro	IPR000888	dTDP-4-dehydrorhamnose 3,5-epimerase-related
2	178	PANTHER	PTHR21047	DTDP-6-DEOXY-D-GLUCOSE-3,5 EPIMERASE
2	178	InterPro	IPR000888	dTDP-4-dehydrorhamnose 3,5-epimerase-related
1	184	Gene3D	G3DSA:2.60.120.10	Jelly Rolls
1	184	InterPro	IPR014710	RmlC-like jelly roll fold
3	174	CDD	cd00438	cupin_RmlC
3	174	InterPro	IPR000888	dTDP-4-dehydrorhamnose 3,5-epimerase-related
1	181	SUPERFAMILY	SSF51182	RmlC-like cupins
1	181	InterPro	IPR011051	RmlC-like cupin 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

0.641

Show in viewer

Surrounding area

Pocket 2 P2Rank #2

0.011

Show in viewer

Surrounding area

Binding pockets · FPocket

Druggability (FPocket): high ≥ 0.7 · medium 0.4–0.69 · low < 0.4

Pocket 1 FPocket #6

0.291

Likely same site as P2Rank 1 3.8 Å 7 shared residues 88% of smaller site

Show in viewer

Surrounding area

Pocket 2 FPocket #2

0.29

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_A0A0H3GSI9	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_03795	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.

60 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 10 records from similar proteins

Structural ligands 5 0 loaded crystals

Measured bioactivity 5 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

ATY PDB via homolog 444.2 Da · LogP -0.71 · TPSA 203.7 Open detail RCSB PDB

SRT PDB via homolog Detail RCSB PDB

TDO PDB via homolog Detail RCSB PDB

TPE PDB via homolog Detail RCSB PDB

TYD 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
ATY RCSB PDB	1DZT	P26394	444.2 Da LogP -0.71 TPSA 203.7	✓ Ro5	✓ Clean	`CC1=CN(C(=O)NC1=O)[C@H]2C[C@@H]([C@H](O2)CO[P@@…`
SRT RCSB PDB	1RTV	Q9HU21	150.1 Da LogP -2.12 TPSA 115.1	✓ Ro5	✓ Clean	`[C@H]([C@H](C(=O)O)O)(C(=O)O)O`
TDO RCSB PDB	6NDR	Q5ZXH5	546.3 Da LogP -2.22 TPSA 253.4	3 viol.	✓ Clean	`C[C@H]1C(=O)[C@H]([C@H]([C@H](O1)O[P@@](=O)(O)O…`
TPE RCSB PDB	1DZT	P26394	520.3 Da LogP 1.38 TPSA 192.7	2 viol.	✓ Clean	`CC1=CN(C(=O)NC1=O)[C@H]2C[C@@H]([C@H](O2)CO[P@@…`
TYD RCSB PDB	1EPZ	O27818	402.2 Da LogP -1.28 TPSA 197.6	✓ Ro5	✓ Clean	`CC1=CN(C(=O)NC1=O)[C@H]2C[C@@H]([C@H](O2)CO[P@]…`

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
CHEMBL592712 ChEMBL	P9WH10	7.21 ~61.7 nM	416.5 Da LogP 3.99 TPSA 81.4	✓ Ro5	✓ Clean	`C=CCn1c2ccccc2c2nnc(SCCCn3c(=O)[nH]c4ccccc43)nc…`
CHEMBL589101 ChEMBL	P9WH10	7.00 ~100.0 nM	404.5 Da LogP 3.82 TPSA 81.4	✓ Ro5	✓ Clean	`CCn1c2ccccc2c2nnc(SCCCn3c(=O)[nH]c4ccccc43)nc21`
CHEMBL590576 ChEMBL	P9WH10	6.40 ~398.1 nM	448.5 Da LogP 2.67 TPSA 115.5	✓ Ro5	✓ Clean	`C=CCn1c2ccccc2c2nnc(S(=O)(=O)CCCn3c(=O)[nH]c4cc…`
CHEMBL592545 ChEMBL	P9WH10	6.30 ~501.2 nM	390.5 Da LogP 3.34 TPSA 81.4	✓ Ro5	✓ Clean	`Cn1c2ccccc2c2nnc(SCCCn3c(=O)[nH]c4ccccc43)nc21`
CHEMBL600648 ChEMBL	P9WH10	6.10 ~794.3 nM	436.5 Da LogP 2.51 TPSA 115.5	✓ Ro5	✓ Clean	`CCn1c2ccccc2c2nnc(S(=O)(=O)CCCn3c(=O)[nH]c4cccc…`

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
ZINC18094029 ZINC	1.000	404.5 Da LogP 3.82 TPSA 81.4	✓ Ro5	✓ Clean	`CCn1c2ccccc2c2nnc(SCCCn3c(=O)[nH]c4ccccc43)nc21`
ZINC18322375 ZINC	1.000	416.5 Da LogP 3.99 TPSA 81.4	✓ Ro5	✓ Clean	`C=CCn1c2ccccc2c2nnc(SCCCn3c(=O)[nH]c4ccccc43)nc…`
ZINC33979243 ZINC	1.000	402.2 Da LogP -1.28 TPSA 197.6	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@H](O)[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC2751170 ZINC	0.875	418.5 Da LogP 4.21 TPSA 81.4	✓ Ro5	✓ Clean	`CCCn1c2ccccc2c2nnc(SCCCn3c(=O)[nH]c4ccccc43)nc21`
ZINC2745826 ZINC	0.821	390.5 Da LogP 3.34 TPSA 81.4	✓ Ro5	✓ Clean	`Cn1c2ccccc2c2nnc(SCCCn3c(=O)[nH]c4ccccc43)nc21`
ZINC2995449 ZINC	0.810	466.6 Da LogP 4.85 TPSA 81.4	✓ Ro5	✓ Clean	`O=c1[nH]c2ccccc2n1CCCSc1nnc2c3ccccc3n(Cc3ccccc3…`
ZINC13507072 ZINC	0.719	482.2 Da LogP -1.16 TPSA 244.1	2 viol.	✓ Clean	`Cc1cn([C@@H]2C[C@@H](O)[C@H](CO[P@@](=O)(O)O[P@…`
ZINC33979251 ZINC	0.719	482.2 Da LogP -1.16 TPSA 244.1	2 viol.	✓ Clean	`Cc1cn([C@@H]2C[C@H](O)[C@H](CO[P@@](=O)(O)O[P@@…`
ZINC12503053 ZINC	0.714	402.2 Da LogP -1.28 TPSA 197.6	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@H](O)[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC33979244 ZINC	0.714	402.2 Da LogP -1.28 TPSA 197.6	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@H](O)[C@H](CO[P@@](=O)(O)OP(=O)…`
ZINC33979245 ZINC	0.714	402.2 Da LogP -1.28 TPSA 197.6	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@@H](O)[C@H](CO[P@@](=O)(O)OP(=…`
ZINC33979246 ZINC	0.714	402.2 Da LogP -1.28 TPSA 197.6	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@@H](O)[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC8215882 ZINC	0.714	402.2 Da LogP -1.28 TPSA 197.6	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@H](O)[C@@H](CO[P@@](=O)(O)OP(=O…`
ZINC6455268 ZINC	0.695	376.4 Da LogP 3.33 TPSA 92.2	✓ Ro5	✓ Clean	`O=c1[nH]c2ccccc2n1CCCSc1nnc2c(n1)[nH]c1ccccc12`
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`
ZINC2869073 ZINC	0.673	286.4 Da LogP 3.89 TPSA 43.6	✓ Ro5	✓ Clean	`CCCCSc1nnc2c3ccccc3n(CC)c2n1`
ZINC13523519 ZINC	0.651	322.2 Da LogP -1.40 TPSA 151.1	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@@H](O)[C@@H](COP(=O)(O)O)O2)c(…`
ZINC1532628 ZINC	0.651	322.2 Da LogP -1.40 TPSA 151.1	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@@H](O)[C@H](COP(=O)(O)O)O2)c(=…`
ZINC1678872 ZINC	0.651	322.2 Da LogP -1.40 TPSA 151.1	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@H](O)[C@@H](COP(=O)(O)O)O2)c(=O…`
ZINC2047010 ZINC	0.651	322.2 Da LogP -1.40 TPSA 151.1	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@@H](O)[C@H](COP(=O)(O)O)O2)c(=O…`
ZINC3870253 ZINC	0.651	322.2 Da LogP -1.40 TPSA 151.1	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@H](O)[C@H](COP(=O)(O)O)O2)c(=O…`
ZINC3870254 ZINC	0.651	322.2 Da LogP -1.40 TPSA 151.1	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@H](O)[C@H](COP(=O)(O)O)O2)c(=O)…`
ZINC6523446 ZINC	0.651	322.2 Da LogP -1.40 TPSA 151.1	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@H](O)[C@@H](COP(=O)(O)O)O2)c(=…`
ZINC12763633 ZINC	0.646	392.5 Da LogP 3.41 TPSA 72.7	✓ Ro5	✓ Clean	`C=CCn1c(SCCCn2c(=O)[nH]c3ccccc32)nc2ccccc2c1=O`
ZINC2779918 ZINC	0.636	272.4 Da LogP 3.50 TPSA 43.6	✓ Ro5	✓ Clean	`CCCSc1nnc2c3ccccc3n(CC)c2n1`
ZINC2774660 ZINC	0.633	284.4 Da LogP 3.67 TPSA 43.6	✓ Ro5	✓ Clean	`C=CCn1c2ccccc2c2nnc(SCCC)nc21`
ZINC2446819 ZINC	0.632	334.4 Da LogP 4.33 TPSA 43.6	✓ Ro5	✓ Clean	`CCn1c2ccccc2c2nnc(SCCc3ccccc3)nc21`
ZINC5490587 ZINC	0.627	297.4 Da LogP 3.40 TPSA 67.4	✓ Ro5	✓ Clean	`CCn1c2ccccc2c2nnc(SCCCC#N)nc21`
ZINC6702687 ZINC	0.619	314.4 Da LogP 2.73 TPSA 80.9	✓ Ro5	✓ Clean	`C=CCn1c2ccccc2c2nnc(SCCC(=O)O)nc21`
ZINC111459735 ZINC	0.614	481.2 Da LogP -1.20 TPSA 249.9	2 viol.	✓ Clean	`Cc1cn([C@@H]2C[C@H](N)[C@H](CO[P@@](=O)(O)O[P@@…`
ZINC138164075 ZINC	0.614	498.2 Da LogP 0.21 TPSA 227.1	2 viol.	✓ Clean	`Cc1cn([C@@H]2C[C@H](O)[C@H](CO[P@@](=O)(O)O[P@@…`
ZINC6979742 ZINC	0.614	274.3 Da LogP 2.08 TPSA 63.8	✓ Ro5	✓ Clean	`CCn1c2ccccc2c2nnc(SCCO)nc21`
ZINC2188705 ZINC	0.610	282.4 Da LogP 3.44 TPSA 43.6	✓ Ro5	✓ Clean	`C=CCSc1nnc2c3ccccc3n(CC=C)c2n1`
ZINC176086 ZINC	0.607	332.4 Da LogP 4.46 TPSA 43.6	✓ Ro5	✓ Clean	`C=CCn1c2ccccc2c2nnc(SCc3ccccc3)nc21`
ZINC17107637 ZINC	0.606	320.2 Da LogP -1.46 TPSA 162.7	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@@H](O)[C@@H](COP(N)(N)=O)O2)c(…`
ZINC17107641 ZINC	0.606	320.2 Da LogP -1.46 TPSA 162.7	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@H](O)[C@@H](COP(N)(N)=O)O2)c(=…`
ZINC5493427 ZINC	0.606	320.2 Da LogP -1.46 TPSA 162.7	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@H](O)[C@H](COP(N)(N)=O)O2)c(=O…`
ZINC5493430 ZINC	0.606	320.2 Da LogP -1.46 TPSA 162.7	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@@H](O)[C@H](COP(N)(N)=O)O2)c(=…`
ZINC142512519 ZINC	0.600	498.2 Da LogP 0.21 TPSA 227.1	2 viol.	✓ Clean	`Cc1cn([C@@H]2C[C@H](O)[C@H](CO[P@@](=O)(O)O[P@@…`
ZINC176091 ZINC	0.600	258.4 Da LogP 3.11 TPSA 43.6	✓ Ro5	✓ Clean	`CCSc1nnc2c3ccccc3n(CC)c2n1`
ZINC446033 ZINC	0.600	270.4 Da LogP 3.28 TPSA 43.6	✓ Ro5	✓ Clean	`C=CCn1c2ccccc2c2nnc(SCC)nc21`
ZINC856931 ZINC	0.600	353.5 Da LogP 3.74 TPSA 46.8	✓ Ro5	✓ Clean	`C=CCn1c2ccccc2c2nnc(SCCN3CCCCC3)nc21`

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 A0A0H3GSI9

Chemistry

ChEMBL CHEMBL592712 ChEMBL CHEMBL589101 ChEMBL CHEMBL590576 ChEMBL CHEMBL592545 ChEMBL CHEMBL600648