KpATCC43816 Protein target profile

di-trans,poly-cis-decaprenylcistransferase

Accession: VK055_2378

Gene: AIK80975.1 uppS 3D evidence: AlphaFold DB model + ColabFold model Metabolism 1 reaction UniProt A0A0H3GS37

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Length 252

Pocket druggability (P2Rank · AlphaFold DB model) 0.958

Metabolic reactions 1

Chokepoint No

Direct ligand evidence 0 71 total records

Functional annotation 1 EC 8 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

Central metabolic position More central than 94.4% of genes in this genome. No isoenzyme backup detected Imported GPR rules do not show an alternative enzyme for the catalyzed reaction set. Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Second pocket predictor agrees P2Rank predicted binding-site probability 0.96. Review the complete evidence below

Risks to review

Evidence coverage

Core evidence streams are available for this target.

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 (%): 42.857 Lower values reduce human off-target concern.
Human E-value: 3.12e-10
Gut microbiome similarity: 7.8% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 88.095 Higher values support similarity to known essential genes.
DEG E-value: 3.38e-168 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 92.96 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) 0.958

Structure A0A0H3GS37

Pocket Pocket 1

Druggability (FPocket) 0.863

Structure A0A0H3GS37

Pocket Pocket 1

ColabFold model

P2Rank 0.955 · Pocket 1

FPocket 0.989 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 371 / 4744 genomes with a hit

Prevalence 7.8%

Metabolic context

Reactions catalyzed, pathway membership, and centrality in the genome-scale metabolic network.

Explore metabolic network

Metabolic context: more central than 94.4% of genes in this genome.

Relative network centrality 94.4% more central than 94.4% of genes in this genome

Chokepoint Not a chokepoint

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MLSANQTVSEISPTHGCRHVAIIMDGNGRWAKRQGKIRAFGHKAGAKSVRRAVSFAANNGIEALTLYAFSSENWNRPAQEVSALMELFVWALDSEVKSLHRHNVRLRIIGDTTRFNARLQERIRKAEALTANNTGLTLNIAANYGGRWDITQGVRLLAKQVQDGTLLPEQITEDMLSQQVCMHELAPVDLVIRTGGEHRISNFLIWQIAYAELYFTDVLWPDFAEQDFEGALHAFVNRERRFGGTEPGGSHA

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 8 GO

Subcellular localization

Localization: Cytoplasmic

Enzyme Commission (EC)

2.5.1.31

Gene Ontology (GO)

GO:0016765 Catalysis of the transfer of an alkyl or aryl (but not methyl) group from one compound (donor) to another (acceptor).
GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
GO:0008834 Catalysis of the reaction: (2E,6E)-farnesyl diphosphate + 8 isopentenyl diphosphate = di-trans,octa-cis-undecaprenyl diphosphate + 8 diphosphate.
GO:0000287 Binding to a magnesium (Mg) ion.
GO:0071555 A process that results in the assembly, arrangement of constituent parts, or disassembly of the cell wall, the rigid or semi-rigid envelope lying outside the cell membrane of plant, fungal and most prokaryotic cells, maintaining their shape and protecting them from osmotic lysis.
GO:0009252 The chemical reactions and pathways resulting in the formation of peptidoglycans, any of a class of glycoconjugates found in bacterial cell walls and consisting of long glycan strands of alternating residues of beta-(1,4) linked N-acetylglucosamine and N-acetylmuramic acid, cross-linked by short peptides.
GO:0016094 The chemical reactions and pathways resulting in the formation of polyprenols, prenols with more than 4 isoprenoid residues, which may be all-trans, or a mixture of cis and trans.
GO:0008360 Any process that modulates the surface configuration of a cell.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

17 records

Show feature table

Start	End	DB	Term	Name
16	243	PANTHER	PTHR10291	DEHYDRODOLICHYL DIPHOSPHATE SYNTHASE FAMILY MEMBER
16	243	InterPro	IPR001441	Decaprenyl diphosphate synthase-like
2	245	Gene3D	G3DSA:3.40.1180.10	-
2	245	InterPro	IPR036424	Decaprenyl diphosphate synthase-like superfamily
18	243	NCBIfam	TIGR00055	polyprenyl diphosphate synthase
18	243	InterPro	IPR001441	Decaprenyl diphosphate synthase-like
16	244	Hamap	MF_01139	Ditrans,polycis-undecaprenyl-diphosphate synthase ((2E,6E)-farnesyl-diphosphate specific) [uppS].
16	244	InterPro	IPR001441	Decaprenyl diphosphate synthase-like
18	239	SUPERFAMILY	SSF64005	Undecaprenyl diphosphate synthase
18	239	InterPro	IPR036424	Decaprenyl diphosphate synthase-like superfamily
19	235	CDD	cd00475	Cis_IPPS
19	235	InterPro	IPR001441	Decaprenyl diphosphate synthase-like
189	206	ProSitePatterns	PS01066	Undecaprenyl pyrophosphate synthase family signature.
189	206	InterPro	IPR018520	Di-trans-poly-cis-decaprenylcistransferase-like, conserved site
23	243	Pfam	PF01255	Putative undecaprenyl diphosphate synthase
23	243	InterPro	IPR001441	Decaprenyl diphosphate synthase-like
5	245	FunFam	G3DSA:3.40.1180.10:FF:000001	(2E,6E)-farnesyl-diphosphate-specific ditrans,polycis-undecaprenyl-diphosphate synthase

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

0.958

Likely same site as FPocket 1 4.9 Å 29 shared residues 85% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.067

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Surrounding area

Pocket 3 P2Rank #3

0.052

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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

0.863 Unusual size

Likely same site as P2Rank 1 4.9 Å 29 shared residues 85% of smaller site

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Surrounding area

Residue sets

UniProt: Active site:31-31

UniProt: Active site:79-79 Proton acceptor

UniProt: Binding site:199-199

UniProt: Binding site:204-204

UniProt: Binding site:205-207

UniProt: Binding site:218-218

UniProt: Binding site:31-31

UniProt: Binding site:32-35

UniProt: Binding site:36-36

UniProt: Binding site:44-44

UniProt: Binding site:48-48

UniProt: Binding site:76-78

UniProt: Binding site:80-80

UniProt: Binding site:82-82

Binding pockets · P2Rank

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

Pocket 1 P2Rank #1

0.955

Likely same site as FPocket 1 7.3 Å 20 shared residues 61% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.069

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Surrounding area

Pocket 3 P2Rank #3

0.064

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Surrounding area

Pocket 4 P2Rank #4

0.013

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Surrounding area

Residue sets

UniProt: Active site:31-31

UniProt: Active site:79-79 Proton acceptor

UniProt: Binding site:199-199

UniProt: Binding site:204-204

UniProt: Binding site:205-207

UniProt: Binding site:218-218

UniProt: Binding site:31-31

UniProt: Binding site:32-35

UniProt: Binding site:36-36

UniProt: Binding site:44-44

UniProt: Binding site:48-48

UniProt: Binding site:76-78

UniProt: Binding site:80-80

UniProt: Binding site:82-82

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_A0A0H3GS37	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_2378	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.

71 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 21 records from similar proteins

Structural ligands 4 0 loaded crystals

Measured bioactivity 17 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

53Q PDB via homolog 406.0 Da · LogP 6.56 · TPSA 12.5 Open detail RCSB PDB

DPO PDB via homolog Detail RCSB PDB

H78 PDB via homolog Detail RCSB PDB

V0D PDB via homolog Detail RCSB PDB

CHEMBL272547 ChEMBL via homolog · pchembl 7.40 (~39.8 nM) 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
53Q RCSB PDB	7JLJ	O31751	406.0 Da LogP 6.56 TPSA 12.5	1 viol.	✓ Clean	`CCN(CC)CCOc1ccc(cc1)/C(=C(\c2ccccc2)/Cl)/c3cccc…`
DPO RCSB PDB	2DTN	P55984	173.9 Da LogP -3.34 TPSA 135.6	✓ Ro5	✓ Clean	`[O-]P(=O)([O-])OP(=O)([O-])[O-]`
H78 RCSB PDB	3WYJ	P60472	948.7 Da LogP 3.71 TPSA 362.9	2 viol.	✓ Clean	`c1cc(cc(c1)c2cccc(c2)NS(=O)(=O)c3cccc(c3)S(=O)(…`
V0D RCSB PDB	7JLR	O31751	338.4 Da LogP 4.48 TPSA 33.4	✓ Ro5	✓ Clean	`CCc1cc(n2c(n1)c(cn2)c3ccc(cc3)F)N4CCCCCC4`

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
CHEMBL272547 ChEMBL	Q97SR4	7.40 ~39.8 nM	404.5 Da LogP 4.62 TPSA 78.4	✓ Ro5	✓ Clean	`O=C(Nc1ccc(C2CCCCC2)cc1)C1=C(O)CC(Cc2ccccc2)NC1…`
CHEMBL404127 ChEMBL	Q97SR4	7.22 ~60.3 nM	396.5 Da LogP 4.95 TPSA 78.4	✓ Ro5	✓ Clean	`O=C(Nc1ccc(C2CCCCC2)cc1)C1=C(O)CC(C2CCCCC2)NC1=O`
CHEMBL271482 ChEMBL	Q97SR4	7.16 ~69.2 nM	328.4 Da LogP 2.38 TPSA 78.4	✓ Ro5	✓ Clean	`O=C(NC1CCCCC1)C1=C(O)CC(Cc2ccccc2)NC1=O`
CHEMBL272054 ChEMBL	Q97SR4	7.16 ~69.2 nM	390.5 Da LogP 4.75 TPSA 78.4	✓ Ro5	✓ Clean	`O=C(Nc1ccc(C2CCCCC2)cc1)C1=C(O)C[C@@H](c2ccccc2…`
CHEMBL256222 ChEMBL	Q97SR4	6.96 ~109.6 nM	414.5 Da LogP 4.36 TPSA 87.7	✓ Ro5	✓ Clean	`O=C(Nc1ccc(Oc2ccccc2)cc1)C1=C(O)CC(Cc2ccccc2)NC…`
CHEMBL272914 ChEMBL	Q97SR4	6.96 ~109.6 nM	405.5 Da LogP 3.56 TPSA 81.7	✓ Ro5	Alert	`O=C(Nc1ccc(N2CCCCC2)cc1)C1=C(O)CC(Cc2ccccc2)NC1…`
CHEMBL257948 ChEMBL	Q97SR4	6.92 ~120.2 nM	398.5 Da LogP 4.24 TPSA 78.4	✓ Ro5	✓ Clean	`O=C(Nc1ccc(-c2ccccc2)cc1)C1=C(O)C(CCc2ccccc2)NC…`
CHEMBL272913 ChEMBL	Q97SR4	6.85 ~141.3 nM	391.3 Da LogP 2.98 TPSA 91.3	✓ Ro5	✓ Clean	`O=C(Nc1ccc(C(F)(F)F)nc1)C1=C(O)CC(Cc2ccccc2)NC1…`
CHEMBL272162 ChEMBL	Q97SR4	6.80 ~158.5 nM	404.5 Da LogP 4.62 TPSA 78.4	✓ Ro5	✓ Clean	`O=C(Nc1ccc(C2CCCCC2)cc1)C1=C(O)C(CCc2ccccc2)NC1…`
CHEMBL271845 ChEMBL	Q97SR4	6.75 ~177.8 nM	390.5 Da LogP 4.75 TPSA 78.4	✓ Ro5	✓ Clean	`O=C(Nc1ccc(C2CCCCC2)cc1)C1=C(O)C[C@H](c2ccccc2)…`
CHEMBL271291 ChEMBL	Q97SR4	6.70 ~199.5 nM	390.5 Da LogP 4.75 TPSA 78.4	✓ Ro5	✓ Clean	`O=C(Nc1ccc(C2CCCCC2)cc1)C1=C(O)CC(c2ccccc2)NC1=O`
CHEMBL404126 ChEMBL	Q97SR4	6.70 ~199.5 nM	370.5 Da LogP 4.42 TPSA 78.4	✓ Ro5	✓ Clean	`CC(C)CC1CC(O)=C(C(=O)Nc2ccc(C3CCCCC3)cc2)C(=O)N1`
CHEMBL269960 ChEMBL	Q97SR4	6.52 ~302.0 nM	390.5 Da LogP 4.53 TPSA 69.6	✓ Ro5	✓ Clean	`O=C(Nc1ccc(C2CCCCC2)cc1)C1=C(O)CN(Cc2ccccc2)C1=O`
CHEMBL255828 ChEMBL	Q97SR4	6.30 ~501.2 nM	391.5 Da LogP 4.65 TPSA 75.6	✓ Ro5	✓ Clean	`O=C(Nc1ccc(C2CCCCC2)cc1)C1=C(O)C(Cc2ccccc2)OC1=O`
CHEMBL5182237 ChEMBL	P60472	6.23 ~588.8 nM	448.3 Da LogP 3.80 TPSA 148.4	✓ Ro5	✓ Clean	`O=P(O)(O)C(O)(Cc1cccc(-c2cccc3oc4ccccc4c23)c1)P…`
CHEMBL272696 ChEMBL	Q97SR4	6.20 ~631.0 nM	388.4 Da LogP 2.75 TPSA 96.2	✓ Ro5	✓ Clean	`O=C(Nc1ccc(-n2ccnc2)cc1)C1=C(O)CC(Cc2ccccc2)NC1…`
CHEMBL256476 ChEMBL	Q97SR4	6.10 ~794.3 nM	405.5 Da LogP 3.56 TPSA 81.7	✓ Ro5	Alert	`O=C(Nc1ccc(N2CCCCC2)cc1)C1=C(O)C(CCc2ccccc2)NC1…`

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
ZINC16051958 ZINC	0.771	448.3 Da LogP 3.80 TPSA 148.4	✓ Ro5	✓ Clean	`O=P(O)(O)C(O)(Cc1cccc(-c2cccc3c2oc2ccccc23)c1)P…`
ZINC15839964 ZINC	0.735	324.4 Da LogP 4.22 TPSA 33.4	✓ Ro5	✓ Clean	`Cc1cc(N2CCCCCC2)n2ncc(-c3ccc(F)cc3)c2n1`
ZINC21798939 ZINC	0.735	310.4 Da LogP 3.83 TPSA 33.4	✓ Ro5	✓ Clean	`Cc1cc(N2CCCCC2)n2ncc(-c3ccc(F)cc3)c2n1`
ZINC21799024 ZINC	0.714	296.3 Da LogP 3.44 TPSA 33.4	✓ Ro5	✓ Clean	`Cc1cc(N2CCCC2)n2ncc(-c3ccc(F)cc3)c2n1`
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`
ZINC1690792 ZINC	0.683	297.4 Da LogP 3.64 TPSA 29.5	✓ Ro5	✓ Clean	`CCN(CC)CCOc1ccc(C(=O)c2ccccc2)cc1`
ZINC7636168 ZINC	0.660	320.4 Da LogP 4.34 TPSA 33.4	✓ Ro5	✓ Clean	`CCCc1cc(N2CCCCC2)n2ncc(-c3ccccc3)c2n1`
ZINC3593496 ZINC	0.652	206.2 Da LogP -1.16 TPSA 121.1	✓ Ro5	✓ Clean	`COC(=O)C[C@@](O)(CC(=O)O)C(=O)O`
ZINC3593497 ZINC	0.652	206.2 Da LogP -1.16 TPSA 121.1	✓ Ro5	✓ Clean	`COC(=O)C[C@](O)(CC(=O)O)C(=O)O`
ZINC11957989 ZINC	0.650	237.3 Da LogP 2.11 TPSA 49.8	✓ Ro5	✓ Clean	`CCN(CC)CCOc1ccc(C(=O)O)cc1`
ZINC5205464 ZINC	0.642	306.4 Da LogP 3.95 TPSA 33.4	✓ Ro5	✓ Clean	`CCCc1cc(N2CCCC2)n2ncc(-c3ccccc3)c2n1`
ZINC14686440 ZINC	0.625	436.4 Da LogP -2.64 TPSA 247.9	1 viol.	✓ Clean	`O=C(O)C[C@](O)(CC(=O)NCCCCNC(=O)C[C@@](O)(CC(=O…`
ZINC14686442 ZINC	0.625	436.4 Da LogP -2.64 TPSA 247.9	1 viol.	✓ Clean	`O=C(O)C[C@@](O)(CC(=O)NCCCCNC(=O)C[C@](O)(CC(=O…`
ZINC14686444 ZINC	0.625	436.4 Da LogP -2.64 TPSA 247.9	1 viol.	✓ Clean	`O=C(O)C[C@@](O)(CC(=O)NCCCCNC(=O)C[C@@](O)(CC(=…`
ZINC32910611 ZINC	0.619	420.5 Da LogP 3.17 TPSA 81.8	✓ Ro5	Alert	`O=C(CN1C(=O)N[C@@H](CCc2ccccc2)C1=O)Nc1ccc(N2CC…`
ZINC32910612 ZINC	0.619	420.5 Da LogP 3.17 TPSA 81.8	✓ Ro5	Alert	`O=C(CN1C(=O)N[C@H](CCc2ccccc2)C1=O)Nc1ccc(N2CCC…`
ZINC21799073 ZINC	0.618	339.4 Da LogP 2.99 TPSA 36.7	✓ Ro5	✓ Clean	`CCN1CCN(c2cc(C)nc3c(-c4ccc(F)cc4)cnn23)CC1`
ZINC7636212 ZINC	0.608	306.4 Da LogP 4.00 TPSA 33.4	✓ Ro5	✓ Clean	`Cc1ccc(-c2cnn3c(N4CCCCC4)cc(C)nc23)cc1`
ZINC2334469 ZINC	0.604	326.8 Da LogP 4.35 TPSA 33.4	✓ Ro5	✓ Clean	`Cc1cc(N2CCCCC2)n2ncc(-c3ccc(Cl)cc3)c2n1`
ZINC9341694 ZINC	0.593	325.4 Da LogP 2.60 TPSA 36.7	✓ Ro5	✓ Clean	`Cc1cc(N2CCN(C)CC2)n2ncc(-c3ccc(F)cc3)c2n1`
ZINC6311433 ZINC	0.591	311.4 Da LogP 4.03 TPSA 29.5	✓ Ro5	✓ Clean	`CCN(CC)CCCOc1ccc(C(=O)c2ccccc2)cc1`
ZINC5323158 ZINC	0.588	292.4 Da LogP 3.61 TPSA 33.4	✓ Ro5	✓ Clean	`Cc1ccc(-c2cnn3c(N4CCCC4)cc(C)nc23)cc1`
ZINC16051959 ZINC	0.587	434.3 Da LogP 3.56 TPSA 135.3	✓ Ro5	✓ Clean	`O=P(O)(O)C(O)(Cc1cccc(-c2cccc(-c3ccccc3)c2)c1)P…`
ZINC16051960 ZINC	0.587	434.3 Da LogP 3.56 TPSA 135.3	✓ Ro5	✓ Clean	`O=P(O)(O)C(O)(Cc1cccc(-c2ccc(-c3ccccc3)cc2)c1)P…`
ZINC2196835 ZINC	0.585	312.8 Da LogP 3.96 TPSA 33.4	✓ Ro5	✓ Clean	`Cc1cc(N2CCCC2)n2ncc(-c3ccc(Cl)cc3)c2n1`
ZINC21798934 ZINC	0.582	312.3 Da LogP 2.68 TPSA 42.7	✓ Ro5	✓ Clean	`Cc1cc(N2CCOCC2)n2ncc(-c3ccc(F)cc3)c2n1`
ZINC21798959 ZINC	0.582	417.5 Da LogP 3.58 TPSA 62.5	✓ Ro5	✓ Clean	`Cc1cc(C)nc(N2CCN(c3cc(C)nc4c(-c5ccc(F)cc5)cnn34…`
ZINC96766512 ZINC	0.581	435.9 Da LogP 4.82 TPSA 36.7	✓ Ro5	✓ Clean	`Cc1cc(N2CCN(Cc3ccccc3Cl)CC2)n2ncc(-c3ccc(F)cc3)…`
ZINC3003759 ZINC	0.578	325.5 Da LogP 4.42 TPSA 29.5	✓ Ro5	✓ Clean	`CCN(CC)CCCCOc1ccc(C(=O)c2ccccc2)cc1`
ZINC13398039 ZINC	0.577	234.2 Da LogP -0.38 TPSA 121.1	✓ Ro5	✓ Clean	`CC(C)OC(=O)C[C@](O)(CC(=O)O)C(=O)O`
ZINC2528012 ZINC	0.577	234.2 Da LogP -0.38 TPSA 121.1	✓ Ro5	✓ Clean	`CC(C)OC(=O)C[C@@](O)(CC(=O)O)C(=O)O`
ZINC5346505 ZINC	0.574	348.5 Da LogP 4.99 TPSA 33.4	✓ Ro5	✓ Clean	`Cc1ccc(-c2cnn3c(N4CCCCC4)cc(C(C)(C)C)nc23)cc1`
ZINC1584362 ZINC	0.571	235.3 Da LogP 2.61 TPSA 29.5	✓ Ro5	✓ Clean	`CCN(CC)CCOc1ccc(C(C)=O)cc1`
ZINC2139 ZINC	0.571	283.4 Da LogP 4.00 TPSA 12.5	✓ Ro5	✓ Clean	`CCN(CC)CCOc1ccc(Cc2ccccc2)cc1`
ZINC21799020 ZINC	0.571	324.4 Da LogP 4.08 TPSA 33.4	✓ Ro5	✓ Clean	`Cc1cc(N2CCC(C)CC2)n2ncc(-c3ccc(F)cc3)c2n1`
ZINC13628220 ZINC	0.569	355.4 Da LogP 1.96 TPSA 56.9	✓ Ro5	✓ Clean	`Cc1cc(N2CCN(CCO)CC2)n2ncc(-c3ccc(F)cc3)c2n1`
ZINC96766511 ZINC	0.567	401.5 Da LogP 4.17 TPSA 36.7	✓ Ro5	✓ Clean	`Cc1cc(N2CCN(Cc3ccccc3)CC2)n2ncc(-c3ccc(F)cc3)c2…`
ZINC4295219 ZINC	0.566	292.4 Da LogP 3.70 TPSA 33.4	✓ Ro5	✓ Clean	`Cc1cc(N2CCCCC2)n2ncc(-c3ccccc3)c2n1`
ZINC1629220 ZINC	0.565	393.9 Da LogP 4.80 TPSA 41.5	✓ Ro5	✓ Clean	`OCCNCCOc1ccc(/C(=C(/Cl)c2ccccc2)c2ccccc2)cc1`
ZINC16957873 ZINC	0.565	393.9 Da LogP 4.80 TPSA 41.5	✓ Ro5	✓ Clean	`OCCNCCOc1ccc(/C(=C(\Cl)c2ccccc2)c2ccccc2)cc1`
ZINC22581216 ZINC	0.564	356.5 Da LogP 3.79 TPSA 24.9	✓ Ro5	✓ Clean	`CCN(CCOc1ccccc1)CCN(CC)CCOc1ccccc1`
ZINC7636174 ZINC	0.564	320.4 Da LogP 4.51 TPSA 33.4	✓ Ro5	✓ Clean	`CC(C)c1cc(N2CCCCC2)n2ncc(-c3ccccc3)c2n1`
ZINC1292 ZINC	0.563	325.5 Da LogP 4.22 TPSA 29.5	✓ Ro5	✓ Clean	`CCN(CC)CCOc1ccc(C(=O)CCc2ccccc2)cc1`
ZINC146315135 ZINC	0.560	204.2 Da LogP 0.86 TPSA 94.8	✓ Ro5	✓ Clean	`CCCCC[C@@](O)(CC(=O)O)C(=O)O`
ZINC146315336 ZINC	0.560	204.2 Da LogP 0.86 TPSA 94.8	✓ Ro5	✓ Clean	`CCCCC[C@](O)(CC(=O)O)C(=O)O`
ZINC1641610 ZINC	0.558	249.4 Da LogP 3.00 TPSA 29.5	✓ Ro5	✓ Clean	`CCC(=O)c1ccc(OCCN(CC)CC)cc1`
ZINC1680911 ZINC	0.558	295.4 Da LogP 4.58 TPSA 12.5	✓ Ro5	✓ Clean	`CCN(CC)CCOc1ccc(/C=C/c2ccccc2)cc1`
ZINC4706227 ZINC	0.558	295.4 Da LogP 4.58 TPSA 12.5	✓ Ro5	✓ Clean	`CCN(CC)CCOc1ccc(/C=C\c2ccccc2)cc1`
ZINC1850353 ZINC	0.556	206.1 Da LogP -0.86 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(O)CC(O)(CC(=O)O)CC(=O)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.

di-trans,poly-cis-decaprenylcistransferase

Promising target candidate with multiple supporting evidence streams.

Main supporting evidence

Risks to review

Evidence coverage

Prioritization evidence

Off-target risk

Essentiality

Structure confidence

Binding-site evidence

Metabolic context

Sequence

Functional annotations

Subcellular localization

Enzyme Commission (EC)

Gene Ontology (GO)

Sequence domains and features

3D structure

Binding pockets · P2Rank

Binding pockets · FPocket

Binding pockets · P2Rank

Binding pockets · FPocket

Structural evidence

Ligand evidence

Cross-references

Sequence

Chemistry

Pathways