KpATCC43816 Protein target profile

bifunctional protein RfaE, domain I

Accession: VK055_4017

Gene: AIK82564.1 rfaE 3D evidence: AlphaFold DB model + ColabFold model Metabolism Not in network UniProt A0A0H3GVR8

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Length 477

Pocket druggability (P2Rank · AlphaFold DB model) 0.909

Direct ligand evidence 0 62 total records

Functional annotation 0 EC 12 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

Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Second pocket predictor agrees P2Rank predicted binding-site probability 0.91. Structure available AlphaFold DB model + ColabFold model Ligand evidence via structure/bioactivity 10 structural and 2 bioactivity records.

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 (%): 39.706 Lower values reduce human off-target concern.
Human E-value: 1.44e-06
Gut microbiome similarity: 3.6% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 92.194 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 90.91 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) 0.909

Structure A0A0H3GVR8

Pocket Pocket 1

Druggability (FPocket) 0.373

Structure A0A0H3GVR8

Pocket Pocket 25

ColabFold model

P2Rank 0.87 · Pocket 1

FPocket 0.314 · Pocket 16

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 170 / 4744 genomes with a hit

Prevalence 3.6%

Metabolic context

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

This protein is not associated with the imported metabolic network for this genome.

Browse the genome's metabolic network

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MKVTLPEFERAGVLVVGDVMLDRYWYGPTSRISPEAPVPVVKVENIEERPGGAANVAMNIASLGATSRLVGLTGIDDAARALSQALANVNVKCDFVSVPTHPTITKLRVLSRNQQLIRLDFEEGFSGVDPQPMHERIQQALGSIGALVLSDYAKGALTSVQTMIRLAREAGVPVLIDPKGTDFERYRGATLLTPNLSEFEAVVGKCQDEAQIVERGMKLIAEFELSALLVTRSEQGMTLLQPGRPPLHMPTQAQEVYDVTGAGDTVIGVLAATLASGNTLEEACYFANAAAGVVVGKLGTSTVSPVELENAVRGRAETGFGVMSEEELKQAVAAARKRGEKVVMTNGVFDILHAGHVSYLANARKLGDRLIVAVNSDASTKRLKGETRPVNPLEQRMIVLGALEAVDWVVSFEEDTPQRLIAGILPDLLVKGGDYKPEQIAGSEEVWANGGEVLVLNFEDGCSTTNIIKKIQKDSDK

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

12 GO

Subcellular localization

Localization: Cytoplasmic

Gene Ontology (GO)

GO:0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.
GO:0016773 Catalysis of the transfer of a phosphorus-containing group from one compound (donor) to an alcohol group (acceptor).
GO:0016301 Catalysis of the transfer of a phosphate group, usually from ATP, to a substrate molecule.
GO:0005975 The chemical reactions and pathways involving carbohydrates, any of a group of organic compounds based of the general formula Cx(H2O)y.
GO:0016779 Catalysis of the transfer of a nucleotidyl group from one compound (donor) to another (acceptor).
GO:0009058 A cellular process consisting of the biochemical pathways by which a living organism synthesizes chemical substances. This typically represents the energy-requiring part of metabolism in which simpler substances are transformed into more complex ones.
GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
GO:0033785 Catalysis of the reaction: D-alpha,beta-D-heptose-7-phosphate + ATP = D-beta-D-heptose-1,7-bisphosphate + ADP.
GO:0033786 Catalysis of the reaction: D-beta-D-heptose-1-phosphate + ATP = ADP-D-glycero-D-manno-heptose.
GO:0097171 The chemical reactions and pathways resulting in the formation of ADP-L-glycero-beta-D-manno-heptose, an ADP-L-glycero-D-manno-heptose having beta-configuration at the anomeric centre of the heptose. ADP-L-glycero-beta-D-manno-heptose (also called ADP-L-beta-D-heptose or ADP-L-glycero-D-manno-heptose) is a nucleotide-sugar precursor of the inner core lipopolysaccharide (LPS) from D-glycero-beta-D-manno-heptose 7-phosphate.
GO:0009244 The chemical reactions and pathways resulting in the formation of the core region of bacterial lipopolysaccharides, which contains ten saccharide residues.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

26 records

Show feature table

Start	End	DB	Term	Name
13	305	Pfam	PF00294	pfkB family carbohydrate kinase
13	305	InterPro	IPR011611	Carbohydrate kinase PfkB
340	471	SUPERFAMILY	SSF52374	Nucleotidylyl transferase
51	74	ProSitePatterns	PS00583	pfkB family of carbohydrate kinases signature 1.
51	74	InterPro	IPR002173	Carbohydrate/purine kinase, PfkB, conserved site
2	309	FunFam	G3DSA:3.40.1190.20:FF:000002	Bifunctional protein HldE
4	474	Hamap	MF_01603	Bifunctional protein HldE [hldE].
4	474	InterPro	IPR023030	Bifunctional protein HldE
12	310	SUPERFAMILY	SSF53613	Ribokinase-like
12	310	InterPro	IPR029056	Ribokinase-like
320	477	Gene3D	G3DSA:3.40.50.620	HUPs
320	477	InterPro	IPR014729	Rossmann-like alpha/beta/alpha sandwich fold
2	309	Gene3D	G3DSA:3.40.1190.20	-
2	309	InterPro	IPR029056	Ribokinase-like
2	315	PANTHER	PTHR46969	BIFUNCTIONAL PROTEIN HLDE
345	435	Pfam	PF01467	Cytidylyltransferase-like
345	435	InterPro	IPR004821	Cytidyltransferase-like domain
332	473	NCBIfam	TIGR02199	D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase
332	473	InterPro	IPR011914	RfaE bifunctional protein, domain II
5	312	NCBIfam	TIGR02198	D-glycero-beta-D-manno-heptose-7-phosphate kinase
5	312	InterPro	IPR011913	RfaE bifunctional protein, domain I
320	477	FunFam	G3DSA:3.40.50.620:FF:000028	Bifunctional protein HldE
13	309	CDD	cd01172	RfaE_like
13	309	InterPro	IPR011913	RfaE bifunctional protein, domain I
342	408	NCBIfam	TIGR00125	cytidyltransferase-like domain
342	408	InterPro	IPR004821	Cytidyltransferase-like domain

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

0.909

Likely same site as FPocket 25 6.0 Å 16 shared residues 100% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.834

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Surrounding area

Pocket 3 P2Rank #3

0.066

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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 #25

0.373 Unusual size

Likely same site as P2Rank 1 6.0 Å 16 shared residues 100% of smaller site

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Surrounding area

Residue sets

UniProt: Active site:264-264

UniProt: Binding site:195-198

Binding pockets · P2Rank

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

Pocket 1 P2Rank #1

0.87

Likely same site as FPocket 16 6.4 Å 16 shared residues 84% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.831

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Surrounding area

Pocket 3 P2Rank #3

0.008

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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 #16

0.314 Unusual size

Likely same site as P2Rank 1 6.4 Å 16 shared residues 84% of smaller site

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Surrounding area

Pocket 2 FPocket #5

0.267 Unusual size

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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_A0A0H3GVR8	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_4017	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.

62 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 12 records from similar proteins

Structural ligands 10 0 loaded crystals

Measured bioactivity 2 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

ACP PDB via homolog 505.2 Da · LogP -1.52 · TPSA 269.9 Open detail RCSB PDB

ANP PDB via homolog Detail RCSB PDB

C2G PDB via homolog Detail RCSB PDB

CDC PDB via homolog Detail RCSB PDB

CHT 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
ACP RCSB PDB	6A8B	A0A3S7X0F5	505.2 Da LogP -1.52 TPSA 269.9	3 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
ANP RCSB PDB	4E84	B4EB35	506.2 Da LogP -2.06 TPSA 281.9	3 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
C2G RCSB PDB	1N1D	P27623	477.3 Da LogP -2.95 TPSA 253.3	2 viol.	✓ Clean	`C1=CN(C(=O)N=C1N)[C@H]2[C@@H]([C@@H]([C@H](O2)C…`
CDC RCSB PDB	4ZCS	Q8IEE9	488.3 Da LogP -2.23 TPSA 215.7	1 viol.	✓ Clean	`C[N+](C)(C)CCO[P@@](=O)([O-])O[P@@](=O)(O)OC[C@…`
CHT RCSB PDB	4ZCQ	Q8IEE9	104.2 Da LogP -0.32 TPSA 20.2	✓ Ro5	✓ Clean	`C[N+](C)(C)CCO`
GMZ RCSB PDB	4E84	B4EB35	370.1 Da LogP -3.63 TPSA 223.7	1 viol.	✓ Clean	`C([C@H]([C@@H]1[C@H]([C@@H]([C@@H]([C@@H](O1)OP…`
M7B RCSB PDB	4E84	B4EB35	290.2 Da LogP -3.74 TPSA 177.1	1 viol.	✓ Clean	`C([C@H]([C@@H]1[C@H]([C@@H]([C@@H]([C@@H](O1)O)…`
P33 RCSB PDB	4ZCS	Q8IEE9	326.4 Da LogP -0.93 TPSA 95.8	✓ Ro5	✓ Clean	`C(COCCOCCOCCOCCOCCOCCO)O`
PC RCSB PDB	4ZCR	Q8IEE9	184.2 Da LogP -0.20 TPSA 66.8	✓ Ro5	✓ Clean	`C[N+](C)(C)CCOP(=O)(O)O`
RIB RCSB PDB	6ILS	A1A6H3	150.1 Da LogP -2.58 TPSA 90.2	✓ Ro5	✓ Clean	`C([C@@H]1[C@H]([C@H]([C@H](O1)O)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
IHC ChEMBL	B4EB35	6.64 ~229.1 nM	462.3 Da LogP 4.53 TPSA 110.1	✓ Ro5	✓ Clean	`c1cc(c(c(c1)Cl)c2cnnc(n2)NCc3nc4cc(ccc4s3)OCC(=…`
IHA ChEMBL	B4EB35	6.09 ~812.8 nM	453.5 Da LogP 3.24 TPSA 128.6	✓ Ro5	✓ Clean	`COc1cccc(c1c2cnnc(n2)NCc3nc4cc(ccc4s3)OCC(=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
ZINC12501520 ZINC	1.000	458.5 Da LogP -0.88 TPSA 123.5	1 viol.	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC3874716 ZINC	1.000	414.5 Da LogP -0.90 TPSA 114.3	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC4283769 ZINC	1.000	238.3 Da LogP -0.96 TPSA 77.4	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCO`
ZINC4521548 ZINC	1.000	282.3 Da LogP -0.95 TPSA 86.6	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCO`
ZINC5178829 ZINC	1.000	326.4 Da LogP -0.93 TPSA 95.8	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCO`
ZINC5178830 ZINC	1.000	370.4 Da LogP -0.91 TPSA 105.1	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC219330894 ZINC	0.873	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)CP(=O)…`
ZINC101145080 ZINC	0.867	489.3 Da LogP -1.60 TPSA 212.9	1 viol.	✓ Clean	`C[N+](C)(C)CCO[P@@](=O)(O)O[P@@](=O)(O)OC[C@@H]…`
ZINC106404522 ZINC	0.867	489.3 Da LogP -1.60 TPSA 212.9	1 viol.	✓ Clean	`C[N+](C)(C)CCO[P@@](=O)(O)O[P@@](=O)(O)OC[C@@H]…`
ZINC12660526 ZINC	0.867	489.3 Da LogP -1.60 TPSA 212.9	1 viol.	✓ Clean	`C[N+](C)(C)CCO[P@@](=O)(O)O[P@@](=O)(O)OC[C@H]1…`
ZINC16696677 ZINC	0.867	489.3 Da LogP -1.60 TPSA 212.9	1 viol.	✓ Clean	`C[N+](C)(C)CCO[P@](=O)(O)O[P@](=O)(O)OC[C@@H]1O…`
ZINC215821427 ZINC	0.867	489.3 Da LogP -1.60 TPSA 212.9	1 viol.	✓ Clean	`C[N+](C)(C)CCO[P@@](=O)(O)O[P@@](=O)(O)OC[C@@H]…`
ZINC36382611 ZINC	0.867	489.3 Da LogP -1.60 TPSA 212.9	1 viol.	✓ Clean	`C[N+](C)(C)CCO[P@@](=O)(O)O[P@@](=O)(O)OC[C@H]1…`
ZINC5048329 ZINC	0.867	489.3 Da LogP -1.60 TPSA 212.9	1 viol.	✓ Clean	`C[N+](C)(C)CCO[P@@](=O)(O)O[P@](=O)(O)OC[C@H]1O…`
ZINC6507065 ZINC	0.867	489.3 Da LogP -1.60 TPSA 212.9	1 viol.	✓ Clean	`C[N+](C)(C)CCO[P@@](=O)(O)O[P@@](=O)(O)OC[C@H]1…`
ZINC9211548 ZINC	0.867	489.3 Da LogP -1.60 TPSA 212.9	1 viol.	✓ Clean	`C[N+](C)(C)CCO[P@](=O)(O)O[P@](=O)(O)OC[C@@H]1O…`
ZINC96023557 ZINC	0.867	489.3 Da LogP -1.60 TPSA 212.9	1 viol.	✓ Clean	`C[N+](C)(C)CCO[P@@](=O)(O)O[P@@](=O)(O)OC[C@H]1…`
ZINC113978818 ZINC	0.781	489.3 Da LogP -1.60 TPSA 212.9	1 viol.	✓ Clean	`C[N+](C)(C)CCO[P@@](=O)(OC[C@H]1O[C@@H](n2ccc(N…`
ZINC113978820 ZINC	0.781	489.3 Da LogP -1.60 TPSA 212.9	1 viol.	✓ Clean	`C[N+](C)(C)CCO[P@](=O)(OC[C@H]1O[C@@H](n2ccc(N)…`
ZINC256671528 ZINC	0.708	490.3 Da LogP -1.48 TPSA 207.1	1 viol.	✓ Clean	`C[N+](C)(C)CCO[P@](=O)(O)O[P@](=O)(O)OC[C@@H]1O…`
ZINC104864216 ZINC	0.705	403.2 Da LogP -2.33 TPSA 223.9	2 viol.	✓ Clean	`Nc1ccn([C@H]2O[C@@H](CO[P@](=O)(O)OP(=O)(O)O)[C…`
ZINC12504412 ZINC	0.705	403.2 Da LogP -2.33 TPSA 223.9	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(O)O)…`
ZINC12504413 ZINC	0.705	403.2 Da LogP -2.33 TPSA 223.9	2 viol.	✓ Clean	`Nc1ccn([C@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(O)O)[…`
ZINC12504414 ZINC	0.705	403.2 Da LogP -2.33 TPSA 223.9	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(O)O)[…`
ZINC13431045 ZINC	0.705	403.2 Da LogP -2.33 TPSA 223.9	2 viol.	✓ Clean	`Nc1ccn([C@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(O)O)[…`
ZINC13431047 ZINC	0.705	403.2 Da LogP -2.33 TPSA 223.9	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(O)O)…`
ZINC13548733 ZINC	0.705	403.2 Da LogP -2.33 TPSA 223.9	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(O)O)[…`
ZINC33913782 ZINC	0.705	403.2 Da LogP -2.33 TPSA 223.9	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(O)O)[…`
ZINC8215624 ZINC	0.705	403.2 Da LogP -2.33 TPSA 223.9	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(O)O)[…`
ZINC115086873 ZINC	0.688	209.2 Da LogP -1.08 TPSA 83.2	✓ Ro5	✓ Clean	`NOCCOCCOCCOCCO`
ZINC137432264 ZINC	0.688	457.6 Da LogP -0.91 TPSA 129.3	1 viol.	✓ Clean	`NCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC146143823 ZINC	0.688	237.3 Da LogP -1.00 TPSA 83.2	✓ Ro5	✓ Clean	`NCCOCCOCCOCCOCCO`
ZINC1542984442 ZINC	0.688	413.5 Da LogP -0.93 TPSA 120.1	✓ Ro5	✓ Clean	`NCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC1565503710 ZINC	0.688	254.3 Da LogP -0.03 TPSA 57.2	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCS`
ZINC1580161 ZINC	0.688	208.3 Da LogP -0.33 TPSA 57.2	✓ Ro5	✓ Clean	`COCCOCCOCCOCCO`
ZINC16052118 ZINC	0.688	340.4 Da LogP -0.28 TPSA 84.8	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCO`
ZINC16052257 ZINC	0.688	384.5 Da LogP -0.26 TPSA 94.1	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC1857792028 ZINC	0.688	430.6 Da LogP 0.04 TPSA 94.1	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCOCCS`
ZINC1857792057 ZINC	0.688	474.6 Da LogP 0.06 TPSA 103.3	1 viol.	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCS`
ZINC34317654 ZINC	0.688	472.6 Da LogP -0.23 TPSA 112.5	1 viol.	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC38917157 ZINC	0.688	210.3 Da LogP -0.04 TPSA 47.9	✓ Ro5	✓ Clean	`OCCOCCOCCOCCS`
ZINC44076059 ZINC	0.688	428.5 Da LogP -0.24 TPSA 103.3	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC5210101 ZINC	0.688	252.3 Da LogP -0.31 TPSA 66.4	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCO`
ZINC5650743 ZINC	0.688	222.3 Da LogP 0.07 TPSA 57.2	✓ Ro5	✓ Clean	`CCOCCOCCOCCOCCO`
ZINC5997860 ZINC	0.688	296.4 Da LogP -0.29 TPSA 75.6	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCO`
ZINC6403917 ZINC	0.688	354.4 Da LogP 0.11 TPSA 84.8	✓ Ro5	✓ Clean	`CCOCCOCCOCCOCCOCCOCCOCCO`
ZINC77271182 ZINC	0.688	281.3 Da LogP -0.98 TPSA 92.4	✓ Ro5	✓ Clean	`NCCOCCOCCOCCOCCOCCO`
ZINC8216134 ZINC	0.688	446.2 Da LogP -2.35 TPSA 238.9	2 viol.	✓ Clean	`NCCO[P@@](=O)(O)O[P@](=O)(O)OC[C@H]1O[C@@H](n2c…`
ZINC90741446 ZINC	0.688	386.5 Da LogP 0.02 TPSA 84.8	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCS`
ZINC90741447 ZINC	0.688	298.4 Da LogP -0.01 TPSA 66.4	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCS`

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 A0A0H3GVR8

Chemistry

ChEMBL IHC ChEMBL IHA