KpATCC43816 Protein target profile

lipopolysaccharide export system ATP-binding protein lptB

Accession: VK055_3866

Gene: AIK82416.1 lptB 3D evidence: Experimental + AlphaFold DB model + ColabFold model Metabolism Not in network UniProt A0A2X3II39

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Length 241

Pocket druggability (P2Rank · AlphaFold DB model) 0.243

Direct ligand evidence 0 66 total records

Functional annotation 0 EC 5 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

Experimental structure available At least one PDB experimental structure is loaded, not just a predicted model - stronger structural coverage than AlphaFold/ColabFold alone. Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Moderate predicted binding pocket FPocket selected-pocket score 0.49. This supports review but is not experimental validation. Structure available Experimental + AlphaFold DB model + ColabFold model 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 (%): 34.375 Lower values reduce human off-target concern.
Human E-value: 1.03e-15
Gut microbiome similarity: 26.4% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 96.68 Higher values support similarity to known essential genes.
DEG E-value: 6.26e-172 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 94.86 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) 0.243

Structure A0A2X3II39

Pocket Pocket 1

Druggability (FPocket) 0.495

Structure A0A2X3II39

Pocket Pocket 1

ColabFold model

P2Rank 0.197 · Pocket 1

FPocket 0.316 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 1254 / 4744 genomes with a hit

Prevalence 26.4%

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.

MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGYLPQEASIFRRLSVYDNLMAVLQIRDDLTSEQREDRAKELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPQQILEDEQVKRVYLGEDFRL

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

5 GO

Subcellular localization

Localization: Cytoplasmic

Gene Ontology (GO)

GO:0043190 A complex for the transport of metabolites into and out of the cell, typically comprised of four domains; two membrane-associated domains and two ATP-binding domains at the intracellular face of the membrane, that form a central pore through the plasma membrane. Each of the four core domains may be encoded as a separate polypeptide or the domains can be fused in any one of a number of ways into multidomain polypeptides. In Bacteria and Archaebacteria, ABC transporters also include substrate binding proteins to bind substrate external to the cytoplasm and deliver it to the transporter.
GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
GO:0016887 Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient.
GO:0055085 The process in which a solute is transported across a lipid bilayer, from one side of a membrane to the other.
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

20 records

Show feature table

Start	End	DB	Term	Name
20	166	Pfam	PF00005	ABC transporter
20	166	InterPro	IPR003439	ABC transporter-like, ATP-binding domain
3	241	NCBIfam	TIGR04406	LPS export ABC transporter ATP-binding protein
3	241	InterPro	IPR030921	LPS export ABC transporter, ATP-binding protein LptB
1	241	Gene3D	G3DSA:3.40.50.300	-
1	241	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
2	240	PANTHER	PTHR45772	CONSERVED COMPONENT OF ABC TRANSPORTER FOR NATURAL AMINO ACIDS-RELATED
1	241	FunFam	G3DSA:3.40.50.300:FF:000151	Lipopolysaccharide ABC transporter ATP-binding protein
4	237	SUPERFAMILY	SSF52540	P-loop containing nucleoside triphosphate hydrolases
4	237	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
138	152	ProSitePatterns	PS00211	ABC transporters family signature.
138	152	InterPro	IPR017871	ABC transporter-like, conserved site
4	237	ProSiteProfiles	PS50893	ATP-binding cassette, ABC transporter-type domain profile.
4	237	InterPro	IPR003439	ABC transporter-like, ATP-binding domain
4	236	CDD	cd03218	ABC_YhbG
4	236	InterPro	IPR030921	LPS export ABC transporter, ATP-binding protein LptB
28	231	SMART	SM00382	AAA_5
28	231	InterPro	IPR003593	AAA+ ATPase domain
215	239	Pfam	PF12399	Branched-chain amino acid ATP-binding cassette transporter
215	239	InterPro	IPR032823	Branched-chain amino acid ATP-binding cassette transporter, C-terminal

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 #4

0.267

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Surrounding area

Pocket 2 P2Rank #6

0.124

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Surrounding area

Pocket 3 P2Rank #7

0.118

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Surrounding area

Pocket 4 P2Rank #8

0.076

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Surrounding area

Pocket 5 P2Rank #13

0.049

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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

0.495

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Surrounding area

Pocket 2 FPocket #7

0.375

Likely same site as P2Rank 2 6.3 Å 5 shared residues 50% of smaller site

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Surrounding area

All structural evidence 1 experimental · 2 predicted

Structural evidence

1 + 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
PDB 7EFO	X-ray	—	A	—	PDBe RCSB PDBj File	Viewing
AlphaFold DB AF_A0A2X3II39	AlphaFold DB	—	—	full sequence	—	Loaded
ColabFold VK055_3866	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.

66 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 16 records from similar proteins

Structural ligands 16 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

AE3 PDB via homolog 134.2 Da · LogP 0.03 · TPSA 38.7 Open detail RCSB PDB

ANP PDB via homolog Detail RCSB PDB

AOV PDB via homolog Detail RCSB PDB

CZJ PDB via homolog Detail RCSB PDB

DCQ 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
AE3 RCSB PDB	6MJP	O30650	134.2 Da LogP 0.03 TPSA 38.7	✓ Ro5	✓ Clean	`CCOCCOCCO`
ANP RCSB PDB	6S8G	P0A9V4	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)…`
AOV RCSB PDB	6MHZ	P0A9V1	544.2 Da LogP -3.05 TPSA 299.4	3 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
CZJ RCSB PDB	6B8B	P0A9V1	586.6 Da LogP 3.32 TPSA 179.8	1 viol.	✓ Clean	`Cc1c(ccc2c1OC(=O)C(=C2O)NC(=O)C34CC5CC(C3)CC(C5…`
DCQ RCSB PDB	6S8N	P0A9V4	322.4 Da LogP 4.49 TPSA 52.6	✓ Ro5	Alert	`CCCCCCCCCCC1=C(C(=O)C(=C(C1=O)OC)OC)C`
JU7 RCSB PDB	6MJP	O30650	346.5 Da LogP 1.33 TPSA 99.4	✓ Ro5	✓ Clean	`C1CCC(CC1)CCCCCCO[C@H]2[C@@H]([C@H]([C@@H]([C@H…`
L0W RCSB PDB	6S8N	P0A9V4	1814.4 Da LogP 21.50 TPSA 394.5	4 viol.	✓ Clean	`CCCCCCCCCCCCCC(=O)O[C@H](CCCCCCCCCCC)CC(=O)O[C@…`
LMD RCSB PDB	6S8G	P0A9V4	538.7 Da LogP 0.33 TPSA 178.5	3 viol.	✓ Clean	`CCCCCCCCCCCCCCO[C@H]1[C@@H]([C@H]([C@@H]([C@H](…`
LMN RCSB PDB	6S8N	P0A9V4	1005.2 Da LogP -1.68 TPSA 357.1	3 viol.	✓ Clean	`CCCCCCCCCCC(CCCCCCCCCC)(CO[C@@H]1[C@@H]([C@@H](…`
LMT RCSB PDB	6S8N	P0A9V4	510.6 Da LogP -0.45 TPSA 178.5	3 viol.	✓ Clean	`CCCCCCCCCCCCO[C@H]1[C@@H]([C@H]([C@@H]([C@H](O1…`
LPP RCSB PDB	7CHA	Q9HVW1	648.9 Da LogP 10.51 TPSA 119.4	2 viol.	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OC[C@H](COP(=O)(O)O)OC(=O)C…`
MA4 RCSB PDB	6MJP	O30650	508.6 Da LogP -0.84 TPSA 178.5	3 viol.	✓ Clean	`C1CCC(CC1)CCCCCCO[C@H]2[C@@H]([C@H]([C@@H]([C@H…`
MMC RCSB PDB	1G9X	Q58663	215.6 Da LogP 0.58 TPSA 0.0	✓ Ro5	✓ Clean	`C[Hg+]`
NOV RCSB PDB	6B89	P0A9V1	612.6 Da LogP 3.63 TPSA 200.0	2 viol.	✓ Clean	`Cc1c(ccc2c1OC(=O)C(=C2O)NC(=O)c3ccc(c(c3)CC=C(C…`
TBU RCSB PDB	1GAJ	Q58663	74.1 Da LogP 0.78 TPSA 20.2	✓ Ro5	✓ Clean	`CC(C)(C)O`
VO4 RCSB PDB	7D0A	A0A086HZU3	114.9 Da LogP -3.69 TPSA 86.2	✓ Ro5	✓ Clean	`[O-][V](=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).

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
ZINC100053689 ZINC	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@H]…`
ZINC100053691 ZINC	1.000	496.6 Da LogP -0.84 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCCO[C@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@H…`
ZINC1501015302 ZINC	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@H…`
ZINC2039285652 ZINC	1.000	454.5 Da LogP -2.01 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCO[C@H]1O[C@H](CO)[C@H](O[C@@H]2O[C@H](C…`
ZINC2039285653 ZINC	1.000	454.5 Da LogP -2.01 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCO[C@H]1O[C@H](CO)[C@H](O[C@@H]2O[C@H](C…`
ZINC2039285654 ZINC	1.000	454.5 Da LogP -2.01 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCO[C@H]1O[C@H](CO)[C@H](O[C@@H]2O[C@H](C…`
ZINC2039285655 ZINC	1.000	454.5 Da LogP -2.01 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCO[C@H]1O[C@H](CO)[C@H](O[C@@H]2O[C@H](C…`
ZINC2053493146 ZINC	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@H]1O[C@H](CO)[C@H](O[C@@H]2O[C@H]…`
ZINC2053493147 ZINC	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@H]1O[C@H](CO)[C@H](O[C@@H]2O[C@H]…`
ZINC2053493148 ZINC	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@H]1O[C@H](CO)[C@H](O[C@@H]2O[C@H]…`
ZINC2053493149 ZINC	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@H]1O[C@H](CO)[C@H](O[C@@H]2O[C@H]…`
ZINC238809244 ZINC	1.000	510.6 Da LogP -0.45 TPSA 178.5	3 viol.	✓ Clean	`CCCCCCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C…`
ZINC238809245 ZINC	1.000	510.6 Da LogP -0.45 TPSA 178.5	3 viol.	✓ Clean	`CCCCCCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C…`
ZINC252695223 ZINC	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@H…`
ZINC252695224 ZINC	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@H…`
ZINC252695225 ZINC	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@H…`
ZINC252695226 ZINC	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@H…`
ZINC2575028 ZINC	1.000	322.4 Da LogP 4.49 TPSA 52.6	✓ Ro5	Alert	`CCCCCCCCCCC1=C(C)C(=O)C(OC)=C(OC)C1=O`
ZINC36178999 ZINC	1.000	424.5 Da LogP 4.27 TPSA 119.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@@H](COP(=O)(O)O)OC(=O)CCCCCCC`
ZINC36179002 ZINC	1.000	424.5 Da LogP 4.27 TPSA 119.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@H](COP(=O)(O)O)OC(=O)CCCCCCC`
ZINC5650743 ZINC	1.000	222.3 Da LogP 0.07 TPSA 57.2	✓ Ro5	✓ Clean	`CCOCCOCCOCCOCCO`
ZINC58649715 ZINC	1.000	496.6 Da LogP -0.84 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@…`
ZINC59978443 ZINC	1.000	454.5 Da LogP -2.01 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@H](…`
ZINC6403917 ZINC	1.000	354.4 Da LogP 0.11 TPSA 84.8	✓ Ro5	✓ Clean	`CCOCCOCCOCCOCCOCCOCCOCCO`
ZINC66157001 ZINC	1.000	468.5 Da LogP -1.62 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@H]…`
ZINC70669940 ZINC	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@@H]1O[C@@H](CO)[C@@H](O[C@H]2O[C@…`
ZINC70669941 ZINC	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@@H]1O[C@@H](CO)[C@@H](O[C@H]2O[C@…`
ZINC70669942 ZINC	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@@H]1O[C@@H](CO)[C@@H](O[C@H]2O[C@…`
ZINC70669943 ZINC	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@@H]1O[C@@H](CO)[C@@H](O[C@H]2O[C@…`
ZINC77311968 ZINC	1.000	454.5 Da LogP -2.01 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@@H]2O[C@H]…`
ZINC83433913 ZINC	1.000	426.5 Da LogP -2.79 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@H](CO…`
ZINC85482724 ZINC	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@H…`
ZINC86002923 ZINC	1.000	426.5 Da LogP -2.79 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCO[C@@H]1O[C@H](CO)[C@H](O[C@H]2O[C@H](CO)…`
ZINC5820131 ZINC	0.971	368.4 Da LogP 2.71 TPSA 119.4	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@@H](COP(=O)(O)O)OC(=O)CCCCC`
ZINC5820134 ZINC	0.971	368.4 Da LogP 2.71 TPSA 119.4	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@H](COP(=O)(O)O)OC(=O)CCCCC`
ZINC100050848 ZINC	0.811	376.5 Da LogP 2.50 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O)[C@H](…`
ZINC100056252 ZINC	0.811	334.5 Da LogP 1.33 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O)[C@H](O)[…`
ZINC100622854 ZINC	0.811	348.5 Da LogP 1.72 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCCCCCCO[C@H]1O[C@@H](CO)[C@@H](O)[C@@H](O…`
ZINC100622858 ZINC	0.811	348.5 Da LogP 1.72 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCCCCCCO[C@H]1O[C@@H](CO)[C@@H](O)[C@@H](O…`
ZINC100623040 ZINC	0.811	334.5 Da LogP 1.33 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCCCCCO[C@@H]1O[C@@H](CO)[C@@H](O)[C@@H](O…`
ZINC105807070 ZINC	0.811	292.4 Da LogP 0.16 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCCO[C@H]1O[C@H](CO)[C@H](O)[C@@H](O)[C@@H…`
ZINC118911494 ZINC	0.811	278.3 Da LogP -0.23 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCO[C@@H]1O[C@H](CO)[C@H](O)[C@@H](O)[C@@H…`
ZINC140958235 ZINC	0.811	348.5 Da LogP 1.72 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCCCCCCO[C@@H]1O[C@H](CO)[C@H](O)[C@@H](O)…`
ZINC48016017 ZINC	0.811	278.3 Da LogP -0.23 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O)[C@H](O)[C@H]…`
ZINC58538417 ZINC	0.811	320.4 Da LogP 0.94 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O)[C@H](O)[C…`
ZINC59206904 ZINC	0.811	292.4 Da LogP 0.16 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O)[C@H](O)[C@@…`
ZINC71788563 ZINC	0.811	292.4 Da LogP 0.16 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCCO[C@@H]1O[C@@H](CO)[C@@H](O)[C@H](O)[C@…`
ZINC85478989 ZINC	0.811	320.4 Da LogP 0.94 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCCCCO[C@H]1O[C@H](CO)[C@@H](O)[C@H](O)[C@…`
ZINC85590888 ZINC	0.811	320.4 Da LogP 0.94 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCCCCO[C@@H]1O[C@@H](CO)[C@@H](O)[C@@H](O)…`
ZINC94437834 ZINC	0.811	292.4 Da LogP 0.16 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCCO[C@H]1O[C@H](CO)[C@H](O)[C@H](O)[C@H]1O`

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 A0A2X3II39

Structure

PDB 7EFO