KpKP13 Protein target profile

DNA topoisomerase III

Accession: KP13_06748

Gene: AHE41852.1 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A1C8Y8K9

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Length 775

Pocket druggability (P2Rank · AlphaFold DB model) 0.936

Direct ligand evidence 0 53 total records

Functional annotation 1 EC 9 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

Moderate predicted binding pocket FPocket selected-pocket score 0.56. This supports review but is not experimental validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.94. Structure available AlphaFold DB model + ColabFold model Ligand evidence via structure/bioactivity 3 structural and 0 bioactivity records.

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 (%): 22.326 Lower values reduce human off-target concern.
Human E-value: 3.55e-10
Gut microbiome similarity: 0.0% 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: 92.99 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) 0.936

Structure A0A1C8Y8K9

Pocket Pocket 1

Druggability (FPocket) 0.564

Structure A0A1C8Y8K9

Pocket Pocket 35

ColabFold model

P2Rank 0.918 · Pocket 1

FPocket 0.467 · Pocket 43

Core conservation Accessory gene

Roary accessory

CoreCruncher accessory

Gut microbiome 2 / 4744 genomes with a hit

Prevalence 0.0%

Sequence

Primary amino-acid sequence viewer.

MRLFIAEKPSLAKAIFEGLGGNPNTEKKNGYFEHGSDVVTWCYGHMLELYDPEDYDEKYSNWRFSDLPIKSVYPPQYKIKPESEAQTRIILSLIDKADNIVHAGDPDEEGCLLVDEILGYAKNTKSVYRLLVRDLNLAPVQKALTDLQPNDKFRGMTLSALARSLCDQGFGYNMTRGCTLKGREKGYDGVLNVGRVQSAVLGLVNMRTLANQNHTESFYYDVFASLLMNGHLIKAKYQTTDDDQIDEKKRLISEAQAAHIAGRVTGKDAVVTIATTKPENTKPPLPLNLSTLQQLCAKRFGYSAKDTLDVMQGLYETHKLLTYPRSDNRYLSDEHYYQAGDIATAIAATVPELASAIADMDKSQKHKAFNASKIEAHHAIIPTTKSGAGIQLNEKERNVYNLVSVYFIGLFYPDAIRNKTKIHFDIKGDTFTATQSVLVQKGWEALGKDNDDEDETEDAGTDGFDLSSLKFNDSGLCESADVDKKKTNPPRYFTASTLLAAMTSAAKFIDDPALRKALEAKDEGSEDRGSIGTEATRAGILEKLAANTGLISIEKEKGYSELVWKTTKQGQEFCAALPPEITKPDISALWAEKQSQIKAGELTVEEFIKENDEYVQGLIDELERNGVSISSNATPCPVCNNGFLRKRKGQNGFFWGCSCYPECKTTFPDKDGKPDMEAKSRSEGSMSRLEAPCPSCSKEIIIRPKGFFCSGCEFKIWSEVSGKKLTQNQVETLIKKGKTGEIKGFTSNKTGKKFDAAIVLQDKATGKLGFQFSKK

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 9 GO

Subcellular localization

Localization: Cytoplasmic

Enzyme Commission (EC)

5.6.2.1

Gene Ontology (GO)

GO:0006265 The process in which a transformation is induced in the topological structure of a double-stranded DNA helix, resulting in a change in linking number.
GO:0003916 Catalysis of the transient cleavage and passage of individual DNA strands or double helices through one another, resulting a topological transformation in double-stranded DNA.
GO:0003917 Catalysis of a DNA topological transformation by transiently cleaving one DNA strand at a time to allow passage of another strand; changes the linking number by +1 per catalytic cycle.
GO:0005694 A structure composed of a very long molecule of DNA and associated proteins (e.g. histones) that carries hereditary information.
GO:0003677 Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
GO:0043597 The Y-shaped region of a cytoplasmic replicating DNA molecule, resulting from the separation of the DNA strands and in which the synthesis of new strands takes place. Also includes associated protein complexes.
GO:0008270 Binding to a zinc ion (Zn).
GO:0006310 Any process in which a new genotype is formed by reassortment of genes resulting in gene combinations different from those that were present in the parents. In eukaryotes genetic recombination can occur by chromosome assortment, intrachromosomal recombination, or nonreciprocal interchromosomal recombination. Interchromosomal recombination occurs by crossing over. In bacteria it may occur by genetic transformation, conjugation, transduction, or F-duction.
GO:0006281 The process of restoring DNA after damage. Genomes are subject to damage by chemical and physical agents in the environment (e.g. UV and ionizing radiations, chemical mutagens, fungal and bacterial toxins, etc.) and by free radicals or alkylating agents endogenously generated in metabolism. DNA is also damaged because of errors during its replication. A variety of different DNA repair pathways have been reported that include direct reversal, base excision repair, nucleotide excision repair, photoreactivation, bypass, double-strand break repair pathway, and mismatch repair pathway.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

45 records

Show feature table

Start	End	DB	Term	Name
126	221	SMART	SM00436	topIban2
126	221	InterPro	IPR003601	DNA topoisomerase, type IA, domain 2
275	574	SMART	SM00437	topIaneu2
275	574	InterPro	IPR003602	DNA topoisomerase, type IA, DNA-binding domain
285	413	Gene3D	G3DSA:1.10.290.10	Topoisomerase I, domain 4
285	413	InterPro	IPR013826	DNA topoisomerase, type IA, central region, subdomain 3
1	623	SUPERFAMILY	SSF56712	Prokaryotic type I DNA topoisomerase
1	623	InterPro	IPR023405	DNA topoisomerase, type IA, core domain
399	415	PRINTS	PR00417	Prokaryotic DNA topoisomerase I signature
399	415	InterPro	IPR013497	DNA topoisomerase, type IA, central
100	113	PRINTS	PR00417	Prokaryotic DNA topoisomerase I signature
100	113	InterPro	IPR013497	DNA topoisomerase, type IA, central
530	544	PRINTS	PR00417	Prokaryotic DNA topoisomerase I signature
530	544	InterPro	IPR013497	DNA topoisomerase, type IA, central
318	327	PRINTS	PR00417	Prokaryotic DNA topoisomerase I signature
318	327	InterPro	IPR013497	DNA topoisomerase, type IA, central
191	209	PRINTS	PR00417	Prokaryotic DNA topoisomerase I signature
191	209	InterPro	IPR013497	DNA topoisomerase, type IA, central
2	727	PANTHER	PTHR11390	PROKARYOTIC DNA TOPOISOMERASE
2	727	InterPro	IPR000380	DNA topoisomerase, type IA
1	666	NCBIfam	TIGR01056	DNA topoisomerase III
1	666	InterPro	IPR005738	DNA topoisomerase III
1	126	SMART	SM00493	toprim5
1	126	InterPro	IPR006171	TOPRIM domain
636	671	Pfam	PF01396	Topoisomerase DNA binding C4 zinc finger
636	671	InterPro	IPR013498	DNA topoisomerase, type IA, zn finger
160	608	Gene3D	G3DSA:1.10.460.10	Topoisomerase I, domain 2
160	608	InterPro	IPR013824	DNA topoisomerase, type IA, central region, subdomain 1
312	327	ProSitePatterns	PS00396	Prokaryotic DNA topoisomerase I active site.
312	327	InterPro	IPR023406	DNA topoisomerase, type IA, active site
156	609	Pfam	PF01131	DNA topoisomerase
156	609	InterPro	IPR013497	DNA topoisomerase, type IA, central
1	147	CDD	cd03362	TOPRIM_TopoIA_TopoIII
1	147	InterPro	IPR034144	DNA topoisomerase 3-like, TOPRIM domain
633	668	SUPERFAMILY	SSF57783	Zinc beta-ribbon
623	671	Gene3D	G3DSA:3.30.65.10	Bacterial Topoisomerase I, domain 1
3	129	Pfam	PF01751	Toprim domain
3	129	InterPro	IPR006171	TOPRIM domain
1	154	Gene3D	G3DSA:3.40.50.140	-
215	490	Gene3D	G3DSA:2.70.20.10	Topoisomerase I, domain 3
215	490	InterPro	IPR013825	DNA topoisomerase, type IA, central region, subdomain 2
711	772	Pfam	PF13342	C-terminal repeat of topoisomerase
711	772	InterPro	IPR025589	Topoisomerase C-terminal repeat
1	136	ProSiteProfiles	PS50880	Toprim domain profile.
1	136	InterPro	IPR006171	TOPRIM 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

0.936

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Surrounding area

Pocket 2 P2Rank #2

0.729

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Surrounding area

Pocket 3 P2Rank #3

0.305

Likely same site as FPocket 35 1.8 Å 14 shared residues 93% of smaller site

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Surrounding area

Pocket 4 P2Rank #4

0.187

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Surrounding area

Pocket 5 P2Rank #5

0.09

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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 #35

0.564

Likely same site as P2Rank 3 1.8 Å 14 shared residues 93% of smaller site

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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

0.918

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Surrounding area

Pocket 2 P2Rank #2

0.454

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Surrounding area

Pocket 3 P2Rank #3

0.359

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Surrounding area

Pocket 4 P2Rank #4

0.085

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Surrounding area

Pocket 5 P2Rank #5

0.081

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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_A0A1C8Y8K9	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_06748	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.

53 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 3 records from similar proteins

Structural ligands 3 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

A3P PDB via homolog 427.2 Da · LogP -1.75 · TPSA 232.6 Open detail RCSB PDB

T3P PDB via homolog Detail RCSB PDB

THP PDB via homolog Detail RCSB PDB

ZINC12501123 ZINC proposed compound · Tanimoto 1.000 Detail ZINC

ZINC4228234 ZINC proposed compound · Tanimoto 1.000 Detail ZINC

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
A3P RCSB PDB	1CY0	P06612	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
T3P RCSB PDB	1CY8	P06612	322.2 Da LogP -1.40 TPSA 151.1	✓ Ro5	✓ Clean	`CC1=CN(C(=O)NC1=O)[C@H]2C[C@@H]([C@H](O2)CO)OP(…`
THP RCSB PDB	1CY1	P06612	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)COP(=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
ZINC12501123 ZINC	1.000	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](…`
ZINC4228234 ZINC	1.000	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](…`
ZINC6521315 ZINC	1.000	322.2 Da LogP -1.40 TPSA 151.1	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@H](OP(=O)(O)O)[C@@H](CO)O2)c(=O…`
ZINC79671662 ZINC	1.000	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@H](O…`
ZINC79671663 ZINC	1.000	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@H](O…`
ZINC3871401 ZINC	0.887	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@@H](…`
ZINC3871402 ZINC	0.887	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@@H]…`
ZINC3871403 ZINC	0.887	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@@H](…`
ZINC3871404 ZINC	0.887	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@@H]…`
ZINC4096223 ZINC	0.887	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](…`
ZINC12958381 ZINC	0.846	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO)[C@@H](OP(=O)(O)…`
ZINC13546985 ZINC	0.846	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO)[C@H](OP(=O)(O)O…`
ZINC1631259 ZINC	0.846	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO)[C@@H](OP(=O)(O)…`
ZINC79090744 ZINC	0.846	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO)[C@H](OP(=O)(O)O…`
ZINC13518964 ZINC	0.827	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@H](…`
ZINC1532515 ZINC	0.827	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@H](O…`
ZINC1571045 ZINC	0.827	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@@H]…`
ZINC1842158 ZINC	0.827	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@H](O…`
ZINC2046931 ZINC	0.827	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@H](…`
ZINC2126310 ZINC	0.827	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](…`
ZINC3201891 ZINC	0.827	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@@H]…`
ZINC3201893 ZINC	0.827	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@@H](…`
ZINC3830180 ZINC	0.827	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@@H](…`
ZINC3860156 ZINC	0.827	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](…`
ZINC3977897 ZINC	0.827	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](COP(=O)(O)O)[C@@H](O…`
ZINC4806442 ZINC	0.827	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@H](O…`
ZINC8613167 ZINC	0.827	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@H](O…`
ZINC11422512 ZINC	0.820	402.2 Da LogP -1.28 TPSA 197.6	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@H](OP(=O)(O)O)[C@@H](COP(=O)(O)…`
ZINC13424932 ZINC	0.750	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO)[C@@H](O)[C@@H]1…`
ZINC13424933 ZINC	0.750	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](CO)[C@@H](O)[C@@H]1O…`
ZINC2036187 ZINC	0.750	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO)[C@H](O)[C@H]1OP…`
ZINC3861741 ZINC	0.750	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO)[C@@H](O)[C@H]1O…`
ZINC44960119 ZINC	0.750	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO)[C@H](O)[C@@H]1O…`
ZINC4513863 ZINC	0.750	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO)[C@@H](O)[C@@H]1…`
ZINC4513866 ZINC	0.750	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO)[C@@H](O)[C@@H]…`
ZINC14766830 ZINC	0.725	284.3 Da LogP -0.94 TPSA 110.6	✓ Ro5	✓ Clean	`CC(=O)O[C@@H]1C[C@@H](n2cc(C)c(=O)[nH]c2=O)O[C@…`
ZINC14766832 ZINC	0.725	284.3 Da LogP -0.94 TPSA 110.6	✓ Ro5	✓ Clean	`CC(=O)O[C@@H]1C[C@H](n2cc(C)c(=O)[nH]c2=O)O[C@@…`
ZINC2516145 ZINC	0.725	284.3 Da LogP -0.94 TPSA 110.6	✓ Ro5	✓ Clean	`CC(=O)O[C@@H]1C[C@@H](n2cc(C)c(=O)[nH]c2=O)O[C@…`
ZINC5119363 ZINC	0.725	284.3 Da LogP -0.94 TPSA 110.6	✓ Ro5	✓ Clean	`CC(=O)O[C@H]1C[C@@H](n2cc(C)c(=O)[nH]c2=O)O[C@H…`
ZINC5119364 ZINC	0.725	284.3 Da LogP -0.94 TPSA 110.6	✓ Ro5	✓ Clean	`CC(=O)O[C@H]1C[C@H](n2cc(C)c(=O)[nH]c2=O)O[C@H]…`
ZINC5119365 ZINC	0.725	284.3 Da LogP -0.94 TPSA 110.6	✓ Ro5	✓ Clean	`CC(=O)O[C@@H]1C[C@H](n2cc(C)c(=O)[nH]c2=O)O[C@H…`
ZINC6521309 ZINC	0.725	284.3 Da LogP -0.94 TPSA 110.6	✓ Ro5	✓ Clean	`CC(=O)O[C@H]1C[C@H](n2cc(C)c(=O)[nH]c2=O)O[C@@H…`
ZINC1842580 ZINC	0.723	242.2 Da LogP -1.51 TPSA 104.5	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@H](O)[C@H](CO)O2)c(=O)[nH]c1=O`
ZINC2159 ZINC	0.723	242.2 Da LogP -1.51 TPSA 104.5	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@@H](O)[C@H](CO)O2)c(=O)[nH]c1=O`
ZINC2545102 ZINC	0.723	242.2 Da LogP -1.51 TPSA 104.5	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@@H](O)[C@H](CO)O2)c(=O)[nH]c1=O`
ZINC25672 ZINC	0.723	242.2 Da LogP -1.51 TPSA 104.5	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@H](O)[C@@H](CO)O2)c(=O)[nH]c1=O`
ZINC2572653 ZINC	0.723	242.2 Da LogP -1.51 TPSA 104.5	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@@H](O)[C@@H](CO)O2)c(=O)[nH]c1…`
ZINC3831529 ZINC	0.723	242.2 Da LogP -1.51 TPSA 104.5	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@H](O)[C@H](CO)O2)c(=O)[nH]c1=O`
ZINC5765078 ZINC	0.723	242.2 Da LogP -1.51 TPSA 104.5	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@@H](O)[C@@H](CO)O2)c(=O)[nH]c1=O`
ZINC6072455 ZINC	0.723	242.2 Da LogP -1.51 TPSA 104.5	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@H](O)[C@@H](CO)O2)c(=O)[nH]c1=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.

Sequence

UniProt A0A1C8Y8K9